ID ITAL_HUMAN Reviewed; 1170 AA.
AC P20701; O43746; Q45H73; Q96HB1; Q9UBC8;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 3.
DT 27-MAR-2024, entry version 234.
DE RecName: Full=Integrin alpha-L {ECO:0000305};
DE AltName: Full=CD11 antigen-like family member A;
DE AltName: Full=Leukocyte adhesion glycoprotein LFA-1 alpha chain;
DE Short=LFA-1A;
DE AltName: Full=Leukocyte function-associated molecule 1 alpha chain;
DE AltName: CD_antigen=CD11a;
DE Flags: Precursor;
GN Name=ITGAL {ECO:0000312|HGNC:HGNC:6148}; Synonyms=CD11A;
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] (ISOFORM 1), PROTEIN SEQUENCE OF 120-132;
RP 226-237; 282-288; 433-441; 522-531; 569-582; 591-604; 831-844 AND 957-974,
RP DOMAIN, AND VARIANT TRP-214.
RX PubMed=2537322; DOI=10.1083/jcb.108.2.703;
RA Larson R.S., Corbi A.L., Berman L., Springer T.;
RT "Primary structure of the leukocyte function-associated molecule-1 alpha
RT subunit: an integrin with an embedded domain defining a protein
RT superfamily.";
RL J. Cell Biol. 108:703-712(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-144; TRP-214; LYS-746
RP AND THR-791.
RG NIEHS SNPs program;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 2), AND VARIANT
RP TRP-214.
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from human
RT chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Lymph;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RX PubMed=8099450; DOI=10.1073/pnas.90.11.5364;
RA Shelley C.S., Farokhzad O.C., Arnaout M.A.;
RT "Identification of cell-specific and developmentally regulated nuclear
RT factors that direct myeloid and lymphoid expression of the CD11a gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5364-5368(1993).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RX PubMed=8103515; DOI=10.1016/s0021-9258(19)36514-7;
RA Nueda A., Lopez-Cabrera M., Vara A., Corbi A.L.;
RT "Characterization of the CD11a (alpha L, LFA-1 alpha) integrin gene
RT promoter.";
RL J. Biol. Chem. 268:19305-19311(1993).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RX PubMed=8097887; DOI=10.1073/pnas.90.9.4221;
RA Cornwell R.D., Gollahon K.A., Hickstein D.D.;
RT "Description of the leukocyte function-associated antigen 1 (LFA-1 or
RT CD11a) promoter.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:4221-4225(1993).
RN [10]
RP FUNCTION.
RX PubMed=11812992; DOI=10.1038/ni755;
RA Ostermann G., Weber K.S., Zernecke A., Schroeder A., Weber C.;
RT "JAM-1 is a ligand of the beta(2) integrin LFA-1 involved in
RT transendothelial migration of leukocytes.";
RL Nat. Immunol. 3:151-158(2002).
RN [11]
RP FUNCTION.
RX PubMed=15356110; DOI=10.4049/jimmunol.173.6.3653;
RA Barber D.F., Faure M., Long E.O.;
RT "LFA-1 contributes an early signal for NK cell cytotoxicity.";
RL J. Immunol. 173:3653-3659(2004).
RN [12]
RP DOMAIN, AND FUNCTION.
RX PubMed=15528364; DOI=10.4049/jimmunol.173.10.6259;
RA Fraemohs L., Koenen R.R., Ostermann G., Heinemann B., Weber C.;
RT "The functional interaction of the beta 2 integrin lymphocyte function-
RT associated antigen-1 with junctional adhesion molecule-A is mediated by the
RT I domain.";
RL J. Immunol. 173:6259-6264(2004).
RN [13]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-1165, AND
RP MUTAGENESIS OF SER-1165.
RX PubMed=16301335; DOI=10.1083/jcb.200504016;
RA Fagerholm S.C., Hilden T.J., Nurmi S.M., Gahmberg C.G.;
RT "Specific integrin alpha and beta chain phosphorylations regulate LFA-1
RT activation through affinity-dependent and -independent mechanisms.";
RL J. Cell Biol. 171:705-715(2005).
