ID ZDH20_HUMAN Reviewed; 365 AA.
AC Q5W0Z9; A8MTV9; C9JG20; I6L9D4; Q2TB82; Q6NVU8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 02-OCT-2024, entry version 158.
DE RecName: Full=Palmitoyltransferase ZDHHC20 {ECO:0000305|PubMed:27153536};
DE EC=2.3.1.225 {ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:29326245};
DE AltName: Full=Acyltransferase ZDHHC20 {ECO:0000305|PubMed:29326245};
DE EC=2.3.1.- {ECO:0000305|PubMed:29326245};
DE AltName: Full=DHHC domain-containing cysteine-rich protein 20 {ECO:0000303|PubMed:27153536};
DE Short=DHHC20 {ECO:0000303|PubMed:27153536};
DE AltName: Full=Zinc finger DHHC domain-containing protein 20 {ECO:0000312|HGNC:HGNC:20749};
GN Name=ZDHHC20 {ECO:0000312|HGNC:HGNC:20749};
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC TISSUE=Ovary, and Testis;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [5]
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305 AND SER-330, AND
RP IDENTIFICATION BY MASS 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=27153536; DOI=10.1016/j.molcel.2016.04.003;
RA Runkle K.B., Kharbanda A., Stypulkowski E., Cao X.J., Wang W., Garcia B.A.,
RA Witze E.S.;
RT "Inhibition of DHHC20-Mediated EGFR Palmitoylation Creates a Dependence on
RT EGFR Signaling.";
RL Mol. Cell 62:385-396(2016).
RN [9]
RP FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=34599882; DOI=10.1016/j.devcel.2021.09.016;
RA Mesquita F.S., Abrami L., Sergeeva O., Turelli P., Qing E., Kunz B.,
RA Raclot C., Paz Montoya J., Abriata L.A., Gallagher T., Dal Peraro M.,
RA Trono D., D'Angelo G., van der Goot F.G.;
RT "S-acylation controls SARS-CoV-2 membrane lipid organization and enhances
RT infectivity.";
RL Dev. Cell 56:1-18(2021).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=33219126; DOI=10.1074/jbc.ra120.015701;
RA Malgapo M.I.P., Safadi J.M., Linder M.E.;
RT "Metallo-beta-Lactamase Domain-Containing Protein 2 (MBLAC2) is S-
RT palmitoylated and exhibits acyl-CoA hydrolase activity.";
RL J. Biol. Chem. 296:100106-100118(2021).
RN [11] {ECO:0007744|PDB:6BML, ECO:0007744|PDB:6BMM, ECO:0007744|PDB:6BMN}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 5-299 IN COMPLEX WITH PALMITATE;
RP SUBSTRATE ANALOG AND ZINC, FUNCTION, CATALYTIC ACTIVITY, DOMAIN,
RP MUTAGENESIS OF ILE-22; SER-29; ASP-153; HIS-154; CYS-156; TRP-158; PHE-171;
RP PHE-174; TYR-181; LEU-227; 240-THR-THR-241; GLU-243; ASN-266; TRP-267 AND
RP PHE-271, ACTIVE SITE, SUBCELLULAR LOCATION, TOPOLOGY, AND PALMITOYLATION.
RX PubMed=29326245; DOI=10.1126/science.aao6326;
RA Rana M.S., Kumar P., Lee C.J., Verardi R., Rajashankar K.R., Banerjee A.;
RT "Fatty acyl recognition and transfer by an integral membrane S-
RT acyltransferase.";
RL Science 359:0-0(2018).
CC -!- FUNCTION: Palmitoyltransferase that could catalyze the addition of
CC palmitate onto various protein substrates (PubMed:27153536,
CC PubMed:29326245, PubMed:33219126). Catalyzes palmitoylation of Cys
CC residues in the cytoplasmic C-terminus of EGFR, and modulates the
CC duration of EGFR signaling by modulating palmitoylation-dependent EGFR
CC internalization and degradation (PubMed:27153536). Has a preference for
CC acyl-CoA with C16 fatty acid chains (PubMed:29326245). Can also utilize
CC acyl-CoA with C14 and C18 fatty acid chains (PubMed:29326245). May
CC palmitoylate CALHM1 subunit of gustatory voltage-gated ion channels and
CC modulate channel gating and kinetics. {ECO:0000250|UniProtKB:Q5Y5T1,
CC ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:29326245,
CC ECO:0000269|PubMed:33219126}.
