ID   FAS_HUMAN               Reviewed;        2511 AA.
AC   P49327; Q13479; Q16702; Q4LE83; Q6P4U5; Q6SS02; Q969R1; Q96C68; Q96IT0;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 3.
DT   02-OCT-2024, entry version 246.
DE   RecName: Full=Fatty acid synthase;
DE            EC=2.3.1.85 {ECO:0000269|PubMed:16215233, ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
DE   AltName: Full=Type I fatty acid synthase;
DE   Includes:
DE     RecName: Full=[Acyl-carrier-protein] S-acetyltransferase;
DE              EC=2.3.1.38 {ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
DE   Includes:
DE     RecName: Full=[Acyl-carrier-protein] S-malonyltransferase;
DE              EC=2.3.1.39 {ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
DE   Includes:
DE     RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase;
DE              EC=2.3.1.41 {ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
DE   Includes:
DE     RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase;
DE              EC=1.1.1.100 {ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
DE   Includes:
DE     RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase;
DE              EC=4.2.1.59 {ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
DE   Includes:
DE     RecName: Full=Enoyl-[acyl-carrier-protein] reductase;
DE              EC=1.3.1.39 {ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
DE   Includes:
DE     RecName: Full=Acyl-[acyl-carrier-protein] hydrolase;
DE              EC=3.1.2.14 {ECO:0000269|PubMed:15507492, ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
GN   Name=FASN; Synonyms=FAS;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, PHOSPHOPANTETHEINYLATION AT SER-2156, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=7567999; DOI=10.1073/pnas.92.19.8695;
RA   Jayakumar A., Tai M.-H., Huang W.-Y., Al-Feel W., Hsu M., Abu-Elheiga L.,
RA   Chirala S.S., Wakil S.J.;
RT   "Human fatty acid synthase: properties and molecular cloning.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:8695-8699(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Hennigar R.A., Jenner K.H., Heine H.S., Kayler A.E., Wood F.D.,
RA   Kuhajda F.P., Pasternack G.R.;
RT   "Molecular cloning of tumor-associated human fatty acid synthase.";
RL   Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Mao J., Wakil S.J.;
RT   "Recharacterization of the human fatty acid synthase (FAS) gene.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RA   Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R.,
RA   Okazaki N., Koga H., Nagase T., Ohara O.;
RT   "Preparation of a set of expression-ready clones of mammalian long cDNAs
RT   encoding large proteins by the ORF trap cloning method.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 1-12; 647-666; 791-802; 1242-1255; 1338-1349 AND
RP   2126-2138, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RA   Bienvenut W.V.;
RL   Submitted (JUL-2005) to UniProtKB.
RN   [8]
RP   PROTEIN SEQUENCE OF 753-758 AND 1285-1297.
RX   PubMed=8022791; DOI=10.1073/pnas.91.14.6379;
RA   Kuhajda F.P., Jenner K., Wood F.D., Hennigar R.A., Jacobs L.B., Dick J.D.,
RA   Pasternack G.R.;
RT   "Fatty acid synthesis: a potential selective target for antineoplastic
RT   therapy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:6379-6383(1994).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2047-2511, AND TISSUE SPECIFICITY.
RX   PubMed=7595075;
RA   Semenkovich C.F., Coleman T., Fiedorek F.T. Jr.;
RT   "Human fatty acid synthase mRNA: tissue distribution, genetic mapping, and
RT   kinetics of decay after glucose deprivation.";
RL   J. Lipid Res. 36:1507-1521(1995).
RN   [10]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=8962082; DOI=10.1073/pnas.93.25.14509;
RA   Jayakumar A., Huang W.Y., Raetz B., Chirala S.S., Wakil S.J.;
RT   "Cloning and expression of the multifunctional human fatty acid synthase
RT   and its subdomains in Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:14509-14514(1996).
RN   [11]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=9356448; DOI=10.1073/pnas.94.23.12326;
RA   Jayakumar A., Chirala S.S., Wakil S.J.;
RT   "Human fatty acid synthase: assembling recombinant halves of the fatty acid
RT   synthase subunit protein reconstitutes enzyme activity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:12326-12330(1997).
RN   [12]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=16215233; DOI=10.1074/jbc.m507082200;
RA   Carlisle-Moore L., Gordon C.R., Machutta C.A., Miller W.T., Tonge P.J.;
RT   "Substrate recognition by the human fatty-acid synthase.";
RL   J. Biol. Chem. 280:42612-42618(2005).
RN   [13]
RP   FUNCTION, AND ACTIVITY REGULATION.
RX   PubMed=16969344; DOI=10.1038/sj.bjc.6603350;
RA   Zhao W., Kridel S., Thorburn A., Kooshki M., Little J., Hebbar S.,
RA   Robbins M.;
RT   "Fatty acid synthase: a novel target for antiglioma therapy.";
RL   Br. J. Cancer 95:869-878(2006).
RN   [14]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND S-NITROSYLATION AT
RP   CYS-1471 AND CYS-2091.
RX   PubMed=26851298; DOI=10.1194/jlr.m065805;
RA   Choi M.S., Jung J.Y., Kim H.J., Ham M.R., Lee T.R., Shin D.W.;
RT   "S-nitrosylation of fatty acid synthase regulates its activity through
RT   dimerization.";
RL   J. Lipid Res. 57:607-615(2016).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Lymphoblast;
RX   PubMed=14654843; DOI=10.1038/nature02166;
RA   Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT   "Proteomic characterization of the human centrosome by protein correlation
RT   profiling.";
RL   Nature 426:570-574(2003).
RN   [16]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Melanoma;
RX   PubMed=17081065; DOI=10.1021/pr060363j;
RA   Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA   Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA   Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT   "Proteomic and bioinformatic characterization of the biogenesis and
RT   function of melanosomes.";
RL   J. Proteome Res. 5:3135-3144(2006).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2198 AND THR-2204, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-2198; THR-2204 AND
RP   SER-2236, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [19]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2204, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [21]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-298; LYS-436; LYS-528;
RP   LYS-673; LYS-1704; LYS-1771; LYS-1847 AND LYS-1995, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [22]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [23]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [24]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [25]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-207; SER-1411;
RP   SER-1584; SER-2198; THR-2204 AND THR-2215, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [26]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1174; SER-1411; SER-2198;
RP   THR-2204 AND THR-2215, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [27]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2449, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA   Impens F., Radoshevich L., Cossart P., Ribet D.;
RT   "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT   external stimuli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN   [28]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [29]
RP   FUNCTION (MICROBIAL INFECTION).
RX   PubMed=34320401; DOI=10.1016/j.celrep.2021.109479;
RA   Williams C.G., Jureka A.S., Silvas J.A., Nicolini A.M., Chvatal S.A.,
RA   Carlson-Stevermer J., Oki J., Holden K., Basler C.F.;
RT   "Inhibitors of VPS34 and fatty-acid metabolism suppress SARS-CoV-2
RT   replication.";
RL   Cell Rep. 36:109479-109479(2021).
RN   [30]
RP   3D-STRUCTURE MODELING, AND STRUCTURE BY ELECTRON MICROSCOPY.
RX   PubMed=11756679; DOI=10.1073/pnas.012589499;
RA   Brink J., Ludtke S.J., Yang C.Y., Gu Z.-W., Wakil S.J., Chiu W.;
RT   "Quaternary structure of human fatty acid synthase by electron
RT   cryomicroscopy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:138-143(2002).
