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 11-NOV-2015, entry version 176. DE RecName: Full=Integrin alpha-L; 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; Synonyms=CD11A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND RP 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 RT alpha 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; RP LYS-746 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., RA Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L., RA Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E., RA Harris P.C., Venter J.C., Adams M.D.; RT "Genome duplications and other features in 12 Mb of DNA sequence from RT human 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., RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., RA 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., RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., RA 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 RT 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; 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 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- RT linked cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 153-335, AND SEQUENCE RP REVISION TO 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 RT beta 2) integrin."; RL Proc. Natl. Acad. Sci. U.S.A. 92:10277-10281(1995). RN [12] 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 RT the CD11a/CD18 integrin."; RL Structure 4:931-942(1996). RN [13] 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 RT CD11a I-domain."; RL J. Mol. Biol. 292:1-9(1999). RN [14] RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 155-331 IN COMPLEX WITH RP 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., RA McCormack A., Zhang R., Joachimiak A., Takagi J., Wang J.H., RA Springer T.A.; RT "Structures of the alpha L I domain and its complex with ICAM-1 reveal RT a shape-shifting pathway for integrin regulation."; RL Cell 112:99-111(2003). CC -!- FUNCTION: Integrin alpha-L/beta-2 is a receptor for ICAM1, ICAM2, CC ICAM3 and ICAM4. It is involved in a variety of immune phenomena CC including leukocyte-endothelial cell interaction, cytotoxic T-cell CC mediated killing, and antibody dependent killing by granulocytes CC and monocytes. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-L CC associates with beta-2. {ECO:0000269|PubMed:12526797}. CC -!- INTERACTION: CC Q9WMX2:- (xeno); NbExp=2; IntAct=EBI-961214, EBI-6863748; CC P08575:PTPRC; NbExp=2; IntAct=EBI-961214, EBI-1341; CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. 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 Note=No experimental confirmation available.; CC Name=3; CC IsoId=P20701-3; Sequence=VSP_042842, VSP_042843; CC -!- TISSUE SPECIFICITY: Leukocytes. CC -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins CC with I-domains do not undergo protease cleavage. CC -!- SIMILARITY: Belongs to the integrin alpha chain family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 7 FG-GAP repeats. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 VWFA domain. {ECO:0000255|PROSITE- CC ProRule:PRU00219}. 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 UniGene; Hs.174103; -. DR PDB; 1CQP; X-ray; 2.60 A; A/B=153-334. DR PDB; 1DGQ; NMR; -; A=152-336. DR PDB; 1IJ4; Model; -; L=153-333. 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 PDBsum; 1CQP; -. DR PDBsum; 1DGQ; -. DR PDBsum; 1IJ4; -. 