RN [14]
RP INTERACTION WITH SARS-COV ORF7A PROTEIN (MICROBIAL INFECTION).
RX PubMed=18020948; DOI=10.1515/bc.2007.157;
RA Haenel K., Willbold D.;
RT "SARS-CoV accessory protein 7a directly interacts with human LFA-1.";
RL Biol. Chem. 388:1325-1332(2007).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-188.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [16]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23775590; DOI=10.1007/s10495-013-0873-z;
RA Kristof E., Zahuczky G., Katona K., Doro Z., Nagy E., Fesues L.;
RT "Novel role of ICAM3 and LFA-1 in the clearance of apoptotic neutrophils by
RT human macrophages.";
RL Apoptosis 18:1235-1251(2013).
RN [17]
RP INTERACTION WITH THBD.
RX PubMed=27055590; DOI=10.1016/j.bbrc.2016.04.007;
RA Kawamoto E., Okamoto T., Takagi Y., Honda G., Suzuki K., Imai H.,
RA Shimaoka M.;
RT "LFA-1 and Mac-1 integrins bind to the serine/threonine-rich domain of
RT thrombomodulin.";
RL Biochem. Biophys. Res. Commun. 473:1005-1012(2016).
RN [18]
RP FUNCTION.
RX PubMed=29100055; DOI=10.1016/j.molcel.2017.10.003;
RA Swaim C.D., Scott A.F., Canadeo L.A., Huibregtse J.M.;
RT "Extracellular ISG15 signals cytokine secretion through the LFA-1 integrin
RT receptor.";
RL Mol. Cell 68:581-590(2017).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 153-335, AND SEQUENCE REVISION TO
RP 214.
RX PubMed=7479767; DOI=10.1073/pnas.92.22.10277;
RA Qu A., Leahy D.J.;
RT "Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, alpha L beta
RT 2) integrin.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:10277-10281(1995).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 153-335.
RX PubMed=8805579; DOI=10.1016/s0969-2126(96)00100-1;
RA Qu A., Leahy D.J.;
RT "The role of the divalent cation in the structure of the I domain from the
RT CD11a/CD18 integrin.";
RL Structure 4:931-942(1996).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 153-334.
RX PubMed=10493852; DOI=10.1006/jmbi.1999.3047;
RA Kallen J., Welzenbach K., Ramage P., Geyl D., Kriwacki R., Legge G.,
RA Cottens S., Weitz-Schmidt G., Hommel U.;
RT "Structural basis for LFA-1 inhibition upon lovastatin binding to the CD11a
RT I-domain.";
RL J. Mol. Biol. 292:1-9(1999).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 155-331 IN COMPLEX WITH ICAM1.
RX PubMed=12526797; DOI=10.1016/s0092-8674(02)01257-6;
RA Shimaoka M., Xiao T., Liu J.H., Yang Y., Dong Y., Jun C.D., McCormack A.,
RA Zhang R., Joachimiak A., Takagi J., Wang J.H., Springer T.A.;
RT "Structures of the alpha L I domain and its complex with ICAM-1 reveal a
RT shape-shifting pathway for integrin regulation.";
RL Cell 112:99-111(2003).
CC -!- FUNCTION: Integrin ITGAL/ITGB2 is a receptor for ICAM1, ICAM2, ICAM3
CC and ICAM4. Integrin ITGAL/ITGB2 is a receptor for F11R
CC (PubMed:11812992, PubMed:15528364). Integrin ITGAL/ITGB2 is a receptor
CC for the secreted form of ubiquitin-like protein ISG15; the interaction
CC is mediated by ITGAL (PubMed:29100055). Involved in a variety of immune
CC phenomena including leukocyte-endothelial cell interaction, cytotoxic
CC T-cell mediated killing, and antibody dependent killing by granulocytes
CC and monocytes. Contributes to natural killer cell cytotoxicity
CC (PubMed:15356110). Involved in leukocyte adhesion and transmigration of
CC leukocytes including T-cells and neutrophils (PubMed:11812992).