CC -!- FUNCTION: (Microbial infection) Dominant palmitoyltransferase
CC responsible for lipidation of SARS coronavirus-2/SARS-CoV-2 spike
CC protein. Through a sequential action with ZDHHC9, rapidly and
CC efficiently palmitoylates spike protein following its synthesis in the
CC endoplasmic reticulum (ER). In the infected cell, promotes spike
CC biogenesis by protecting it from premature ER degradation, increases
CC half-life and controls the lipid organization of its immediate membrane
CC environment. Once the virus has formed, spike palmitoylation controls
CC fusion with the target cell. {ECO:0000269|PubMed:34599882}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-
CC hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151;
CC EC=2.3.1.225; Evidence={ECO:0000269|PubMed:29326245,
CC ECO:0000269|PubMed:33219126, ECO:0000269|PubMed:34599882};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000305|PubMed:29326245};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + tetradecanoyl-CoA = CoA + S-
CC tetradecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59736, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:15433, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:143199;
CC Evidence={ECO:0000269|PubMed:29326245};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59737;
CC Evidence={ECO:0000305|PubMed:29326245};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + octadecanoyl-CoA = CoA + S-
CC octadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59740, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:15434, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:143200;
CC Evidence={ECO:0000269|PubMed:29326245};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741;
CC Evidence={ECO:0000305|PubMed:29326245};
CC -!- INTERACTION:
CC Q5W0Z9-4; P07339: CTSD; NbExp=3; IntAct=EBI-25840130, EBI-2115097;
CC Q5W0Z9-4; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-25840130, EBI-396669;
CC Q5W0Z9-4; O76024: WFS1; NbExp=3; IntAct=EBI-25840130, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:29326245}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:29326245}. Cell membrane
CC {ECO:0000269|PubMed:27153536}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:29326245}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:27153536}. Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:34599882}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment
CC membrane {ECO:0000305|PubMed:34599882}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5W0Z9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5W0Z9-2; Sequence=VSP_016276, VSP_016277;
CC Name=3;
CC IsoId=Q5W0Z9-3; Sequence=VSP_040481, VSP_040482;
CC Name=4;
CC IsoId=Q5W0Z9-4; Sequence=VSP_056002;
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000269|PubMed:29326245}.
CC -!- PTM: Autopalmitoylated (in vitro). {ECO:0000269|PubMed:29326245}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL136219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08309.1; -; Genomic_DNA.
DR EMBL; BC034944; AAH34944.1; -; mRNA.
DR EMBL; BC050367; AAH50367.2; -; mRNA.
DR EMBL; BC067898; AAH67898.1; -; mRNA.
DR EMBL; BC110517; AAI10518.1; -; mRNA.
DR CCDS; CCDS45017.1; -. [Q5W0Z9-3]
DR CCDS; CCDS81758.1; -. [Q5W0Z9-1]
DR RefSeq; NP_001273567.1; NM_001286638.1.
DR RefSeq; NP_001316988.1; NM_001330059.1. [Q5W0Z9-1]
DR RefSeq; NP_694983.2; NM_153251.3. [Q5W0Z9-3]
DR PDB; 6BML; X-ray; 2.95 A; A/B=5-299.
DR PDB; 6BMM; X-ray; 2.35 A; A/B=7-299.
DR PDB; 6BMN; X-ray; 2.25 A; A/B=5-299.
DR PDB; 7KHM; X-ray; 2.88 A; A/B=2-316.
DR PDBsum; 6BML; -.
DR PDBsum; 6BMM; -.
DR PDBsum; 6BMN; -.
DR PDBsum; 7KHM; -.
DR AlphaFoldDB; Q5W0Z9; -.
DR SMR; Q5W0Z9; -.
DR BioGRID; 128991; 40.
DR IntAct; Q5W0Z9; 22.
DR MINT; Q5W0Z9; -.
DR STRING; 9606.ENSP00000383433; -.
DR BindingDB; Q5W0Z9; -.
DR ChEMBL; CHEMBL5169156; -.
DR TCDB; 8.A.114.1.6; the huntington-interacting protein 14 (hip14) family.
DR iPTMnet; Q5W0Z9; -.
DR PhosphoSitePlus; Q5W0Z9; -.
DR SwissPalm; Q5W0Z9; -.
DR BioMuta; ZDHHC20; -.
DR DMDM; 74748004; -.
DR jPOST; Q5W0Z9; -.
DR MassIVE; Q5W0Z9; -.
DR PaxDb; 9606-ENSP00000371905; -.
DR PeptideAtlas; Q5W0Z9; -.
DR ProteomicsDB; 61482; -.