RN   [31]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2218-2502, AND CATALYTIC ACTIVITY.
RX   PubMed=15507492; DOI=10.1073/pnas.0406901101;
RA   Chakravarty B., Gu Z., Chirala S.S., Wakil S.J., Quiocho F.A.;
RT   "Human fatty acid synthase: structure and substrate selectivity of the
RT   thioesterase domain.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:15567-15572(2004).
RN   [32]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2119-2207 IN COMPLEX WITH AASDHPPT
RP   AND COENZYME A.
RX   PubMed=18022563; DOI=10.1016/j.chembiol.2007.10.013;
RA   Bunkoczi G., Pasta S., Joshi A., Wu X., Kavanagh K.L., Smith S.,
RA   Oppermann U.;
RT   "Mechanism and substrate recognition of human holo ACP synthase.";
RL   Chem. Biol. 14:1243-1253(2007).
RN   [33]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2200-2511 IN COMPLEX WITH
RP   ORLISTAT, AND ACTIVE SITE FOR THIOESTERASE ACTIVITY.
RX   PubMed=17618296; DOI=10.1038/nsmb1265;
RA   Pemble C.W. IV, Johnson L.C., Kridel S.J., Lowther W.T.;
RT   "Crystal structure of the thioesterase domain of human fatty acid synthase
RT   inhibited by Orlistat.";
RL   Nat. Struct. Mol. Biol. 14:704-709(2007).
RN   [34]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 422-831 IN COMPLEX WITH
RP   MALONYL-COENZYME A.
RG   Structural genomics consortium (SGC);
RT   "Structure of the MAT domain of human FAS with malonyl-CoA.";
RL   Submitted (FEB-2009) to the PDB data bank.
RN   [35] {ECO:0007744|PDB:2JFD}
RP   X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 422-823.
RX   PubMed=19549604; DOI=10.1016/j.chembiol.2009.04.011;
RA   Bunkoczi G., Misquitta S., Wu X., Lee W.H., Rojkova A., Kochan G.,
RA   Kavanagh K.L., Oppermann U., Smith S.;
RT   "Structural basis for different specificities of acyltransferases
RT   associated with the human cytosolic and mitochondrial fatty acid
RT   synthases.";
RL   Chem. Biol. 16:667-675(2009).
RN   [36]
RP   VARIANT HIS-477.
RX   PubMed=28472301; DOI=10.1093/hmg/ddx175;
RA   Pinggera A., Mackenroth L., Rump A., Schallner J., Beleggia F., Wollnik B.,
RA   Striessnig J.;
RT   "New gain-of-function mutation shows CACNA1D as recurrently mutated gene in
RT   autism spectrum disorders and epilepsy.";
RL   Hum. Mol. Genet. 26:2923-2932(2017).
CC   -!- FUNCTION: Fatty acid synthetase is a multifunctional enzyme that
CC       catalyzes the de novo biosynthesis of long-chain saturated fatty acids
CC       starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This
CC       multifunctional protein contains 7 catalytic activities and a site for
CC       the binding of the prosthetic group 4'-phosphopantetheine of the acyl
CC       carrier protein ([ACP]) domain. {ECO:0000269|PubMed:16215233,
CC       ECO:0000269|PubMed:16969344, ECO:0000269|PubMed:26851298,
CC       ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC       ECO:0000269|PubMed:9356448}.
CC   -!- FUNCTION: (Microbial infection) Fatty acid synthetase activity is
CC       required for SARS coronavirus-2/SARS-CoV-2 replication.
CC       {ECO:0000269|PubMed:34320401}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + n malonyl-CoA + 2n NADPH + 2n H(+) = a long-chain
CC         fatty acid + (n+1) CoA + n CO2 + 2n NADP(+).; EC=2.3.1.85;
CC         Evidence={ECO:0000269|PubMed:16215233, ECO:0000269|PubMed:26851298,
CC         ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + holo-[ACP] = acetyl-[ACP] + CoA;
CC         Xref=Rhea:RHEA:41788, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78446; EC=2.3.1.38;
CC         Evidence={ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999,
CC         ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41789;
CC         Evidence={ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999,
CC         ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC         Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449; EC=2.3.1.39;
CC         Evidence={ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999,
CC         ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41793;
CC         Evidence={ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999,
CC         ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
CC         + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC         EC=2.3.1.41; Evidence={ECO:0000269|PubMed:26851298,
CC         ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837;
CC         Evidence={ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999,
CC         ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC         + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC         COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC         Evidence={ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999,
CC         ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17399;
CC         Evidence={ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999,
CC         ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;
CC         Evidence={ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999,
CC         ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13098;
CC         Evidence={ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999,
CC         ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2,3-saturated acyl-[ACP] + NADP(+) = a (2E)-enoyl-[ACP] +
CC         H(+) + NADPH; Xref=Rhea:RHEA:22564, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC         COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.39;
CC         Evidence={ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999,
CC         ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22566;
CC         Evidence={ECO:0000269|PubMed:26851298, ECO:0000269|PubMed:7567999,
CC         ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + hexadecanoyl-[ACP] = H(+) + hexadecanoate + holo-[ACP];
CC         Xref=Rhea:RHEA:41932, Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78483; EC=3.1.2.14;
CC         Evidence={ECO:0000269|PubMed:15507492, ECO:0000269|PubMed:7567999,
CC         ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41933;
CC         Evidence={ECO:0000269|PubMed:15507492, ECO:0000269|PubMed:7567999,
CC         ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] +
CC         CO2 + holo-[ACP]; Xref=Rhea:RHEA:41800, Rhea:RHEA-COMP:9621,
CC         Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78446, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41801;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxobutanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxybutanoyl-
CC         [ACP] + NADP(+); Xref=Rhea:RHEA:41804, Rhea:RHEA-COMP:9625,
CC         Rhea:RHEA-COMP:9626, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78450, ChEBI:CHEBI:78451;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41805;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxybutanoyl-[ACP] = (2E)-butenoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:41808, Rhea:RHEA-COMP:9626, Rhea:RHEA-COMP:9627,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78451, ChEBI:CHEBI:78453;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41809;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-butenoyl-[ACP] + H(+) + NADPH = butanoyl-[ACP] + NADP(+);
CC         Xref=Rhea:RHEA:41812, Rhea:RHEA-COMP:9627, Rhea:RHEA-COMP:9628,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78453, ChEBI:CHEBI:78454;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41813;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=butanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxohexanoyl-[ACP] +
CC         CO2 + holo-[ACP]; Xref=Rhea:RHEA:41820, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9628, Rhea:RHEA-COMP:9629, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78454, ChEBI:CHEBI:78456;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41821;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxohexanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyhexanoyl-
CC         [ACP] + NADP(+); Xref=Rhea:RHEA:41824, Rhea:RHEA-COMP:9629,
CC         Rhea:RHEA-COMP:9630, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78456, ChEBI:CHEBI:78457;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41825;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxyhexanoyl-[ACP] = (2E)-hexenoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:41828, Rhea:RHEA-COMP:9630, Rhea:RHEA-COMP:9631,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78457, ChEBI:CHEBI:78458;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41829;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-hexenoyl-[ACP] + H(+) + NADPH = hexanoyl-[ACP] + NADP(+);
CC         Xref=Rhea:RHEA:41832, Rhea:RHEA-COMP:9631, Rhea:RHEA-COMP:9632,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78458, ChEBI:CHEBI:78459;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41833;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hexanoyl-[ACP] + malonyl-[ACP] = 3-oxooctanoyl-[ACP] +
CC         CO2 + holo-[ACP]; Xref=Rhea:RHEA:41836, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9632, Rhea:RHEA-COMP:9633, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78459, ChEBI:CHEBI:78460;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41837;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxooctanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyoctanoyl-
CC         [ACP] + NADP(+); Xref=Rhea:RHEA:41840, Rhea:RHEA-COMP:9633,
CC         Rhea:RHEA-COMP:9634, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78460, ChEBI:CHEBI:78461;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41841;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxyoctanoyl-[ACP] = (2E)-octenoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:41844, Rhea:RHEA-COMP:9634, Rhea:RHEA-COMP:9635,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78461, ChEBI:CHEBI:78462;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41845;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-octenoyl-[ACP] + H(+) + NADPH = NADP(+) + octanoyl-[ACP];