CC Required for generation of common lymphoid progenitor cells in bone
CC marrow, indicating a role in lymphopoiesis (By similarity). Integrin
CC ITGAL/ITGB2 in association with ICAM3, contributes to apoptotic
CC neutrophil phagocytosis by macrophages (PubMed:23775590).
CC {ECO:0000250|UniProtKB:P24063, ECO:0000269|PubMed:11812992,
CC ECO:0000269|PubMed:15356110, ECO:0000269|PubMed:15528364,
CC ECO:0000269|PubMed:23775590, ECO:0000269|PubMed:29100055}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (PubMed:12526797).
CC The ITGAL alpha subunit associates with the ITGB2 beta subunit
CC (PubMed:12526797). Interacts with THBD (PubMed:27055590).
CC {ECO:0000269|PubMed:12526797, ECO:0000269|PubMed:27055590}.
CC -!- SUBUNIT: (Microbial infection) Interacts with SARS-CoV Orf7a protein.
CC {ECO:0000269|PubMed:18020948}.
CC -!- INTERACTION:
CC P20701; P05362: ICAM1; NbExp=3; IntAct=EBI-961214, EBI-1035358;
CC P20701; P08575: PTPRC; NbExp=2; IntAct=EBI-961214, EBI-1341;
CC P20701; PRO_0000037551 [Q9WMX2]; Xeno; NbExp=2; IntAct=EBI-961214, EBI-6863748;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16301335};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P20701-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P20701-2; Sequence=VSP_002738;
CC Name=3;
CC IsoId=P20701-3; Sequence=VSP_042842, VSP_042843;
CC -!- TISSUE SPECIFICITY: Leukocytes. {ECO:0000269|PubMed:16301335,
CC ECO:0000269|PubMed:23775590}.
CC -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain
CC (PubMed:2537322). Integrins with I-domains do not undergo protease
CC cleavage. The I-domain is necessary and sufficient for interaction with
CC ICAM1 and F11R (PubMed:15528364). {ECO:0000269|PubMed:15528364,
CC ECO:0000269|PubMed:2537322}.
CC -!- PTM: In resting T-cells, up to 40% of surface ITGAL is constitutively
CC phosphorylated. Phosphorylation causes conformational changes needed
CC for ligand binding and is necessary for activation by some
CC physiological agents. {ECO:0000269|PubMed:16301335}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/itgal/";
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DR EMBL; Y00796; CAA68747.1; -; mRNA.
DR EMBL; DQ131904; AAZ38713.1; -; Genomic_DNA.
DR EMBL; AC002310; AAC31672.1; -; Genomic_DNA.
DR EMBL; AC116348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471192; EAW52243.1; -; Genomic_DNA.
DR EMBL; BC008777; AAH08777.1; -; mRNA.
DR EMBL; M95609; AAA16474.2; -; Genomic_DNA.
DR EMBL; Z22804; CAA80461.1; -; Genomic_DNA.
DR EMBL; M87662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS32433.1; -. [P20701-1]
DR CCDS; CCDS45461.1; -. [P20701-3]
DR PIR; S03308; S03308.
DR RefSeq; NP_001107852.1; NM_001114380.1. [P20701-3]
DR RefSeq; NP_002200.2; NM_002209.2. [P20701-1]
DR PDB; 1CQP; X-ray; 2.60 A; A/B=153-334.
DR PDB; 1DGQ; NMR; -; A=152-336.
DR PDB; 1LFA; X-ray; 1.80 A; A/B=150-336.
DR PDB; 1MJN; X-ray; 1.30 A; A=153-331.
DR PDB; 1MQ8; X-ray; 3.30 A; B/D=155-331.
DR PDB; 1MQ9; X-ray; 2.00 A; A=153-331.
DR PDB; 1MQA; X-ray; 2.50 A; A=153-331.
DR PDB; 1RD4; X-ray; 2.40 A; A/B/C/D=150-336.