DR ProteomicsDB; 65788; -. [Q5W0Z9-1]
DR ProteomicsDB; 65789; -. [Q5W0Z9-2]
DR ProteomicsDB; 65790; -. [Q5W0Z9-3]
DR Pumba; Q5W0Z9; -.
DR Antibodypedia; 4929; 217 antibodies from 24 providers.
DR DNASU; 253832; -.
DR Ensembl; ENST00000320220.13; ENSP00000313583.9; ENSG00000180776.17. [Q5W0Z9-4]
DR Ensembl; ENST00000382466.7; ENSP00000371905.3; ENSG00000180776.17. [Q5W0Z9-3]
DR Ensembl; ENST00000400590.8; ENSP00000383433.3; ENSG00000180776.17. [Q5W0Z9-1]
DR Ensembl; ENST00000415724.2; ENSP00000401232.1; ENSG00000180776.17. [Q5W0Z9-1]
DR GeneID; 253832; -.
DR KEGG; hsa:253832; -.
DR MANE-Select; ENST00000400590.8; ENSP00000383433.3; NM_001330059.2; NP_001316988.1.
DR UCSC; uc001uoa.4; human. [Q5W0Z9-1]
DR AGR; HGNC:20749; -.
DR CTD; 253832; -.
DR DisGeNET; 253832; -.
DR GeneCards; ZDHHC20; -.
DR HGNC; HGNC:20749; ZDHHC20.
DR HPA; ENSG00000180776; Low tissue specificity.
DR MIM; 617972; gene.
DR neXtProt; NX_Q5W0Z9; -.
DR OpenTargets; ENSG00000180776; -.
DR PharmGKB; PA134880838; -.
DR VEuPathDB; HostDB:ENSG00000180776; -.
DR eggNOG; KOG1315; Eukaryota.
DR GeneTree; ENSGT00940000153716; -.
DR InParanoid; Q5W0Z9; -.
DR OMA; AFHNYKF; -.
DR OrthoDB; 6683at2759; -.
DR PhylomeDB; Q5W0Z9; -.
DR TreeFam; TF316044; -.
DR PathwayCommons; Q5W0Z9; -.
DR Reactome; R-HSA-9694548; Maturation of spike protein.
DR SignaLink; Q5W0Z9; -.
DR BioGRID-ORCS; 253832; 19 hits in 1154 CRISPR screens.
DR ChiTaRS; ZDHHC20; human.
DR GenomeRNAi; 253832; -.
DR Pharos; Q5W0Z9; Tbio.
DR PRO; PR:Q5W0Z9; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q5W0Z9; protein.
DR Bgee; ENSG00000180776; Expressed in upper arm skin and 191 other cell types or tissues.
DR ExpressionAtlas; Q5W0Z9; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:UniProt.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IMP:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0016409; F:palmitoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0019705; F:protein-cysteine S-myristoyltransferase activity; IEA:RHEA.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0140439; F:protein-cysteine S-stearoyltransferase activity; IEA:RHEA.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IDA:UniProtKB.
DR GO; GO:0044794; P:positive regulation by host of viral process; IDA:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; IDA:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR GO; GO:0016188; P:synaptic vesicle maturation; IBA:GO_Central.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR PANTHER; PTHR12246; PALMITOYLTRANSFERASE ZDHHC16; 1.