CC         Xref=Rhea:RHEA:41848, Rhea:RHEA-COMP:9635, Rhea:RHEA-COMP:9636,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78462, ChEBI:CHEBI:78463;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41849;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + malonyl-[ACP] + octanoyl-[ACP] = 3-oxodecanoyl-[ACP] +
CC         CO2 + holo-[ACP]; Xref=Rhea:RHEA:41852, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9637, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78463, ChEBI:CHEBI:78464;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41853;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxodecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxydecanoyl-
CC         [ACP] + NADP(+); Xref=Rhea:RHEA:41856, Rhea:RHEA-COMP:9637,
CC         Rhea:RHEA-COMP:9638, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78464, ChEBI:CHEBI:78466;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41857;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41861;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-decenoyl-[ACP] + H(+) + NADPH = decanoyl-[ACP] + NADP(+);
CC         Xref=Rhea:RHEA:41864, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9640,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78467, ChEBI:CHEBI:78468;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41865;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=decanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxododecanoyl-[ACP]
CC         + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41868, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9640, Rhea:RHEA-COMP:9641, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78468, ChEBI:CHEBI:78469;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41869;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxododecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxydodecanoyl-
CC         [ACP] + NADP(+); Xref=Rhea:RHEA:41872, Rhea:RHEA-COMP:9641,
CC         Rhea:RHEA-COMP:9642, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78469, ChEBI:CHEBI:78470;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41873;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxydodecanoyl-[ACP] = (2E)-dodecenoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:41876, Rhea:RHEA-COMP:9642, Rhea:RHEA-COMP:9643,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78470, ChEBI:CHEBI:78472;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41877;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-dodecenoyl-[ACP] + H(+) + NADPH = dodecanoyl-[ACP] +
CC         NADP(+); Xref=Rhea:RHEA:41880, Rhea:RHEA-COMP:9643, Rhea:RHEA-
CC         COMP:9644, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:65264, ChEBI:CHEBI:78472;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41881;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dodecanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxotetradecanoyl-
CC         [ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41884, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:65264, ChEBI:CHEBI:78449, ChEBI:CHEBI:78473;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41885;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxotetradecanoyl-[ACP] + H(+) + NADPH = (3R)-
CC         hydroxytetradecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41888,
CC         Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9646, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78473,
CC         ChEBI:CHEBI:78474; Evidence={ECO:0000269|PubMed:7567999,
CC         ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41889;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxytetradecanoyl-[ACP] = (2E)-tetradecenoyl-[ACP] +
CC         H2O; Xref=Rhea:RHEA:41892, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9647,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78474, ChEBI:CHEBI:78475;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41893;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-tetradecenoyl-[ACP] + H(+) + NADPH = NADP(+) +
CC         tetradecanoyl-[ACP]; Xref=Rhea:RHEA:41896, Rhea:RHEA-COMP:9647,
CC         Rhea:RHEA-COMP:9648, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78475, ChEBI:CHEBI:78477;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41897;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + malonyl-[ACP] + tetradecanoyl-[ACP] = 3-
CC         oxohexadecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41900,
CC         Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9649,
CC         Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78477,
CC         ChEBI:CHEBI:78478; Evidence={ECO:0000269|PubMed:7567999,
CC         ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41901;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxohexadecanoyl-[ACP] + H(+) + NADPH = (3R)-
CC         hydroxyhexadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41904, Rhea:RHEA-
CC         COMP:9649, Rhea:RHEA-COMP:9650, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78478, ChEBI:CHEBI:78480;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41905;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxyhexadecanoyl-[ACP] = (2E)-hexadecenoyl-[ACP] +
CC         H2O; Xref=Rhea:RHEA:41908, Rhea:RHEA-COMP:9650, Rhea:RHEA-COMP:9651,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78480, ChEBI:CHEBI:78481;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41909;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-hexadecenoyl-[ACP] + H(+) + NADPH = hexadecanoyl-[ACP] +
CC         NADP(+); Xref=Rhea:RHEA:41912, Rhea:RHEA-COMP:9651, Rhea:RHEA-
CC         COMP:9652, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78481, ChEBI:CHEBI:78483;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41913;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC         ECO:0000269|PubMed:9356448};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hexadecanoyl-[ACP] + malonyl-[ACP] = 3-oxooctadecanoyl-
CC         [ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41916, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9653, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78483, ChEBI:CHEBI:78487;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41917;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxooctadecanoyl-[ACP] + H(+) + NADPH = (3R)-
CC         hydroxyoctadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41920, Rhea:RHEA-
CC         COMP:9653, Rhea:RHEA-COMP:9654, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78487, ChEBI:CHEBI:78488;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41921;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxyoctadecanoyl-[ACP] = (2E)-octadecenoyl-[ACP] +
CC         H2O; Xref=Rhea:RHEA:41924, Rhea:RHEA-COMP:9654, Rhea:RHEA-COMP:9655,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78488, ChEBI:CHEBI:78489;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41925;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-octadecenoyl-[ACP] + H(+) + NADPH = NADP(+) +
CC         octadecanoyl-[ACP]; Xref=Rhea:RHEA:41928, Rhea:RHEA-COMP:9655,
CC         Rhea:RHEA-COMP:9656, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78489, ChEBI:CHEBI:78495;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41929;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + tetradecanoyl-[ACP] = H(+) + holo-[ACP] +
CC         tetradecanoate; Xref=Rhea:RHEA:30123, Rhea:RHEA-COMP:9648, Rhea:RHEA-
CC         COMP:9685, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78477; EC=3.1.2.14;
CC         Evidence={ECO:0000269|PubMed:8962082, ECO:0000269|PubMed:9356448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30124;
CC         Evidence={ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + octadecanoyl-[ACP] = H(+) + holo-[ACP] + octadecanoate;
CC         Xref=Rhea:RHEA:63204, Rhea:RHEA-COMP:9656, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78495;
CC         Evidence={ECO:0000269|PubMed:15507492, ECO:0000269|PubMed:7567999,
CC         ECO:0000269|PubMed:8962082};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63205;
CC         Evidence={ECO:0000269|PubMed:15507492, ECO:0000269|PubMed:7567999,
CC         ECO:0000269|PubMed:8962082};
CC   -!- ACTIVITY REGULATION: Activated by S-nitrosylation which promotes enzyme
CC       dimerization (PubMed:26851298). Cerulenin, a potent non-competitive
CC       pharmacological inhibitor of FAS, binds covalently to the active site
CC       of the condensing enzyme region, inactivating a key enzyme step in
CC       fatty acid synthesis (PubMed:16969344). {ECO:0000269|PubMed:16969344,
CC       ECO:0000269|PubMed:26851298}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=8 uM for acetyl-CoA {ECO:0000269|PubMed:7567999};
CC         KM=20 uM for malonyl-CoA {ECO:0000269|PubMed:7567999};
CC         KM=25 uM for NADPH {ECO:0000269|PubMed:7567999};
CC         KM=4 uM for butanoyl-CoA {ECO:0000269|PubMed:7567999};
CC         KM=7 uM for acetyl-CoA {ECO:0000269|PubMed:16215233};
CC         KM=6 uM for malonyl-CoA {ECO:0000269|PubMed:16215233};
CC         KM=5 uM for NADPH {ECO:0000269|PubMed:16215233};
CC         Vmax=29.6 nmol/min/mg enzyme for the incorporation of acetyl-CoA into
CC         fatty acids {ECO:0000269|PubMed:7567999};
CC         Vmax=220.6 nmol/min/mg enzyme for the incorporation of malonyl-CoA
CC         into fatty acids {ECO:0000269|PubMed:7567999};
CC         Vmax=462 nmol/min/mg enzyme for the oxidation of NADPH
CC         {ECO:0000269|PubMed:7567999};
CC         Vmax=440 nmol/min/mg enzyme for the oxidation of NADPH (at pH 7.0)
CC         {ECO:0000269|PubMed:16215233};
CC       pH dependence:
CC         Optimum pH is 6.5 to 6.7. {ECO:0000269|PubMed:7567999};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000269|PubMed:7567999, ECO:0000269|PubMed:8962082,
CC       ECO:0000269|PubMed:9356448}.