DR PDB; 1T0P; X-ray; 1.66 A; A=153-326.
DR PDB; 1XDD; X-ray; 2.20 A; A/B=152-336.
DR PDB; 1XDG; X-ray; 2.10 A; A/B=152-336.
DR PDB; 1XUO; X-ray; 1.80 A; A/B=152-336.
DR PDB; 1ZON; X-ray; 2.00 A; A=150-336.
DR PDB; 1ZOO; X-ray; 3.00 A; A/B=150-336.
DR PDB; 1ZOP; X-ray; 2.00 A; A/B=150-336.
DR PDB; 2ICA; X-ray; 1.56 A; A=154-332.
DR PDB; 2K8O; NMR; -; A=1113-1170.
DR PDB; 2M3E; NMR; -; A=1082-1128.
DR PDB; 2O7N; X-ray; 1.75 A; A=154-332.
DR PDB; 3BN3; X-ray; 2.10 A; A=154-332.
DR PDB; 3BQM; X-ray; 1.95 A; B/C=153-334.
DR PDB; 3BQN; X-ray; 1.80 A; B/C=153-334.
DR PDB; 3E2M; X-ray; 2.00 A; A/B=152-334.
DR PDB; 3EOA; X-ray; 2.80 A; I/J=153-333.
DR PDB; 3EOB; X-ray; 3.60 A; I/J=153-333.
DR PDB; 3F74; X-ray; 1.70 A; A/B/C=153-332.
DR PDB; 3F78; X-ray; 1.60 A; A/B/C=153-332.
DR PDB; 3HI6; X-ray; 2.30 A; A/B=153-332.
DR PDB; 3M6F; X-ray; 1.85 A; A=154-332.
DR PDB; 3TCX; X-ray; 3.60 A; B/D/F/H/J/L/N/P/R/T/V/X/Z/b=154-332.
DR PDB; 4IXD; X-ray; 1.80 A; A=152-336.
DR PDB; 5E6R; X-ray; 2.90 A; A=26-770.
DR PDB; 5E6S; X-ray; 2.15 A; A/C/E=26-770.
DR PDB; 5E6U; X-ray; 2.50 A; A=26-770.
DR PDB; 6BXB; X-ray; 2.39 A; A/B=153-331.
DR PDB; 6BXF; X-ray; 3.20 A; A/B=153-331.
DR PDB; 6BXJ; X-ray; 2.09 A; A=153-331.
DR PDB; 6CKB; X-ray; 2.80 A; A/B=153-331.
DR PDB; 7KC3; X-ray; 1.80 A; C=149-341.
DR PDB; 7KC5; X-ray; 1.86 A; A/C=153-334.
DR PDB; 7KC6; X-ray; 1.85 A; A/C=153-334.
DR PDBsum; 1CQP; -.
DR PDBsum; 1DGQ; -.
DR PDBsum; 1LFA; -.
DR PDBsum; 1MJN; -.
DR PDBsum; 1MQ8; -.
DR PDBsum; 1MQ9; -.
DR PDBsum; 1MQA; -.
DR PDBsum; 1RD4; -.
DR PDBsum; 1T0P; -.
DR PDBsum; 1XDD; -.
DR PDBsum; 1XDG; -.
DR PDBsum; 1XUO; -.
DR PDBsum; 1ZON; -.
DR PDBsum; 1ZOO; -.
DR PDBsum; 1ZOP; -.
DR PDBsum; 2ICA; -.
DR PDBsum; 2K8O; -.
DR PDBsum; 2M3E; -.
DR PDBsum; 2O7N; -.
DR PDBsum; 3BN3; -.
DR PDBsum; 3BQM; -.
DR PDBsum; 3BQN; -.
DR PDBsum; 3E2M; -.
DR PDBsum; 3EOA; -.
DR PDBsum; 3EOB; -.
DR PDBsum; 3F74; -.
DR PDBsum; 3F78; -.
DR PDBsum; 3HI6; -.
