ID ITA1_HUMAN Reviewed; 1179 AA. AC P56199; B2RNU0; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 213. DE RecName: Full=Integrin alpha-1; DE AltName: Full=CD49 antigen-like family member A; DE AltName: Full=Laminin and collagen receptor; DE AltName: Full=VLA-1; DE AltName: CD_antigen=CD49a; DE Flags: Precursor; GN Name=ITGA1; 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=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 29-1179. RX PubMed=8428973; DOI=10.1016/s0021-9258(18)53871-0; RA Briesewitz R., Epstein M.R., Marcantonio E.E.; RT "Expression of native and truncated forms of the human integrin alpha 1 RT subunit."; RL J. Biol. Chem. 268:2989-2996(1993). RN [4] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-532. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [5] RP FUNCTION IN EGFR SIGNALING, AND INTERACTION WITH PTPN2. RX PubMed=15592458; DOI=10.1038/ncb1209; RA Mattila E., Pellinen T., Nevo J., Vuoriluoto K., Arjonen A., Ivaska J.; RT "Negative regulation of EGFR signalling through integrin-alpha1beta1- RT mediated activation of protein tyrosine phosphatase TCPTP."; RL Nat. Cell Biol. 7:78-85(2005). RN [6] RP INTERACTION WITH RAB21. RX PubMed=16754960; DOI=10.1083/jcb.200509019; RA Pellinen T., Arjonen A., Vuoriluoto K., Kallio K., Fransen J.A.M., RA Ivaska J.; RT "Small GTPase Rab21 regulates cell adhesion and controls endosomal traffic RT of beta1-integrins."; RL J. Cell Biol. 173:767-780(2006). RN [7] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-100; ASN-105; ASN-217; ASN-341; RP ASN-418; ASN-460; ASN-532; ASN-780; ASN-840; ASN-966; ASN-974 AND ASN-1008. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [9] 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 [10] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 168-359. RX PubMed=10455165; DOI=10.1074/jbc.274.35.24906; RA Rich R.L., Deivanayagam C.C., Owens R.T., Carson M., Hook A., Moore D., RA Symersky J., Yang V.W., Narayana S.V., Hook M.; RT "Trench-shaped binding sites promote multiple classes of interactions RT between collagen and the adherence receptors, alpha(1)beta(1) integrin and RT Staphylococcus aureus cna MSCRAMM."; RL J. Biol. Chem. 274:24906-24913(1999). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 166-356. RX PubMed=14660600; DOI=10.1074/jbc.m312912200; RA Nymalm Y., Puranen J.S., Nyholm T.K., Kapyla J., Kidron H., RA Pentikainen O.T., Airenne T.T., Heino J., Slotte J.P., Johnson M.S., RA Salminen T.A.; RT "Jararhagin-derived RKKH peptides induce structural changes in alpha1I RT domain of human integrin alpha1beta1."; RL J. Biol. Chem. 279:7962-7970(2004). CC -!- FUNCTION: Integrin alpha-1/beta-1 is a receptor for laminin and CC collagen. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R CC in collagen. Involved in anchorage-dependent, negative regulation of CC EGF-stimulated cell growth. {ECO:0000269|PubMed:15592458}. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-1 associates CC with beta-1. Interacts with RAB21. Interacts (via cytoplasmic domain) CC with PTPN2; activates PTPN2 phosphatase activity towards EGFR and CC negatively regulates EGF signaling. {ECO:0000269|PubMed:15592458, CC ECO:0000269|PubMed:16754960}. CC -!- INTERACTION: CC P56199; P04512; Xeno; NbExp=2; IntAct=EBI-2554465, EBI-15711650; CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. CC -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with CC I-domains do not undergo protease cleavage. CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {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; AC027326; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC022133; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC025180; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC137121; AAI37122.1; -; mRNA. DR EMBL; BC137122; AAI37123.1; -; mRNA. DR EMBL; X68742; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS3955.1; -. DR