CC   -!- SUBUNIT: Homodimer which is arranged in a head to tail fashion
CC       (PubMed:17618296, PubMed:18022563, Ref.34). Interacts with CEACAM1;
CC       this interaction is insulin and phosphorylation-dependent; reduces
CC       fatty-acid synthase activity. {ECO:0000269|PubMed:17618296,
CC       ECO:0000269|PubMed:18022563, ECO:0000269|Ref.34}.
CC   -!- INTERACTION:
CC       P49327; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-356658, EBI-10827839;
CC       P49327; Q16665: HIF1A; NbExp=4; IntAct=EBI-356658, EBI-447269;
CC       P49327; P42858: HTT; NbExp=13; IntAct=EBI-356658, EBI-466029;
CC       P49327; Q8IV20: LACC1; NbExp=8; IntAct=EBI-356658, EBI-12508070;
CC       P49327; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-356658, EBI-739832;
CC       P49327; PRO_0000045603 [Q99IB8]; Xeno; NbExp=6; IntAct=EBI-356658, EBI-6927928;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17081065}.
CC       Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass
CC       spectrometry in melanosome fractions from stage I to stage IV.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Prominent expression in brain, lung,
CC       liver and mammary gland. {ECO:0000269|PubMed:7567999,
CC       ECO:0000269|PubMed:7595075}.
CC   -!- PTM: S-nitrosylation of Fatty acid synthase at cysteine residues Cys-
CC       1471 or Cys-2091 is important for the enzyme dimerization. In
CC       adipocytes, S-nitrosylation of Fatty acid synthase occurs under
CC       physiological conditions and gradually increases during adipogenesis.
CC       {ECO:0000269|PubMed:26851298}.
CC   -!- MISCELLANEOUS: The relatively low beta-ketoacyl synthase activity may
CC       be attributable to the low 4'-phosphopantetheine content of the
CC       protein.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB35516.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAC50259.1; Type=Miscellaneous discrepancy; Note=Several sequencing errors.; Evidence={ECO:0000305};
CC       Sequence=BAE06070.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U26644; AAC50259.1; ALT_SEQ; mRNA.
DR   EMBL; U29344; AAA73576.1; -; mRNA.
DR   EMBL; AY451392; AAS09886.1; -; mRNA.
DR   EMBL; AB209988; BAE06070.1; ALT_INIT; mRNA.
DR   EMBL; AC135056; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC007267; AAH07267.1; -; mRNA.
DR   EMBL; BC007909; AAH07909.1; -; mRNA.
DR   EMBL; BC014634; AAH14634.2; -; mRNA.
DR   EMBL; BC063242; AAH63242.1; -; mRNA.
DR   EMBL; S80437; AAB35516.1; ALT_INIT; mRNA.
DR   CCDS; CCDS11801.1; -.
DR   PIR; A57788; A57788.
DR   PIR; G01880; G01880.
DR   RefSeq; NP_004095.4; NM_004104.4.
DR   RefSeq; XP_011521840.1; XM_011523538.2.
DR   PDB; 1XKT; X-ray; 2.60 A; A/B=2218-2502.
DR   PDB; 2CG5; X-ray; 2.70 A; B=2119-2207.
DR   PDB; 2JFD; X-ray; 2.81 A; A/B/C/D=422-823.
DR   PDB; 2JFK; X-ray; 2.40 A; A/B/C/D=422-831.
DR   PDB; 2PX6; X-ray; 2.30 A; A/B=2200-2511.
DR   PDB; 3HHD; X-ray; 2.15 A; A/B/C/D=2-963.
DR   PDB; 3TJM; X-ray; 1.48 A; A=2218-2500.
DR   PDB; 4PIV; X-ray; 2.30 A; A/B=1110-2114.
DR   PDB; 4W82; X-ray; 1.70 A; A/B=1529-1867.
DR   PDB; 4W9N; X-ray; 1.84 A; A/B/C/D=1529-1867.
DR   PDB; 4Z49; X-ray; 1.70 A; A/B=2221-2502.
DR   PDB; 5C37; X-ray; 2.30 A; A/C=1108-1523, A/C=1877-2122.
DR   PDB; 6NNA; X-ray; 2.26 A; A/B=1109-2114.
DR   PDB; 7MHD; X-ray; 2.03 A; A=2215-2503.
DR   PDB; 7MHE; X-ray; 2.80 A; AAA=2215-2503.
DR   PDB; 8EYI; EM; 2.70 A; E/F=855-2511.
DR   PDB; 8EYK; EM; 2.70 A; E/F=855-2511.
DR   PDB; 8G7X; X-ray; 1.81 A; A/B=858-1103.
DR   PDB; 8GKC; EM; 2.45 A; A/D=855-2511.
DR   PDBsum; 1XKT; -.
DR   PDBsum; 2CG5; -.
DR   PDBsum; 2JFD; -.
DR   PDBsum; 2JFK; -.
DR   PDBsum; 2PX6; -.
DR   PDBsum; 3HHD; -.
DR   PDBsum; 3TJM; -.
DR   PDBsum; 4PIV; -.
DR   PDBsum; 4W82; -.
DR   PDBsum; 4W9N; -.
DR   PDBsum; 4Z49; -.
DR   PDBsum; 5C37; -.
DR   PDBsum; 6NNA; -.
DR   PDBsum; 7MHD; -.
DR   PDBsum; 7MHE; -.
DR   PDBsum; 8EYI; -.
DR   PDBsum; 8EYK; -.