DR PDBsum; 3M6F; -.
DR PDBsum; 3TCX; -.
DR PDBsum; 4IXD; -.
DR PDBsum; 5E6R; -.
DR PDBsum; 5E6S; -.
DR PDBsum; 5E6U; -.
DR PDBsum; 6BXB; -.
DR PDBsum; 6BXF; -.
DR PDBsum; 6BXJ; -.
DR PDBsum; 6CKB; -.
DR PDBsum; 7KC3; -.
DR PDBsum; 7KC5; -.
DR PDBsum; 7KC6; -.
DR AlphaFoldDB; P20701; -.
DR BMRB; P20701; -.
DR SMR; P20701; -.
DR BioGRID; 109889; 11.
DR ComplexPortal; CPX-1825; Integrin alphaL-beta2 complex.
DR DIP; DIP-623N; -.
DR IntAct; P20701; 11.
DR MINT; P20701; -.
DR STRING; 9606.ENSP00000349252; -.
DR BindingDB; P20701; -.
DR ChEMBL; CHEMBL1803; -.
DR DrugBank; DB04724; (S)-2-((S)-3-isobutyl-2,5-dioxo-4-quinolin-3-ylmethyl-[1,4]diazepan-1yl)-N-methyl-3-naphtalen-2-yl-propionamide.
DR DrugBank; DB02177; 1-Acetyl-4-(4-{4-[(2-Ethoxyphenyl)Thio]-3-Nitrophenyl}Pyridin-2-Yl)Piperazine.
DR DrugBank; DB07486; 3-({4-[(1E)-3-morpholin-4-yl-3-oxoprop-1-en-1-yl]-2,3-bis(trifluoromethyl)phenyl}sulfanyl)aniline.
DR DrugBank; DB06972; 7A-[(4-cyanophenyl)methyl]-6-(3,5-dichlorophenyl)-5-oxo-2,3,5,7A-tetrahydro-1H-pyrrolo[1,2-A]pyrrole-7-carbonitrile.
DR DrugBank; DB00098; Antithymocyte immunoglobulin (rabbit).
DR DrugBank; DB00095; Efalizumab.
DR DrugBank; DB03932; LFA703.
DR DrugBank; DB11611; Lifitegrast.
DR DrugBank; DB00227; Lovastatin.
DR DrugBank; DB08860; Pitavastatin.
DR DrugBank; DB01098; Rosuvastatin.
DR DrugBank; DB00641; Simvastatin.
DR DrugCentral; P20701; -.
DR GuidetoPHARMACOLOGY; 2451; -.
DR TCDB; 8.A.54.1.6; the integrin (integrin) family.
DR GlyConnect; 1410; 9 N-Linked glycans (1 site).
DR GlyCosmos; P20701; 12 sites, 9 glycans.
DR GlyGen; P20701; 12 sites, 9 N-linked glycans (1 site).
DR iPTMnet; P20701; -.
DR PhosphoSitePlus; P20701; -.
DR BioMuta; ITGAL; -.
DR DMDM; 88911345; -.
DR jPOST; P20701; -.
DR MassIVE; P20701; -.
DR MaxQB; P20701; -.
DR PaxDb; 9606-ENSP00000349252; -.
DR PeptideAtlas; P20701; -.
DR ProteomicsDB; 53774; -. [P20701-1]
DR ProteomicsDB; 53775; -. [P20701-2]
DR ProteomicsDB; 53776; -. [P20701-3]
DR ABCD; P20701; 46 sequenced antibodies.
DR Antibodypedia; 13698; 2405 antibodies from 47 providers.
DR DNASU; 3683; -.
DR Ensembl; ENST00000356798.11; ENSP00000349252.5; ENSG00000005844.19. [P20701-1]
DR Ensembl; ENST00000358164.9; ENSP00000350886.5; ENSG00000005844.19. [P20701-3]
DR GeneID; 3683; -.
DR KEGG; hsa:3683; -.
DR MANE-Select; ENST00000356798.11; ENSP00000349252.5; NM_002209.3; NP_002200.2.
