ITA2_HUMAN
ID ITA2_HUMAN Reviewed; 1181 AA.
AC P17301; Q14595;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 232.
DE RecName: Full=Integrin alpha-2;
DE AltName: Full=CD49 antigen-like family member B;
DE AltName: Full=Collagen receptor;
DE AltName: Full=Platelet membrane glycoprotein Ia;
DE Short=GPIa;
DE AltName: Full=VLA-2 subunit alpha;
DE AltName: CD_antigen=CD49b;
DE Flags: Precursor;
GN Name=ITGA2; Synonyms=CD49B;
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], PROTEIN SEQUENCE OF 30-44, AND VARIANT LYS-534.
RC TISSUE=Endothelial cell;
RX PubMed=2545729; DOI=10.1083/jcb.109.1.397;
RA Takada Y., Hemler M.E.;
RT "The primary structure of the VLA-2/collagen receptor alpha 2 subunit
RT (platelet GPIa): homology to other integrins and the presence of a possible
RT collagen-binding domain.";
RL J. Cell Biol. 109:397-407(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-691 AND GLN-1127.
RG SeattleSNPs variation discovery resource;
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX PubMed=8276836; DOI=10.1016/s0021-9258(17)42373-8;
RA Zutter M.M., Santoro S.A., Painter A.S., Tsung Y.L., Gafford A.;
RT "The human alpha 2 integrin gene promoter. Identification of positive and
RT negative regulatory elements important for cell-type and developmentally
RT restricted gene expression.";
RL J. Biol. Chem. 269:463-469(1994).
RN [5]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN ECHOVIRUS 1 AND
RP HUMAN ECHOVIRUS 8 CAPSID PROTEINS.
RX PubMed=8411387; DOI=10.1128/jvi.67.11.6847-6852.1993;
RA Bergelson J.M., St John N., Kawaguchi S., Chan M., Stubdal H., Modlin J.,
RA Finberg R.W.;
RT "Infection by echoviruses 1 and 8 depends on the alpha 2 subunit of human
RT VLA-2.";
RL J. Virol. 67:6847-6852(1993).
RN [6]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ROTAVIRUS A VP4
RP PROTEIN.
RX PubMed=12941907; DOI=10.1128/jvi.77.18.9969-9978.2003;
RA Graham K.L., Halasz P., Tan Y., Hewish M.J., Takada Y., Mackow E.R.,
RA Robinson M.K., Coulson B.S.;
RT "Integrin-using rotaviruses bind alpha2beta1 integrin alpha2 I domain via
RT VP4 DGE sequence and recognize alphaXbeta2 and alphaVbeta3 by using VP7
RT during cell entry.";
RL J. Virol. 77:9969-9978(2003).
RN [7]
RP INTERACTION WITH RAB21, AND MUTAGENESIS OF PHE-1159; LYS-1160; ARG-1161;
RP LYS-1162; GLU-1164 AND LYS-1165.
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 [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-343.
RC TISSUE=Platelet;
RX PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200;
RA Lewandrowski U., Moebius J., Walter U., Sickmann A.;
RT "Elucidation of N-glycosylation sites on human platelet proteins: a
RT glycoproteomic approach.";
RL Mol. Cell. Proteomics 5:226-233(2006).
RN [9]
RP MUTAGENESIS OF LYS-1160; ARG-1161 AND LYS-1162.
RX PubMed=18804435; DOI=10.1016/j.devcel.2008.08.001;
RA Pellinen T., Tuomi S., Arjonen A., Wolf M., Edgren H., Meyer H., Grosse R.,
RA Kitzing T., Rantala J.K., Kallioniemi O., Faessler R., Kallio M.,
RA Ivaska J.;
RT "Integrin trafficking regulated by Rab21 is necessary for cytokinesis.";
RL Dev. Cell 15:371-385(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-343.
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 [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-343.
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 [14]
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 [15]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 168-368.