DR   PDBsum; 8G7X; -.
DR   PDBsum; 8GKC; -.
DR   AlphaFoldDB; P49327; -.
DR   EMDB; EMD-28690; -.
DR   EMDB; EMD-28691; -.
DR   EMDB; EMD-40182; -.
DR   SMR; P49327; -.
DR   BioGRID; 108488; 1066.
DR   DIP; DIP-33681N; -.
DR   IntAct; P49327; 135.
DR   MINT; P49327; -.
DR   STRING; 9606.ENSP00000304592; -.
DR   BindingDB; P49327; -.
DR   ChEMBL; CHEMBL4158; -.
DR   DrugBank; DB01034; Cerulenin.
DR   DrugBank; DB01083; Orlistat.
DR   DrugCentral; P49327; -.
DR   GuidetoPHARMACOLOGY; 2608; -.
DR   SwissLipids; SLP:000000765; -.
DR   ESTHER; human-FASN; Thioesterase.
DR   CarbonylDB; P49327; -.
DR   GlyCosmos; P49327; 2 sites, 1 glycan.
DR   GlyGen; P49327; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; P49327; -.
DR   MetOSite; P49327; -.
DR   PhosphoSitePlus; P49327; -.
DR   SwissPalm; P49327; -.
DR   BioMuta; FASN; -.
DR   DMDM; 269849686; -.
DR   CPTAC; CPTAC-369; -.
DR   CPTAC; CPTAC-370; -.
DR   CPTAC; CPTAC-371; -.
DR   CPTAC; CPTAC-372; -.
DR   jPOST; P49327; -.
DR   MassIVE; P49327; -.
DR   PaxDb; 9606-ENSP00000304592; -.
DR   PeptideAtlas; P49327; -.
DR   PRIDE; P49327; -.
DR   ProteomicsDB; 55989; -.
DR   Pumba; P49327; -.
DR   Antibodypedia; 1650; 831 antibodies from 41 providers.
DR   DNASU; 2194; -.
DR   Ensembl; ENST00000306749.4; ENSP00000304592.2; ENSG00000169710.9.
DR   GeneID; 2194; -.
DR   KEGG; hsa:2194; -.
DR   MANE-Select; ENST00000306749.4; ENSP00000304592.2; NM_004104.5; NP_004095.4.
DR   UCSC; uc002kdu.4; human.
DR   AGR; HGNC:3594; -.
DR   CTD; 2194; -.
DR   DisGeNET; 2194; -.
DR   GeneCards; FASN; -.
DR   HGNC; HGNC:3594; FASN.
DR   HPA; ENSG00000169710; Tissue enhanced (adipose tissue, breast).
DR   MIM; 600212; gene.
DR   neXtProt; NX_P49327; -.
DR   OpenTargets; ENSG00000169710; -.
DR   PharmGKB; PA28006; -.
DR   VEuPathDB; HostDB:ENSG00000169710; -.
DR   eggNOG; KOG1202; Eukaryota.
DR   GeneTree; ENSGT00940000157276; -.
DR   HOGENOM; CLU_000022_31_7_1; -.
DR   InParanoid; P49327; -.
DR   OMA; KMRGGEF; -.
DR   OrthoDB; 3378513at2759; -.
DR   PhylomeDB; P49327; -.
DR   TreeFam; TF300549; -.
DR   BioCyc; MetaCyc:HS09992-MONOMER; -.
DR   BRENDA; 2.3.1.39; 2681.
DR   BRENDA; 2.3.1.85; 2681.
DR   PathwayCommons; P49327; -.
DR   Reactome; R-HSA-163765; ChREBP activates metabolic gene expression.
DR   Reactome; R-HSA-199220; Vitamin B5 (pantothenate) metabolism.
DR   Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR   Reactome; R-HSA-75105; Fatty acyl-CoA biosynthesis.
DR   Reactome; R-HSA-9029558; NR1H2 & NR1H3 regulate gene expression linked to lipogenesis.
DR   SABIO-RK; P49327; -.
DR   SignaLink; P49327; -.
DR   SIGNOR; P49327; -.
DR   UniPathway; UPA00094; -.
DR   BioGRID-ORCS; 2194; 173 hits in 1172 CRISPR screens.
DR   ChiTaRS; FASN; human.
DR   EvolutionaryTrace; P49327; -.
DR   GeneWiki; Fatty_acid_synthase; -.
DR   GenomeRNAi; 2194; -.
DR   Pharos; P49327; Tchem.
DR   PRO; PR:P49327; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P49327; protein.
DR   Bgee; ENSG00000169710; Expressed in right hemisphere of cerebellum and 185 other cell types or tissues.
DR   ExpressionAtlas; P49327; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0042587; C:glycogen granule; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0047450; F:(3R)-3-hydroxybutanoyl-[acyl-carrier-protein] hydratase activity; IEA:RHEA.
DR   GO; GO:0008693; F:(3R)-3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity; IEA:RHEA.
DR   GO; GO:0008659; F:(3R)-3-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:RHEA.
DR   GO; GO:0047451; F:(3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:RHEA.
DR   GO; GO:0004317; F:(3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:RHEA.
DR   GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IDA:FlyBase.
DR   GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR   GO; GO:0141148; F:enoyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR   GO; GO:0016297; F:fatty acyl-[ACP] hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
DR   GO; GO:0090557; P:establishment of endothelial intestinal barrier; IEA:Ensembl.
DR   GO; GO:0008611; P:ether lipid biosynthetic process; IEA:Ensembl.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006631; P:fatty acid metabolic process; TAS:ProtInc.
DR   GO; GO:0002068; P:glandular epithelial cell development; IEA:Ensembl.
DR   GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR   GO; GO:0030879; P:mammary gland development; IEA:Ensembl.
DR   GO; GO:0044788; P:modulation by host of viral process; IDA:UniProtKB.
DR   GO; GO:0030224; P:monocyte differentiation; IEA:Ensembl.
DR   GO; GO:0030223; P:neutrophil differentiation; IEA:Ensembl.
DR   GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd08954; KR_1_FAS_SDR_x; 2.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 2.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR049391; FAS_pseudo-KR.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR013217; Methyltransf_12.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR049900; PKS_mFAS_DH.
DR   InterPro; IPR050091; PKS_NRPS_Biosynth_Enz.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR001031; Thioesterase.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF7; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   Pfam; PF21149; FAS_pseudo-KR; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF08242; Methyltransf_12; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR   PROSITE; PS52019; PKS_MFAS_DH; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Hydrolase; Isopeptide bond;
KW   Lipid biosynthesis; Lipid metabolism; Lyase; Multifunctional enzyme; NAD;
KW   NADP; Oxidoreductase; Phosphopantetheine; Phosphoprotein;
KW   Proteomics identification; Pyridoxal phosphate; Reference proteome;
KW   S-nitrosylation; Transferase; Ubl conjugation.