DR UCSC; uc002dyi.5; human. [P20701-1]
DR AGR; HGNC:6148; -.
DR CTD; 3683; -.
DR DisGeNET; 3683; -.
DR GeneCards; ITGAL; -.
DR HGNC; HGNC:6148; ITGAL.
DR HPA; ENSG00000005844; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 153370; gene.
DR neXtProt; NX_P20701; -.
DR OpenTargets; ENSG00000005844; -.
DR PharmGKB; PA29948; -.
DR VEuPathDB; HostDB:ENSG00000005844; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000161495; -.
DR HOGENOM; CLU_004111_3_0_1; -.
DR InParanoid; P20701; -.
DR OMA; TVCFQLK; -.
DR OrthoDB; 3816176at2759; -.
DR PhylomeDB; P20701; -.
DR TreeFam; TF105391; -.
DR PathwayCommons; P20701; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8949275; RUNX3 Regulates Immune Response and Cell Migration.
DR SignaLink; P20701; -.
DR SIGNOR; P20701; -.
DR BioGRID-ORCS; 3683; 16 hits in 1155 CRISPR screens.
DR ChiTaRS; ITGAL; human.
DR EvolutionaryTrace; P20701; -.
DR GeneWiki; CD11a; -.
DR GenomeRNAi; 3683; -.
DR Pharos; P20701; Tclin.
DR PRO; PR:P20701; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P20701; Protein.
DR Bgee; ENSG00000005844; Expressed in granulocyte and 176 other cell types or tissues.
DR ExpressionAtlas; P20701; baseline and differential.
DR Genevisible; P20701; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0034687; C:integrin alphaL-beta2 complex; IDA:UniProtKB.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0050839; F:cell adhesion molecule binding; IMP:UniProtKB.
DR GO; GO:0030369; F:ICAM-3 receptor activity; IMP:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:BHF-UCL.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IMP:BHF-UCL.
DR GO; GO:0006954; P:inflammatory response; NAS:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:ARUK-UCL.
DR GO; GO:0035683; P:memory T cell extravasation; IDA:ARUK-UCL.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR GO; GO:0043113; P:receptor clustering; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR GO; GO:0002291; P:T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; IMP:BHF-UCL.
DR CDD; cd01469; vWA_integrins_alpha_subunit; 1.
DR Gene3D; 1.20.5.2120; -; 1.
DR Gene3D; 1.20.5.930; Bicelle-embedded integrin alpha(iib) transmembrane segment; 1.
DR Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 2.
DR Gene3D; 2.60.40.1460; Integrin domains. Chain A, domain 2; 1.
DR Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR Gene3D; 2.60.40.1530; ntegrin, alpha v. Chain A, domain 4; 1.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR018184; Integrin_alpha_C_CS.
DR InterPro; IPR013649; Integrin_alpha_Ig-like_1.
DR InterPro; IPR048285; Integrin_alpha_Ig-like_2.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR23220; INTEGRIN ALPHA; 1.
DR PANTHER; PTHR23220:SF84; INTEGRIN ALPHA-L; 1.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF08441; Integrin_A_Ig_1; 1.
DR Pfam; PF20805; Integrin_A_Ig_2; 1.
DR Pfam; PF00357; Integrin_alpha; 1.
DR Pfam; PF00092; VWA; 1.
DR PRINTS; PR01185; INTEGRINA.
DR PRINTS; PR00453; VWFADOMAIN.