PIR; A45226; A45226. DR RefSeq; NP_852478.1; NM_181501.1. DR PDB; 1PT6; X-ray; 1.87 A; A/B=166-366. DR PDB; 1QC5; X-ray; 2.00 A; A/B=168-359. DR PDB; 1QCY; X-ray; 2.30 A; A=169-361. DR PDB; 2L8S; NMR; -; A=1135-1179. DR PDB; 2M32; NMR; -; A=168-359. DR PDB; 4A0Q; X-ray; 1.90 A; A/B=166-366. DR PDB; 5HGJ; X-ray; 1.40 A; A/B=170-364. DR PDBsum; 1PT6; -. DR PDBsum; 1QC5; -. DR PDBsum; 1QCY; -. DR PDBsum; 2L8S; -. DR PDBsum; 2M32; -. DR PDBsum; 4A0Q; -. DR PDBsum; 5HGJ; -. DR AlphaFoldDB; P56199; -. DR BMRB; P56199; -. DR SMR; P56199; -. DR BioGRID; 109879; 45. DR ComplexPortal; CPX-1798; Integrin alpha1-beta1 complex. DR CORUM; P56199; -. DR DIP; DIP-206N; -. DR IntAct; P56199; 22. DR MINT; P56199; -. DR STRING; 9606.ENSP00000282588; -. DR BindingDB; P56199; -. DR ChEMBL; CHEMBL3682; -. DR GuidetoPHARMACOLOGY; 2437; -. DR TCDB; 8.A.54.1.1; the integrin (integrin) family. DR GlyConnect; 1405; 8 N-Linked glycans (4 sites). DR GlyCosmos; P56199; 26 sites, 7 glycans. DR GlyGen; P56199; 27 sites, 7 N-linked glycans (4 sites), 1 O-linked glycan (1 site). DR iPTMnet; P56199; -. DR PhosphoSitePlus; P56199; -. DR BioMuta; ITGA1; -. DR DMDM; 124056463; -. DR CPTAC; CPTAC-1614; -. DR EPD; P56199; -. DR jPOST; P56199; -. DR MassIVE; P56199; -. DR MaxQB; P56199; -. DR PaxDb; 9606-ENSP00000282588; -. DR PeptideAtlas; P56199; -. DR ProteomicsDB; 56903; -. DR Pumba; P56199; -. DR ABCD; P56199; 9 sequenced antibodies. DR Antibodypedia; 10955; 652 antibodies from 38 providers. DR DNASU; 3672; -. DR Ensembl; ENST00000282588.7; ENSP00000282588.5; ENSG00000213949.10. DR GeneID; 3672; -. DR KEGG; hsa:3672; -. DR MANE-Select; ENST00000282588.7; ENSP00000282588.5; NM_181501.2; NP_852478.1. DR UCSC; uc003jou.4; human. DR AGR; HGNC:6134; -. DR CTD; 3672; -. DR DisGeNET; 3672; -. DR GeneCards; ITGA1; -. DR HGNC; HGNC:6134; ITGA1. DR HPA; ENSG00000213949; Tissue enhanced (intestine). DR MIM; 192968; gene. DR neXtProt; NX_P56199; -. DR OpenTargets; ENSG00000213949; -. DR PharmGKB; PA29935; -. DR VEuPathDB; HostDB:ENSG00000213949; -. DR eggNOG; KOG3637; Eukaryota. DR GeneTree; ENSGT00940000157646; -. DR HOGENOM; CLU_004111_2_1_1; -. DR InParanoid; P56199; -. DR OMA; THTFLAI; -. DR OrthoDB; 3816176at2759; -. DR PhylomeDB; P56199; -. DR TreeFam; TF105391; -. DR PathwayCommons; P56199; -. DR Reactome; R-HSA-216083; Integrin cell surface interactions. DR Reactome; R-HSA-3000157; Laminin interactions. DR Reactome; R-HSA-416700; Other semaphorin interactions. DR Reactome; R-HSA-445355; Smooth Muscle Contraction. DR Reactome; R-HSA-447041; CHL1 interactions. DR Reactome; R-HSA-75892; Platelet Adhesion to exposed collagen. DR SignaLink; P56199; -. DR SIGNOR; P56199; -. DR BioGRID-ORCS; 3672; 15 hits in 1153 CRISPR screens. DR ChiTaRS; ITGA1; human. DR EvolutionaryTrace; P56199; -. DR GeneWiki; CD49a; -. DR GenomeRNAi; 3672; -. DR Pharos; P56199; Tbio. DR PRO; PR:P56199; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; P56199; Protein. DR Bgee; ENSG00000213949; Expressed in calcaneal tendon and 184 other cell types or tissues. DR ExpressionAtlas; P56199; baseline and differential. DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl. DR GO; GO:0045178; C:basal part of cell; IEA:Ensembl. 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:0005925; C:focal adhesion; IDA:UniProtKB. DR GO; GO:0034665; C:integrin alpha1-beta1 complex; IDA:UniProtKB. DR GO; GO:0008305; C:integrin complex; IBA:GO_Central. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0043204; C:perikaryon; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0005518; F:collagen binding; TAS:UniProtKB. DR GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; 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:0019903; F:protein phosphatase binding; IPI:UniProtKB. DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central. DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central. DR GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB. DR GO; GO:0045123; P:cellular extravasation; IEA:Ensembl. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB. DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl. DR GO; GO:0030593; P:neutrophil chemotaxis; IEA:Ensembl. DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl. DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl. DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IDA:UniProtKB. DR GO; GO:0042311; P:vasodilation; IEA:Ensembl. DR CDD; cd01469; vWA_integrins_alpha_subunit; 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; 1. 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 Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 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; IPR048286; Integrin_alpha_Ig-like_3. 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:SF22; INTEGRIN ALPHA-1; 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; PF20806; Integrin_A_Ig_3; 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; 3. 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; P56199; HS. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Cell adhesion; Disulfide bond; Glycoprotein; KW Integrin; Magnesium; Membrane; Metal-binding; Receptor; Reference proteome; KW Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..28 FT /evidence="ECO:0000255" FT CHAIN 29..1179 FT /note="Integrin alpha-1" FT /id="PRO_0000174215" FT TOPO_DOM 29..1141 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1142..1164 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1165..1179 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REPEAT 30..91 FT /note="FG-GAP 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 101..160 FT /note="FG-GAP 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT DOMAIN 161..360 FT /note="VWFA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT REPEAT 365..417 FT /note="FG-GAP 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 422..475 FT /note="FG-GAP 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 476..538 FT /note="FG-GAP 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 557..615 FT /note="FG-GAP 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 619..679 FT /note="FG-GAP 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT MOTIF 1167..1171 FT /note="GFFKR motif" FT BINDING 498 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 500 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 502 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 506 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 580 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 582 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 584 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 588 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 642 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 644 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 646 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 650 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P08648" FT CARBOHYD 74 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 100 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 105 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 112 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 217 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 317 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 341 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 402 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 418 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 460 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 532 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 699 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 748 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 780 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 840 