FT   CHAIN           1..2511
FT                   /note="Fatty acid synthase"
FT                   /id="PRO_0000180276"
FT   DOMAIN          1..406
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   DOMAIN          838..1108
FT                   /note="PKS/mFAS DH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   DOMAIN          2121..2198
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          429..817
FT                   /note="Acyl and malonyl transferases"
FT                   /evidence="ECO:0000250"
FT   REGION          838..966
FT                   /note="N-terminal hotdog fold"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   REGION          981..1108
FT                   /note="C-terminal hotdog fold"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   REGION          1635..1863
FT                   /note="Enoyl reductase"
FT                   /evidence="ECO:0000250"
FT   REGION          1864..2118
FT                   /note="Beta-ketoacyl reductase"
FT                   /evidence="ECO:0000250"
FT   REGION          2207..2511
FT                   /note="Thioesterase"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        161
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        293
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        331
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        581
FT                   /note="For malonyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        878
FT                   /note="Proton acceptor; for dehydratase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   ACT_SITE        1031
FT                   /note="Proton donor; for dehydratase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   ACT_SITE        2308
FT                   /note="For thioesterase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022,
FT                   ECO:0000269|PubMed:17618296"
FT   ACT_SITE        2481
FT                   /note="For thioesterase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   BINDING         647..648
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250|UniProtKB:P19096"
FT   BINDING         671
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250|UniProtKB:P19096"
FT   BINDING         773
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250|UniProtKB:P19096"
FT   BINDING         1671..1688
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="1"
FT                   /ligand_note="for enoyl reductase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         1886..1901
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="2"
FT                   /ligand_note="for ketoreductase activity"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895"
FT   MOD_RES         63
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         70
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         207
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         298
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         436
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         528
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         673
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         725
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P19096"
FT   MOD_RES         992
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P19096"
FT   MOD_RES         1174
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         1411
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         1471
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000269|PubMed:26851298"
FT   MOD_RES         1584
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1594
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P19096"
FT   MOD_RES         1704
FT                   /note="N6-(pyridoxal phosphate)lysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1704
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         1771
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         1847
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         1995
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         2091
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000269|PubMed:26851298"
FT   MOD_RES         2156
FT                   /note="O-(pantetheine 4'-phosphoryl)serine; alternate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000269|PubMed:7567999"
FT   MOD_RES         2156
FT                   /note="Phosphoserine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P12785"
FT   MOD_RES         2198
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         2204
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19369195,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         2215
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         2236
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         2391
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P19096"
FT   CROSSLNK        2449
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25114211"
FT   VARIANT         477
FT                   /note="R -> H (in dbSNP:rs113931914)"
FT                   /evidence="ECO:0000269|PubMed:28472301"
FT                   /id="VAR_079534"
FT   VARIANT         1483
FT                   /note="V -> I (in dbSNP:rs2228305)"
FT                   /id="VAR_055479"
FT   VARIANT         1694
FT                   /note="R -> H (in dbSNP:rs561903908)"
FT                   /id="VAR_055480"
FT   VARIANT         1888
FT                   /note="I -> V (in dbSNP:rs2228307)"
FT                   /id="VAR_055481"
FT   CONFLICT        459..462
FT                   /note="AVPA -> LSPT (in Ref. 2; AAA73576)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        528..529
FT                   /note="KP -> NR (in Ref. 2; AAA73576)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        637
FT                   /note="G -> A (in Ref. 2; AAA73576)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        801
FT                   /note="G -> R (in Ref. 2; AAA73576)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        902
FT                   /note="A -> P (in Ref. 2; AAA73576)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        958
FT                   /note="V -> M (in Ref. 3; AAS09886)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1121
FT                   /note="P -> S (in Ref. 2; AAA73576 and 3; AAS09886)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1151
FT                   /note="K -> T (in Ref. 6; AAH63242)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1353..1356
FT                   /note="LGDI -> SGH (in Ref. 2; AAA73576)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1386
FT                   /note="L -> V (in Ref. 2; AAA73576)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1467..1468
FT                   /note="NR -> T (in Ref. 2; AAA73576)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1827
FT                   /note="K -> E (in Ref. 3; AAS09886)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1934
FT                   /note="R -> A (in Ref. 2; AAA73576)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2065
FT                   /note="D -> H (in Ref. 9; AAB35516)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2087
FT                   /note="R -> A (in Ref. 2; AAA73576)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2363
FT                   /note="A -> P (in Ref. 9; AAB35516)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2428
FT                   /note="R -> G (in Ref. 2; AAA73576)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2453
FT                   /note="A -> T (in Ref. 9; AAB35516)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2456
FT                   /note="E -> Q (in Ref. 9; AAB35516)"
FT                   /evidence="ECO:0000305"
FT   STRAND          4..13
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          16..18
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           19..27
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          36..40
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           44..46
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   TURN            62..66
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           69..73
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           77..92
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           97..100
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          106..110
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           115..120
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   TURN            124..126
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           130..135
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           139..148
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          154..158
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           160..162
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           163..176
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          181..189
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           194..202
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          227..235
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           236..238
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          243..253
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           266..279
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           284..286
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          287..291
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           300..312
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          320..323
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           326..329