RX PubMed=9353312; DOI=10.1074/jbc.272.45.28512;
RA Emsley J., King S.L., Bergelson J.M., Liddington R.C.;
RT "Crystal structure of the I domain from integrin alpha2beta1.";
RL J. Biol. Chem. 272:28512-28517(1997).
RN [16]
RP VARIANT LYS-534, AND POLYMORPHISM.
RX PubMed=7901236; DOI=10.1172/jci116849;
RA Santoso S., Kalb R., Walka M., Kiefel V., Mueller-Eckhardt C., Newman P.J.;
RT "The human platelet alloantigens Br(a) and Brb are associated with a single
RT amino acid polymorphism on glycoprotein Ia (integrin subunit alpha 2).";
RL J. Clin. Invest. 92:2427-2432(1993).
RN [17]
RP VARIANT LYS-534, AND POLYMORPHISM.
RX PubMed=10744142;
RA Kroll H., Gardemann A., Fechter A., Haberbosch W., Santoso S.;
RT "The impact of the glycoprotein Ia collagen receptor subunit A1648G gene
RT polymorphism on coronary artery disease and acute myocardial infarction.";
RL Thromb. Haemost. 83:392-396(2000).
RN [18]
RP VARIANT LEU-532.
RX PubMed=23368983; DOI=10.1111/vox.12019;
RA Bertrand G., Jallu V., Beranger T., Bianchi F., Casale C., Dufour V.,
RA Chenet C., Quesne J., Martageix C., Kaplan C.;
RT "HPA-5 typing discrepancy reveals an Ile503Leu substitution in platelet
RT GPIa (alpha2 integrin).";
RL Vox Sang. 105:73-76(2013).
CC -!- FUNCTION: Integrin alpha-2/beta-1 is a receptor for laminin, collagen,
CC collagen C-propeptides, fibronectin and E-cadherin. It recognizes the
CC proline-hydroxylated sequence G-F-P-G-E-R in collagen. It is
CC responsible for adhesion of platelets and other cells to collagens,
CC modulation of collagen and collagenase gene expression, force
CC generation and organization of newly synthesized extracellular matrix.
CC -!- FUNCTION: (Microbial infection) Integrin ITGA2:ITGB1 acts as a receptor
CC for Human rotavirus A. {ECO:0000269|PubMed:12941907}.
CC -!- FUNCTION: (Microbial infection) Integrin ITGA2:ITGB1 acts as a receptor
CC for Human echoviruses 1 and 8. {ECO:0000269|PubMed:8411387}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-2 associates
CC with beta-1. Interacts with HPS5 and RAB21.
CC {ECO:0000269|PubMed:16754960}.
CC -!- SUBUNIT: (Microbial infection) Integrin ITGA2:ITGB1 interacts (via
CC ITAG2 I-domain) with rotavirus A VP4 protein.
CC {ECO:0000269|PubMed:12941907}.
CC -!- SUBUNIT: (Microbial infection) Integrin ITGA2:ITGB1 interacts with
CC human echoviruses 1 and 8 capsid proteins.
CC {ECO:0000269|PubMed:8411387}.
CC -!- INTERACTION:
CC P17301; P05556: ITGB1; NbExp=5; IntAct=EBI-702960, EBI-703066;
CC P17301; P35968: KDR; NbExp=2; IntAct=EBI-702960, EBI-1005487;
CC P17301; Q9H0F6: SHARPIN; NbExp=5; IntAct=EBI-702960, EBI-3942966;
CC P17301; P84092: Ap2m1; Xeno; NbExp=2; IntAct=EBI-702960, EBI-297693;
CC P17301; P35282: Rab21; Xeno; NbExp=7; IntAct=EBI-702960, EBI-1993555;
CC P17301; P04512; Xeno; NbExp=3; IntAct=EBI-702960, 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 -!- POLYMORPHISM: Position 534 is associated with platelet-specific
CC alloantigen HPA-5 (Br). HPA-5B/Br(a) has Lys-534 and HPA-5A/Br(b) has
CC Glu-534. HPA-5B is involved in neonatal alloimmune thrombocytopenia
CC (NAIT or NATP). The Lys-534-Glu polymorphism may play a role in
CC coronary artery disease (CAD). {ECO:0000269|PubMed:10744142,
CC ECO:0000269|PubMed:7901236}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/itga2/";
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DR EMBL; X17033; CAA34894.1; -; mRNA.