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 883 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 908 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 915 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 939 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 966 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 974 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 1008 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 1073 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1083 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1102 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1113 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 82..92 FT /evidence="ECO:0000250" FT DISULFID 688..697 FT /evidence="ECO:0000250" FT DISULFID 703..756 FT /evidence="ECO:0000250" FT DISULFID 808..814 FT /evidence="ECO:0000250" FT DISULFID 878..886 FT /evidence="ECO:0000250" FT DISULFID 1030..1062 FT /evidence="ECO:0000250" FT DISULFID 1065..1072 FT /evidence="ECO:0000250" FT VARIANT 480 FT /note="T -> M (in dbSNP:rs4145748)" FT /id="VAR_034022" FT VARIANT 670 FT /note="V -> I (in dbSNP:rs2279587)" FT /id="VAR_049630" FT VARIANT 961 FT /note="I -> M (in dbSNP:rs12520591)" FT /id="VAR_034023" FT VARIANT 1108 FT /note="E -> G (in dbSNP:rs988574)" FT /id="VAR_034024" FT CONFLICT 198 FT /note="E -> K (in Ref. 3)" FT /evidence="ECO:0000305" FT CONFLICT 254 FT /note="I -> T (in Ref. 3)" FT /evidence="ECO:0000305" FT CONFLICT 705 FT /note="D -> E (in Ref. 3)" FT /evidence="ECO:0000305" FT STRAND 171..178 FT /evidence="ECO:0007829|PDB:5HGJ" FT HELIX 187..197 FT /evidence="ECO:0007829|PDB:5HGJ" FT STRAND 206..222 FT /evidence="ECO:0007829|PDB:5HGJ" FT TURN 224..226 FT /evidence="ECO:0007829|PDB:1PT6" FT HELIX 230..238 FT /evidence="ECO:0007829|PDB:5HGJ" FT HELIX 250..259 FT /evidence="ECO:0007829|PDB:5HGJ" FT TURN 260..262 FT /evidence="ECO:0007829|PDB:5HGJ" FT HELIX 264..266 FT /evidence="ECO:0007829|PDB:5HGJ" FT STRAND 272..282 FT /evidence="ECO:0007829|PDB:5HGJ" FT HELIX 287..289 FT /evidence="ECO:0007829|PDB:5HGJ" FT HELIX 290..299 FT /evidence="ECO:0007829|PDB:5HGJ" FT STRAND 302..309 FT /evidence="ECO:0007829|PDB:5HGJ" FT HELIX 311..315 FT /evidence="ECO:0007829|PDB:5HGJ" FT HELIX 321..330 FT /evidence="ECO:0007829|PDB:5HGJ" FT HELIX 335..338 FT /evidence="ECO:0007829|PDB:5HGJ" FT STRAND 339..344 FT /evidence="ECO:0007829|PDB:5HGJ" FT HELIX 345..351 FT /evidence="ECO:0007829|PDB:5HGJ" FT HELIX 352..359 FT /evidence="ECO:0007829|PDB:5HGJ" FT HELIX 1143..1168 FT /evidence="ECO:0007829|PDB:2L8S" SQ SEQUENCE 1179 AA; 130848 MW; 1A86F30FD916C845 CRC64; MAPRPRARPG VAVACCWLLT VVLRCCVSFN VDVKNSMTFS GPVEDMFGYT VQQYENEEGK WVLIGSPLVG QPKNRTGDVY KCPVGRGESL PCVKLDLPVN TSIPNVTEVK ENMTFGSTLV TNPNGGFLAC GPLYAYRCGH LHYTTGICSD VSPTFQVVNS IAPVQECSTQ LDIVIVLDGS NSIYPWDSVT AFLNDLLERM DIGPKQTQVG IVQYGENVTH EFNLNKYSST EEVLVAAKKI VQRGGRQTMT ALGIDTARKE AFTEARGARR GVKKVMVIVT DGESHDNHRL KKVIQDCEDE NIQRFSIAIL GSYNRGNLST EKFVEEIKSI ASEPTEKHFF NVSDELALVT IVKTLGERIF ALEATADQSA ASFEMEMSQT GFSAHYSQDW VMLGAVGAYD WNGTVVMQKA SQIIIPRNTT FNVESTKKNE PLASYLGYTV NSATASSGDV LYIAGQPRYN HTGQVIIYRM EDGNIKILQT LSGEQIGSYF GSILTTTDID KDSNTDILLV GAPMYMGTEK EEQGKVYVYA LNQTRFEYQM SLEPIKQTCC SSRQHNSCTT ENKNEPCGAR FGTAIAAVKD LNLDGFNDIV IGAPLEDDHG GAVYIYHGSG KTIRKEYAQR IPSGGDGKTL KFFGQSIHGE MDLNGDGLTD VTIGGLGGAA LFWSRDVAVV KVTMNFEPNK VNIQKKNCHM EGKETVCINA TVCFDVKLKS KEDTIYEADL QYRVTLDSLR QISRSFFSGT QERKVQRNIT VRKSECTKHS FYMLDKHDFQ DSVRITLDFN LTDPENGPVL DDSLPNSVHE YIPFAKDCGN KEKCISDLSL HVATTEKDLL IVRSQNDKFN VSLTVKNTKD SAYNTRTIVH YSPNLVFSGI EAIQKDSCES NHNITCKVGY PFLRRGEMVT FKILFQFNTS YLMENVTIYL SATSDSEEPP ETLSDNVVNI SIPVKYEVGL QFYSSASEYH ISIAANETVP EVINSTEDIG NEINIFYLIR KSGSFPMPEL KLSISFPNMT SNGYPVLYPT GLSSSENANC RPHIFEDPFS INSGKKMTTS TDHLKRGTIL DCNTCKFATI TCNLTSSDIS QVNVSLILWK PTFIKSYFSS LNLTIRGELR SENASLVLSS SNQKRELAIQ ISKDGLPGRV PLWVILLSAF AGLLLLMLLI LALWKIGFFK RPLKKKMEK //