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           333..335
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           336..350
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           367..370
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          373..376
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          387..393
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          397..406
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           416..419
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          422..430
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           431..443
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   TURN            444..446
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           448..457
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   TURN            462..464
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          467..477
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          481..484
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          492..496
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   TURN            504..509
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           510..512
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           514..527
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           528..530
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           534..539
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           545..547
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           549..569
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          575..579
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           583..590
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           596..611
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          618..625
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           627..633
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          639..645
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          648..654
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           655..667
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          672..675
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          677..679
FT                   /evidence="ECO:0007829|PDB:2JFD"
FT   HELIX           685..690
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           691..701
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          702..704
FT                   /evidence="ECO:0007829|PDB:2JFD"
FT   STRAND          715..717
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           719..721
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           725..728
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           732..740
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           745..749
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          757..764
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           768..774
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          780..783
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           792..805
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           812..815
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           831..833
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   HELIX           847..849
FT                   /evidence="ECO:0007829|PDB:3HHD"
FT   STRAND          858..865
FT                   /evidence="ECO:0007829|PDB:8G7X"
FT   STRAND          867..870
FT                   /evidence="ECO:0007829|PDB:8EYI"
FT   HELIX           873..877
FT                   /evidence="ECO:0007829|PDB:8G7X"
FT   STRAND          878..880
FT                   /evidence="ECO:0007829|PDB:8GKC"
FT   STRAND          883..885
FT                   /evidence="ECO:0007829|PDB:8G7X"
FT   HELIX           888..903
FT                   /evidence="ECO:0007829|PDB:8G7X"
FT   HELIX           907..909
FT                   /evidence="ECO:0007829|PDB:8G7X"
FT   STRAND          912..919
FT                   /evidence="ECO:0007829|PDB:8G7X"
FT   STRAND          927..938
FT                   /evidence="ECO:0007829|PDB:8G7X"
FT   TURN            939..942
FT                   /evidence="ECO:0007829|PDB:8G7X"
FT   STRAND          943..948
FT                   /evidence="ECO:0007829|PDB:8G7X"
FT   STRAND          951..960
FT                   /evidence="ECO:0007829|PDB:8G7X"
FT   HELIX           966..969
FT                   /evidence="ECO:0007829|PDB:8G7X"
FT   STRAND          981..983
FT                   /evidence="ECO:0007829|PDB:8EYI"
FT   STRAND          984..986
FT                   /evidence="ECO:0007829|PDB:8G7X"
FT   HELIX           987..996
FT                   /evidence="ECO:0007829|PDB:8G7X"
FT   STRAND          999..1001
FT                   /evidence="ECO:0007829|PDB:8GKC"
FT   HELIX           1003..1005
FT                   /evidence="ECO:0007829|PDB:8G7X"
FT   STRAND          1008..1012
FT                   /evidence="ECO:0007829|PDB:8G7X"
FT   STRAND          1015..1021
FT                   /evidence="ECO:0007829|PDB:8G7X"
FT   HELIX           1026..1039
FT                   /evidence="ECO:0007829|PDB:8G7X"
FT   STRAND          1047..1057
FT                   /evidence="ECO:0007829|PDB:8G7X"
FT   HELIX           1059..1065
FT                   /evidence="ECO:0007829|PDB:8G7X"
FT   STRAND          1074..1081
FT                   /evidence="ECO:0007829|PDB:8G7X"
FT   TURN            1082..1085
FT                   /evidence="ECO:0007829|PDB:8G7X"
FT   STRAND          1086..1089
FT                   /evidence="ECO:0007829|PDB:8G7X"
FT   STRAND          1092..1101
FT                   /evidence="ECO:0007829|PDB:8G7X"
FT   STRAND          1113..1127
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   TURN            1128..1130
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   HELIX           1132..1149
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   HELIX           1173..1175
FT                   /evidence="ECO:0007829|PDB:5C37"
FT   HELIX           1177..1187
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   HELIX           1200..1205
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   HELIX           1206..1211
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   TURN            1213..1217
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   HELIX           1218..1220
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   HELIX           1222..1233
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   STRAND          1236..1246
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   HELIX           1247..1250
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   TURN            1253..1255
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   HELIX           1256..1260
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   STRAND          1263..1265
FT                   /evidence="ECO:0007829|PDB:5C37"
FT   STRAND          1267..1276
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   HELIX           1277..1283
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   HELIX           1284..1289
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   STRAND          1293..1296
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   HELIX           1305..1307
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   STRAND          1309..1316
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   TURN            1317..1319
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   HELIX           1325..1334
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   STRAND          1336..1347
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   HELIX           1352..1360
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   HELIX           1374..1383
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   STRAND          1387..1394
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   STRAND          1397..1404
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   STRAND          1413..1416
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   HELIX           1424..1433
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   STRAND          1441..1445
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   HELIX           1453..1460
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   HELIX           1466..1468
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   STRAND          1469..1474
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   STRAND          1479..1482
FT                   /evidence="ECO:0007829|PDB:8EYI"
FT   HELIX           1491..1499
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   STRAND          1502..1507
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   STRAND          1510..1518
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   STRAND          1525..1529
FT                   /evidence="ECO:0007829|PDB:8GKC"
FT   STRAND          1531..1537
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   HELIX           1541..1543
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   STRAND          1544..1548
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   HELIX           1550..1553
FT                   /evidence="ECO:0007829|PDB:8GKC"
FT   STRAND          1562..1570
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   HELIX           1573..1579
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   HELIX           1585..1587
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   HELIX           1589..1592
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   STRAND          1602..1606
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   STRAND          1612..1616
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   STRAND          1622..1628