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 ProteinModelPortal; P20701; -. DR SMR; P20701; 154-331, 1082-1170. DR BioGrid; 109889; 6. DR DIP; DIP-623N; -. DR IntAct; P20701; 7. DR MINT; MINT-1130696; -. DR STRING; 9606.ENSP00000349252; -. DR BindingDB; P20701; -. DR ChEMBL; CHEMBL2096661; -. DR DrugBank; DB00098; Antithymocyte globulin. DR DrugBank; DB00095; Efalizumab. DR DrugBank; DB00227; Lovastatin. DR GuidetoPHARMACOLOGY; 2451; -. DR PhosphoSite; P20701; -. DR BioMuta; ITGAL; -. DR DMDM; 88911345; -. DR MaxQB; P20701; -. DR PaxDb; P20701; -. DR PRIDE; P20701; -. DR DNASU; 3683; -. DR Ensembl; ENST00000356798; ENSP00000349252; ENSG00000005844. [P20701-1] DR Ensembl; ENST00000358164; ENSP00000350886; ENSG00000005844. [P20701-3] DR GeneID; 3683; -. DR KEGG; hsa:3683; -. DR UCSC; uc002dyi.4; human. [P20701-1] DR UCSC; uc002dyj.4; human. [P20701-3] DR CTD; 3683; -. DR GeneCards; ITGAL; -. DR H-InvDB; HIX0012960; -. DR H-InvDB; HIX0026987; -. DR HGNC; HGNC:6148; ITGAL. DR HPA; CAB025011; -. DR MIM; 153370; gene. DR neXtProt; NX_P20701; -. DR PharmGKB; PA29948; -. DR eggNOG; KOG3637; Eukaryota. DR eggNOG; ENOG410XPVZ; LUCA. DR GeneTree; ENSGT00760000118782; -. DR HOGENOM; HOG000113114; -. DR HOVERGEN; HBG006188; -. DR InParanoid; P20701; -. DR KO; K05718; -. DR OMA; GEDKKCE; -. DR OrthoDB; EOG74XS5V; -. DR PhylomeDB; P20701; -. DR TreeFam; TF105391; -. 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 SignaLink; P20701; -. DR ChiTaRS; ITGAL; human. DR EvolutionaryTrace; P20701; -. DR GeneWiki; CD11a; -. DR GenomeRNAi; 3683; -. DR NextBio; 14415; -. DR PRO; PR:P20701; -. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; P20701; -. DR CleanEx; HS_ITGAL; -. DR ExpressionAtlas; P20701; baseline and differential. DR Genevisible; P20701; HS. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl. DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0001772; C:immunological synapse; IEA:Ensembl. DR GO; GO:0034687; C:integrin alphaL-beta2 complex; IDA:UniProtKB. DR GO; GO:0008305; C:integrin complex; NAS:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0050798; P:activated T cell proliferation; IEA:Ensembl. DR GO; GO:0007596; P:blood coagulation; TAS:Reactome. DR GO; GO:0007155; P:cell adhesion; NAS:UniProtKB. DR GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB. DR GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome. 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; IEA:UniProtKB-KW. DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:BHF-UCL. DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome. DR GO; GO:0006928; P:movement of cell or subcellular component; TAS:ProtInc. DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IEA:Ensembl. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl. DR GO; GO:0043113; P:receptor clustering; IMP:UniProtKB. DR GO; GO:0050776; P:regulation of immune response; TAS:Reactome. 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 InterPro; IPR013517; FG-GAP. DR InterPro; IPR013519; Int_alpha_beta-p. DR InterPro; IPR000413; Integrin_alpha. DR InterPro; IPR013649; Integrin_alpha-2. DR InterPro; IPR018184; Integrin_alpha_C_CS. DR InterPro; IPR002035; VWF_A. DR Pfam; PF01839; FG-GAP; 1. DR Pfam; PF00357; Integrin_alpha; 1. DR Pfam; PF08441; Integrin_alpha2; 1. DR Pfam; PF00092; VWA; 1. DR PRINTS; PR01185; INTEGRINA. DR SMART; SM00191; Int_alpha; 5. DR SMART; SM00327; VWA; 1. DR SUPFAM; SSF53300; SSF53300; 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; KW Complete proteome; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Integrin; Magnesium; Membrane; Metal-binding; KW Polymorphism; Receptor; Reference proteome; Repeat; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1 25 FT CHAIN 26 1170 Integrin alpha-L. FT /FTId=PRO_0000016292. FT TOPO_DOM 26 1090 Extracellular. {ECO:0000255}. FT TRANSMEM 1091 1111 Helical. {ECO:0000255}. FT TOPO_DOM 1112 1170 Cytoplasmic. {ECO:0000255}. FT REPEAT 31 82 FG-GAP 1. FT REPEAT 83 141 FG-GAP 2. FT DOMAIN 156 327 VWFA. {ECO:0000255|PROSITE- FT ProRule:PRU00219}. FT REPEAT 338 389 FG-GAP 3. FT REPEAT 390 445 FG-GAP 4. FT REPEAT 446 506 FG-GAP 5. FT REPEAT 507 563 FG-GAP 6. FT REPEAT 567 627 FG-GAP 7. FT CA_BIND 468 476 {ECO:0000255}. FT CA_BIND 530 538 {ECO:0000255}. FT CA_BIND 590 598 {ECO:0000255}. FT MOTIF 1115 1119 GFFKR motif. FT CARBOHYD 65 65 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 89 89 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 188 188 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:19349973}. FT CARBOHYD 649 649 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 670 670 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 726 726 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 730 730 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 862 862 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 885 885 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 897 897 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 1060 1060 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 1071 1071 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 73 80 {ECO:0000250}. FT DISULFID 111 129 {ECO:0000250}. FT DISULFID 653 707 {ECO:0000250}. FT DISULFID 771 777 {ECO:0000250}. FT DISULFID 845 861 {ECO:0000250}. FT DISULFID 998 1013 {ECO:0000250}. FT DISULFID 1021 1052 {ECO:0000250}. FT VAR_SEQ 110 192 Missing (in isoform 3). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_042842. FT VAR_SEQ 746 746 Missing (in isoform 3). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_042843. FT VAR_SEQ 954 954 Q -> QGVHGLVEMQTSKQILCRPAGDAEHTVGAQEGELPC FT PWGVSEAFRDNIRAGPCR (in isoform 2). FT {ECO:0000305}. FT /FTId=VSP_002738. FT VARIANT 144 144 R -> H (in dbSNP:rs34166708). FT {ECO:0000269|Ref.2}. FT /FTId=VAR_025235. FT VARIANT 214 214 R -> W (in dbSNP:rs1064524). FT {ECO:0000269|PubMed:10493829, FT ECO:0000269|PubMed:2537322, FT ECO:0000269|Ref.2}. FT /FTId=VAR_025236. FT VARIANT 746 746 Q -> K (in dbSNP:rs34838942). FT {ECO:0000269|Ref.2}. FT /FTId=VAR_025237. FT VARIANT 791 791 R -> T (in dbSNP:rs2230433). FT {ECO:0000269|Ref.2}. FT /FTId=VAR_025238. FT CONFLICT 660 660 I -> Y (in Ref. 1; CAA68747). FT {ECO:0000305}. FT STRAND 155 162 {ECO:0000244|PDB:1MJN}. FT HELIX 169 185 {ECO:0000244|PDB:1MJN}. FT TURN 186 188 {ECO:0000244|PDB:1MJN}. FT STRAND 189 206 {ECO:0000244|PDB:1MJN}. FT HELIX 208 214 {ECO:0000244|PDB:1MJN}. FT HELIX 217 221 {ECO:0000244|PDB:1MJN}. FT HELIX 233 243 {ECO:0000244|PDB:1MJN}. FT HELIX 247 249 {ECO:0000244|PDB:1MJN}. FT STRAND 255 265 {ECO:0000244|PDB:1MJN}. FT HELIX 274 276 {ECO:0000244|PDB:1MJN}. FT STRAND 279 287 {ECO:0000244|PDB:1MJN}. FT HELIX 288 290 {ECO:0000244|PDB:1MJN}. FT HELIX 293 297 {ECO:0000244|PDB:1MJN}. FT HELIX 298 302 {ECO:0000244|PDB:1MJN}. FT HELIX 307 310 {ECO:0000244|PDB:1MJN}. FT STRAND 311 316 {ECO:0000244|PDB:1MJN}. FT HELIX 317 319 {ECO:0000244|PDB:1MJN}. FT HELIX 323 330 {ECO:0000244|PDB:1MJN}. FT STRAND 331 333 {ECO:0000244|PDB:3BQN}. FT TURN 1082 1086 {ECO:0000244|PDB:2M3E}. FT HELIX 1090 1114 {ECO:0000244|PDB:2M3E}. FT HELIX 1118 1123 {ECO:0000244|PDB:2K8O}. FT TURN 1124 1127 {ECO:0000244|PDB:2K8O}. FT HELIX 1137 1147 {ECO:0000244|PDB:2K8O}. FT HELIX 1153 1155 {ECO:0000244|PDB:2K8O}. FT HELIX 1156 1165 {ECO:0000244|PDB:2K8O}. FT HELIX 1167 1170 {ECO:0000244|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 //