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/"; 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; 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 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. DR Genevisible; P20701; HS. 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 //