DR SMART; SM00191; Int_alpha; 5.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR SUPFAM; SSF69179; Integrin domains; 2.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Host-virus interaction; Integrin; Magnesium; Membrane; Metal-binding;
KW Phagocytosis; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1170
FT /note="Integrin alpha-L"
FT /id="PRO_0000016292"
FT TOPO_DOM 26..1090
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1091..1111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1112..1170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 31..82
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 83..141
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT DOMAIN 156..327
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REPEAT 338..389
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 390..445
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 446..506
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 507..563
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 567..627
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REGION 1128..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1115..1119
FT /note="GFFKR motif"
FT COMPBIAS 1154..1170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 468
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 470
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 472
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 476
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 530
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 532
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 534
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 538
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 590
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 594
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 598
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT MOD_RES 1165
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16301335"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 649
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 726
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 730
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 862
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 885
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 897
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1060
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1071
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 73..80
FT /evidence="ECO:0000250"
FT DISULFID 111..129
FT /evidence="ECO:0000250"
FT DISULFID 653..707
FT /evidence="ECO:0000250"
FT DISULFID 771..777
FT /evidence="ECO:0000250"
FT DISULFID 845..861
FT /evidence="ECO:0000250"
FT DISULFID 998..1013
FT /evidence="ECO:0000250"
FT DISULFID 1021..1052
FT /evidence="ECO:0000250"
FT VAR_SEQ 110..192
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042842"
FT VAR_SEQ 746
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042843"
FT VAR_SEQ 954
FT /note="Q -> QGVHGLVEMQTSKQILCRPAGDAEHTVGAQEGELPCPWGVSEAFRDN
FT IRAGPCR (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_002738"
FT VARIANT 144
FT /note="R -> H (in dbSNP:rs34166708)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_025235"
FT VARIANT 214
FT /note="R -> W (in dbSNP:rs1064524)"
FT /evidence="ECO:0000269|PubMed:10493829,
FT ECO:0000269|PubMed:2537322, ECO:0000269|Ref.2"
FT /id="VAR_025236"
FT VARIANT 746
FT /note="Q -> K (in dbSNP:rs34838942)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_025237"
FT VARIANT 791
FT /note="R -> T (in dbSNP:rs2230433)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_025238"
FT MUTAGEN 1165
FT /note="S->A: Abolishes phosphorylation and MEM-83-activated
FT T-cell adhesion to ICAM1. Abolishes integrin alpha-L/beta-2
FT activation by CXCL12 and TERF2IP/RAP1. Does not affect
FT heterodimerization of cell surface expression. Does not
FT affect TCR- or phorbol ester-activated T-cell adhesion to
FT ICAM1."
FT /evidence="ECO:0000269|PubMed:16301335"
FT CONFLICT 660
FT /note="I -> Y (in Ref. 1; CAA68747)"
FT /evidence="ECO:0000305"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:5E6U"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:5E6S"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:5E6S"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:5E6S"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:5E6S"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 108..119