DR PANTHER; PTHR12246:SF13; PALMITOYLTRANSFERASE ZDHHC16; 1.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Alternative splicing; Cell membrane;
KW Cytoplasm; Endoplasmic reticulum; Golgi apparatus; Host-virus interaction;
KW Lipoprotein; Membrane; Metal-binding; Palmitate; Phosphoprotein;
KW Proteomics identification; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..365
FT /note="Palmitoyltransferase ZDHHC20"
FT /id="PRO_0000212906"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:29326245"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29326245"
FT TOPO_DOM 36..53
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:29326245"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29326245"
FT TOPO_DOM 75..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:29326245"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29326245"
FT TOPO_DOM 191..207
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:29326245"
FT TRANSMEM 208..231
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29326245"
FT TOPO_DOM 232..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:29326245"
FT DOMAIN 126..176
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 156
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000269|PubMed:29326245"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29326245,
FT ECO:0007744|PDB:6BMN"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29326245,
FT ECO:0007744|PDB:6BMN"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:29326245"
FT BINDING 140..143
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:29326245"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29326245,
FT ECO:0007744|PDB:6BMN"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29326245,
FT ECO:0007744|PDB:6BMN"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29326245,
FT ECO:0007744|PDB:6BMN"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29326245,
FT ECO:0007744|PDB:6BMN"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29326245,
FT ECO:0007744|PDB:6BMN"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29326245,
FT ECO:0007744|PDB:6BMN"
FT SITE 29
FT /note="Important for selectivity toward medium-length fatty
FT acids"
FT /evidence="ECO:0000269|PubMed:29326245"
FT SITE 181
FT /note="Important for selectivity toward medium-length fatty
FT acids"
FT /evidence="ECO:0000269|PubMed:29326245"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT VAR_SEQ 124..130
FT /note="TIRYCEK -> SLMQSTK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016276"
FT VAR_SEQ 131..365
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016277"
FT VAR_SEQ 315..365
FT /note="SSGSNQPFPIKPLSESKNRLLDSESQWLENGAEEGIVKSGTNNHVTVAIEN
FT -> RSKLQR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056002"
FT VAR_SEQ 315
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040481"
FT VAR_SEQ 355..365
FT /note="TNNHVTVAIEN -> V (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040482"
FT MUTAGEN 22
FT /note="I->W: Strongly reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:29326245"
FT MUTAGEN 29
FT /note="S->F: Strongly reduced catalytic activity. Enhances
FT activity with acyl-CoA with C12 and C14 fatty acid chains."
FT /evidence="ECO:0000269|PubMed:29326245"
FT MUTAGEN 153
FT /note="D->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:29326245"
FT MUTAGEN 154
FT /note="H->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:29326245"
FT MUTAGEN 156
FT /note="C->S: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:29326245"
FT MUTAGEN 158
FT /note="W->A: Strongly reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:29326245"
FT MUTAGEN 171
FT /note="F->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:29326245"
FT MUTAGEN 174
FT /note="F->A: Strongly reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:29326245"
FT MUTAGEN 181
FT /note="Y->A: Moderately reduced catalytic activity.
FT Enhances activity with acyl-CoA with C18 and C20 fatty acid
FT chains."
FT /evidence="ECO:0000269|PubMed:29326245"
FT MUTAGEN 227
FT /note="L->W: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:29326245"
FT MUTAGEN 240..241
FT /note="TT->AA: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:29326245"
FT MUTAGEN 243
FT /note="E->A: Mildly reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:29326245"
FT MUTAGEN 266
FT /note="N->A: Strongly reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:29326245"
FT MUTAGEN 267
FT /note="Missing: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:29326245"
FT MUTAGEN 271
FT /note="F->A: Mildly reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:29326245"
FT HELIX 7..14
FT /evidence="ECO:0007829|PDB:6BMN"
FT HELIX 17..34
FT /evidence="ECO:0007829|PDB:6BMN"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:6BMN"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:6BMN"
FT HELIX 48..74
FT /evidence="ECO:0007829|PDB:6BMN"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:6BMN"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:6BMN"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:6BMN"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:6BMN"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:6BMN"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:6BMN"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:6BMN"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:6BMN"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:6BMN"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:6BMN"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:6BMN"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:6BMN"
FT HELIX 168..197
FT /evidence="ECO:0007829|PDB:6BMN"
FT HELIX 204..237
FT /evidence="ECO:0007829|PDB:6BMN"
FT HELIX 241..245
FT /evidence="ECO:0007829|PDB:6BMN"
FT TURN 256..259
FT /evidence="ECO:0007829|PDB:6BMN"
FT HELIX 263..271
FT /evidence="ECO:0007829|PDB:6BMN"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:6BMN"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:6BMN"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:6BMN"
SQ SEQUENCE 365 AA; 42278 MW; 179D8882138E4F53 CRC64;
MAPWTLWRCC QRVVGWVPVL FITFVVVWSY YAYVVELCVF TIFGNEENGK TVVYLVAFHL
FFVMFVWSYW MTIFTSPASP SKEFYLSNSE KERYEKEFSQ ERQQEILRRA ARALPIYTTS
ASKTIRYCEK CQLIKPDRAH HCSACDSCIL KMDHHCPWVN NCVGFSNYKF FLLFLLYSLL
YCLFVAATVL EYFIKFWTNE LTDTRAKFHV LFLFFVSAMF FISVLSLFSY HCWLVGKNRT
TIESFRAPTF SYGPDGNGFS LGCSKNWRQV FGDEKKYWLL PIFSSLGDGC SFPTRLVGMD
PEQASVTNQN EYARSSGSNQ PFPIKPLSES KNRLLDSESQ WLENGAEEGI VKSGTNNHVT
VAIEN
//