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   HELIX           1630..1632
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   STRAND          1633..1635
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   HELIX           1642..1645
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   HELIX           1649..1659
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   TURN            1660..1663
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   STRAND          1670..1675
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   HELIX           1679..1690
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   STRAND          1694..1701
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   HELIX           1702..1711
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   HELIX           1717..1719
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   STRAND          1720..1722
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   STRAND          1723..1726
FT                   /evidence="ECO:0007829|PDB:4W9N"
FT   HELIX           1728..1735
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   TURN            1736..1738
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   STRAND          1741..1746
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   TURN            1747..1751
FT                   /evidence="ECO:0007829|PDB:4W9N"
FT   HELIX           1753..1757
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   STRAND          1760..1769
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   HELIX           1772..1775
FT                   /evidence="ECO:0007829|PDB:8GKC"
FT   STRAND          1779..1781
FT                   /evidence="ECO:0007829|PDB:8GKC"
FT   TURN            1784..1788
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   STRAND          1790..1794
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   HELIX           1796..1799
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   TURN            1801..1803
FT                   /evidence="ECO:0007829|PDB:4W9N"
FT   HELIX           1805..1819
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   STRAND          1828..1832
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   HELIX           1833..1835
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   HELIX           1836..1845
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   STRAND          1849..1857
FT                   /evidence="ECO:0007829|PDB:4W82"
FT   STRAND          1873..1876
FT                   /evidence="ECO:0007829|PDB:8GKC"
FT   STRAND          1885..1890
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   TURN            1891..1893
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   HELIX           1895..1906
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   STRAND          1911..1915
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   HELIX           1923..1934
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   STRAND          1938..1942
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   HELIX           1949..1962
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   STRAND          1963..1970
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   HELIX           1980..1982
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   HELIX           1985..2009
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   STRAND          2015..2021
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   HELIX           2022..2025
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   HELIX           2032..2050
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   STRAND          2056..2060
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   STRAND          2065..2067
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   TURN            2068..2070
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   STRAND          2075..2077
FT                   /evidence="ECO:0007829|PDB:5C37"
FT   HELIX           2088..2099
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   STRAND          2104..2111
FT                   /evidence="ECO:0007829|PDB:6NNA"
FT   HELIX           2127..2134
FT                   /evidence="ECO:0007829|PDB:2CG5"
FT   TURN            2149..2153
FT                   /evidence="ECO:0007829|PDB:2CG5"
FT   HELIX           2156..2170
FT                   /evidence="ECO:0007829|PDB:2CG5"
FT   HELIX           2176..2180
FT                   /evidence="ECO:0007829|PDB:2CG5"
FT   HELIX           2184..2192
FT                   /evidence="ECO:0007829|PDB:2CG5"
FT   HELIX           2219..2222
FT                   /evidence="ECO:0007829|PDB:3TJM"
FT   STRAND          2230..2233
FT                   /evidence="ECO:0007829|PDB:3TJM"
FT   STRAND          2239..2241
FT                   /evidence="ECO:0007829|PDB:3TJM"
FT   STRAND          2244..2247
FT                   /evidence="ECO:0007829|PDB:3TJM"
FT   HELIX           2255..2257
FT                   /evidence="ECO:0007829|PDB:3TJM"
FT   HELIX           2258..2263
FT                   /evidence="ECO:0007829|PDB:3TJM"
FT   STRAND          2268..2271
FT                   /evidence="ECO:0007829|PDB:3TJM"
FT   HELIX           2282..2293
FT                   /evidence="ECO:0007829|PDB:3TJM"
FT   TURN            2294..2296
FT                   /evidence="ECO:0007829|PDB:3TJM"
FT   STRAND          2303..2307
FT                   /evidence="ECO:0007829|PDB:3TJM"
FT   HELIX           2309..2325
FT                   /evidence="ECO:0007829|PDB:3TJM"
FT   STRAND          2333..2338
FT                   /evidence="ECO:0007829|PDB:3TJM"
FT   HELIX           2343..2352
FT                   /evidence="ECO:0007829|PDB:3TJM"
FT   HELIX           2360..2375
FT                   /evidence="ECO:0007829|PDB:3TJM"
FT   HELIX           2380..2387
FT                   /evidence="ECO:0007829|PDB:3TJM"
FT   STRAND          2390..2392
FT                   /evidence="ECO:0007829|PDB:3TJM"
FT   HELIX           2393..2407
FT                   /evidence="ECO:0007829|PDB:3TJM"
FT   HELIX           2413..2432
FT                   /evidence="ECO:0007829|PDB:3TJM"
FT   STRAND          2443..2447
FT                   /evidence="ECO:0007829|PDB:3TJM"
FT   STRAND          2453..2458
FT                   /evidence="ECO:0007829|PDB:4Z49"
FT   TURN            2459..2463
FT                   /evidence="ECO:0007829|PDB:3TJM"
FT   HELIX           2464..2466
FT                   /evidence="ECO:0007829|PDB:3TJM"
FT   STRAND          2468..2470
FT                   /evidence="ECO:0007829|PDB:7MHD"
FT   STRAND          2472..2476
FT                   /evidence="ECO:0007829|PDB:3TJM"
FT   HELIX           2483..2485
FT                   /evidence="ECO:0007829|PDB:3TJM"
FT   HELIX           2487..2499
FT                   /evidence="ECO:0007829|PDB:3TJM"
SQ   SEQUENCE   2511 AA;  273427 MW;  7A07171FEFA3287B CRC64;
     MEEVVIAGMS GKLPESENLQ EFWDNLIGGV DMVTDDDRRW KAGLYGLPRR SGKLKDLSRF
     DASFFGVHPK QAHTMDPQLR LLLEVTYEAI VDGGINPDSL RGTHTGVWVG VSGSETSEAL
     SRDPETLVGY SMVGCQRAMM ANRLSFFFDF RGPSIALDTA CSSSLMALQN AYQAIHSGQC
     PAAIVGGINV LLKPNTSVQF LRLGMLSPEG TCKAFDTAGN GYCRSEGVVA VLLTKKSLAR
     RVYATILNAG TNTDGFKEQG VTFPSGDIQE QLIRSLYQSA GVAPESFEYI EAHGTGTKVG
     DPQELNGITR ALCATRQEPL LIGSTKSNMG HPEPASGLAA LAKVLLSLEH GLWAPNLHFH
     SPNPEIPALL DGRLQVVDQP LPVRGGNVGI NSFGFGGSNV HIILRPNTQP PPAPAPHATL
     PRLLRASGRT PEAVQKLLEQ GLRHSQDLAF LSMLNDIAAV PATAMPFRGY AVLGGERGGP
     EVQQVPAGER PLWFICSGMG TQWRGMGLSL MRLDRFRDSI LRSDEAVKPF GLKVSQLLLS
     TDESTFDDIV HSFVSLTAIQ IGLIDLLSCM GLRPDGIVGH SLGEVACGYA DGCLSQEEAV
     LAAYWRGQCI KEAHLPPGAM AAVGLSWEEC KQRCPPGVVP ACHNSKDTVT ISGPQAPVFE
     FVEQLRKEGV FAKEVRTGGM AFHSYFMEAI APPLLQELKK VIREPKPRSA RWLSTSIPEA
     QWHSSLARTS SAEYNVNNLV SPVLFQEALW HVPEHAVVLE IAPHALLQAV LKRGLKPSCT
     IIPLMKKDHR DNLEFFLAGI GRLHLSGIDA NPNALFPPVE FPAPRGTPLI SPLIKWDHSL
     AWDVPAAEDF PNGSGSPSAA IYNIDTSSES PDHYLVDHTL DGRVLFPATG YLSIVWKTLA
     RALGLGVEQL PVVFEDVVLH QATILPKTGT VSLEVRLLEA SRAFEVSENG NLVVSGKVYQ
     WDDPDPRLFD HPESPTPNPT EPLFLAQAEV YKELRLRGYD YGPHFQGILE ASLEGDSGRL
     LWKDNWVSFM DTMLQMSILG SAKHGLYLPT RVTAIHIDPA THRQKLYTLQ DKAQVADVVV
     SRWLRVTVAG GVHISGLHTE SAPRRQQEQQ VPILEKFCFT PHTEEGCLSE RAALQEELQL
     CKGLVQALQT KVTQQGLKMV VPGLDGAQIP RDPSQQELPR LLSAACRLQL NGNLQLELAQ
     VLAQERPKLP EDPLLSGLLD SPALKACLDT AVENMPSLKM KVVEVLAGHG HLYSRIPGLL
     SPHPLLQLSY TATDRHPQAL EAAQAELQQH DVAQGQWDPA DPAPSALGSA DLLVCNCAVA
     ALGDPASALS NMVAALREGG FLLLHTLLRG HPLGDIVAFL TSTEPQYGQG ILSQDAWESL
     FSRVSLRLVG LKKSFYGSTL FLCRRPTPQD SPIFLPVDDT SFRWVESLKG ILADEDSSRP
     VWLKAINCAT SGVVGLVNCL RREPGGNRLR CVLLSNLSST SHVPEVDPGS AELQKVLQGD
     LVMNVYRDGA WGAFRHFLLE EDKPEEPTAH AFVSTLTRGD LSSIRWVCSS LRHAQPTCPG
     AQLCTVYYAS LNFRDIMLAT GKLSPDAIPG KWTSQDSLLG MEFSGRDASG KRVMGLVPAK
     GLATSVLLSP DFLWDVPSNW TLEEAASVPV VYSTAYYALV VRGRVRPGET LLIHSGSGGV
     GQAAIAIALS LGCRVFTTVG SAEKRAYLQA RFPQLDSTSF ANSRDTSFEQ HVLWHTGGKG
     VDLVLNSLAE EKLQASVRCL ATHGRFLEIG KFDLSQNHPL GMAIFLKNVT FHGVLLDAFF
     NESSADWREV WALVQAGIRD GVVRPLKCTV FHGAQVEDAF RYMAQGKHIG KVVVQVLAEE
     PEAVLKGAKP KLMSAISKTF CPAHKSYIIA GGLGGFGLEL AQWLIQRGVQ KLVLTSRSGI
     RTGYQAKQVR RWRRQGVQVQ VSTSNISSLE GARGLIAEAA QLGPVGGVFN LAVVLRDGLL
     ENQTPEFFQD VCKPKYSGTL NLDRVTREAC PELDYFVVFS SVSCGRGNAG QSNYGFANSA
     MERICEKRRH EGLPGLAVQW GAIGDVGILV ETMSTNDTIV SGTLPQRMAS CLEVLDLFLN
     QPHMVLSSFV LAEKAAAYRD RDSQRDLVEA VAHILGIRDL AAVNLDSSLA DLGLDSLMSV
     EVRQTLEREL NLVLSVREVR QLTLRKLQEL SSKADEASEL ACPTPKEDGL AQQQTQLNLR
     SLLVNPEGPT LMRLNSVQSS ERPLFLVHPI EGSTTVFHSL ASRLSIPTYG LQCTRAAPLD
     SIHSLAAYYI DCIRQVQPEG PYRVAGYSYG ACVAFEMCSQ LQAQQSPAPT HNSLFLFDGS
     PTYVLAYTQS YRAKLTPGCE AEAETEAICF FVQQFTDMEH NRVLEALLPL KGLEERVAAA
     VDLIIKSHQG LDRQELSFAA RSFYYKLRAA EQYTPKAKYH GNVMLLRAKT GGAYGEDLGA
     DYNLSQVCDG KVSVHVIEGD HRTLLEGSGL ESIISIIHSS LAEPRVSVRE G
//