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 122..134
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:1MJN"
FT HELIX 169..185
FT /evidence="ECO:0007829|PDB:1MJN"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:1MJN"
FT STRAND 189..206
FT /evidence="ECO:0007829|PDB:1MJN"
FT HELIX 208..214
FT /evidence="ECO:0007829|PDB:1MJN"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:1MJN"
FT HELIX 233..243
FT /evidence="ECO:0007829|PDB:1MJN"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:1MJN"
FT STRAND 255..265
FT /evidence="ECO:0007829|PDB:1MJN"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:1MJN"
FT STRAND 279..287
FT /evidence="ECO:0007829|PDB:1MJN"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:1MJN"
FT HELIX 293..297
FT /evidence="ECO:0007829|PDB:1MJN"
FT HELIX 298..302
FT /evidence="ECO:0007829|PDB:1MJN"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:1MJN"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:1MJN"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:1MJN"
FT HELIX 323..330
FT /evidence="ECO:0007829|PDB:1MJN"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:3BQN"
FT STRAND 352..359
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:5E6S"
FT HELIX 370..373
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 375..380
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 387..391
FT /evidence="ECO:0007829|PDB:5E6S"
FT TURN 398..401
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 406..411
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 413..416
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 419..424
FT /evidence="ECO:0007829|PDB:5E6S"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 432..437
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 446..452
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 462..467
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 477..482
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 493..499
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 501..510
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 523..527
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 531..535
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 539..543
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 549..554
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 558..561
FT /evidence="ECO:0007829|PDB:5E6R"
FT STRAND 566..570
FT /evidence="ECO:0007829|PDB:5E6S"
FT HELIX 571..574
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 583..589
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 593..595
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 598..603
FT /evidence="ECO:0007829|PDB:5E6S"
FT STRAND 606..612
FT /evidence="ECO:0007829|PDB:5E6S"
FT TURN 1082..1086
FT /evidence="ECO:0007829|PDB:2M3E"
FT HELIX 1090..1114
FT /evidence="ECO:0007829|PDB:2M3E"
FT HELIX 1118..1123
FT /evidence="ECO:0007829|PDB:2K8O"
FT TURN 1124..1127
FT /evidence="ECO:0007829|PDB:2K8O"
FT HELIX 1137..1147
FT /evidence="ECO:0007829|PDB:2K8O"
FT HELIX 1153..1155
FT /evidence="ECO:0007829|PDB:2K8O"
FT HELIX 1156..1165
FT /evidence="ECO:0007829|PDB:2K8O"
FT HELIX 1167..1170
FT /evidence="ECO:0007829|PDB:2K8O"
SQ SEQUENCE 1170 AA; 128770 MW; 22A7AF92EF286876 CRC64;
MKDSCITVMA MALLSGFFFF APASSYNLDV RGARSFSPPR AGRHFGYRVL QVGNGVIVGA
PGEGNSTGSL YQCQSGTGHC LPVTLRGSNY TSKYLGMTLA TDPTDGSILA CDPGLSRTCD
QNTYLSGLCY LFRQNLQGPM LQGRPGFQEC IKGNVDLVFL FDGSMSLQPD EFQKILDFMK
DVMKKLSNTS YQFAAVQFST SYKTEFDFSD YVKRKDPDAL LKHVKHMLLL TNTFGAINYV
ATEVFREELG ARPDATKVLI IITDGEATDS GNIDAAKDII RYIIGIGKHF QTKESQETLH
KFASKPASEF VKILDTFEKL KDLFTELQKK IYVIEGTSKQ DLTSFNMELS SSGISADLSR
GHAVVGAVGA KDWAGGFLDL KADLQDDTFI GNEPLTPEVR AGYLGYTVTW LPSRQKTSLL
ASGAPRYQHM GRVLLFQEPQ GGGHWSQVQT IHGTQIGSYF GGELCGVDVD QDGETELLLI
GAPLFYGEQR GGRVFIYQRR QLGFEEVSEL QGDPGYPLGR FGEAITALTD INGDGLVDVA
VGAPLEEQGA VYIFNGRHGG LSPQPSQRIE GTQVLSGIQW FGRSIHGVKD LEGDGLADVA
VGAESQMIVL SSRPVVDMVT LMSFSPAEIP VHEVECSYST SNKMKEGVNI TICFQIKSLI
PQFQGRLVAN LTYTLQLDGH RTRRRGLFPG GRHELRRNIA VTTSMSCTDF SFHFPVCVQD
LISPINVSLN FSLWEEEGTP RDQRAQGKDI PPILRPSLHS ETWEIPFEKN CGEDKKCEAN
LRVSFSPARS RALRLTAFAS LSVELSLSNL EEDAYWVQLD LHFPPGLSFR KVEMLKPHSQ
IPVSCEELPE ESRLLSRALS CNVSSPIFKA GHSVALQMMF NTLVNSSWGD SVELHANVTC
NNEDSDLLED NSATTIIPIL YPINILIQDQ EDSTLYVSFT PKGPKIHQVK HMYQVRIQPS
IHDHNIPTLE AVVGVPQPPS EGPITHQWSV QMEPPVPCHY EDLERLPDAA EPCLPGALFR
CPVVFRQEIL VQVIGTLELV GEIEASSMFS LCSSLSISFN SSKHFHLYGS NASLAQVVMK
VDVVYEKQML YLYVLSGIGG LLLLLLIFIV LYKVGFFKRN LKEKMEAGRG VPNGIPAEDS
EQLASGQEAG DPGCLKPLHE KDSESGGGKD
//