DR EMBL; AF512556; AAM34795.1; -; Genomic_DNA.
DR EMBL; L24121; AAA16619.2; -; Genomic_DNA.
DR CCDS; CCDS3957.1; -.
DR PIR; A33998; A33998.
DR RefSeq; NP_002194.2; NM_002203.3.
DR PDB; 1AOX; X-ray; 2.10 A; A/B=169-367.
DR PDB; 1DZI; X-ray; 2.10 A; A=172-355.
DR PDB; 1V7P; X-ray; 1.90 A; C=167-366.
DR PDB; 4BJ3; X-ray; 3.04 A; A/B=171-368.
DR PDB; 5HJ2; X-ray; 2.15 A; A/B/C/D/E/F=170-366.
DR PDB; 5THP; X-ray; 3.01 A; C/F/I/L/O/R=170-366.
DR PDB; 6ND8; X-ray; 2.90 A; C/F/I/L/O/R=170-366.
DR PDB; 6ND9; X-ray; 2.90 A; C/F/I/L/O/R=170-366.
DR PDB; 6NDA; X-ray; 3.15 A; C/F/I/L/O/R=170-366.
DR PDB; 6NDB; X-ray; 3.20 A; C/F/I/L/O/R=170-366.
DR PDB; 6NDC; X-ray; 3.35 A; C/F/I/L/O/R=170-366.
DR PDB; 6NDD; X-ray; 3.05 A; C/F/I/L/O/R=170-366.
DR PDB; 6NDE; X-ray; 3.50 A; C/F/I/L/O/R=170-366.
DR PDB; 6NDF; X-ray; 3.05 A; C/F/I/L/O/R=170-366.
DR PDB; 6NDG; X-ray; 3.15 A; C/F/I/L/O/R=170-366.
DR PDB; 6NDH; X-ray; 2.90 A; C/F/I/L/O/R=170-366.
DR PDBsum; 1AOX; -.
DR PDBsum; 1DZI; -.
DR PDBsum; 1V7P; -.
DR PDBsum; 4BJ3; -.
DR PDBsum; 5HJ2; -.
DR PDBsum; 5THP; -.
DR PDBsum; 6ND8; -.
DR PDBsum; 6ND9; -.
DR PDBsum; 6NDA; -.
DR PDBsum; 6NDB; -.
DR PDBsum; 6NDC; -.
DR PDBsum; 6NDD; -.
DR PDBsum; 6NDE; -.
DR PDBsum; 6NDF; -.
DR PDBsum; 6NDG; -.
DR PDBsum; 6NDH; -.
DR AlphaFoldDB; P17301; -.
DR BMRB; P17301; -.
DR BioGRID; 109880; 125.
DR ComplexPortal; CPX-1801; Integrin alpha2-beta1 complex.
DR CORUM; P17301; -.
DR DIP; DIP-67N; -.
DR IntAct; P17301; 42.
DR MINT; P17301; -.
DR STRING; 9606.ENSP00000296585; -.
DR BindingDB; P17301; -.
DR ChEMBL; CHEMBL4998; -.
DR GuidetoPHARMACOLOGY; 2440; -.
DR GlyConnect; 1406; 29 N-Linked glycans (6 sites).
DR GlyGen; P17301; 10 sites, 33 N-linked glycans (6 sites).
DR iPTMnet; P17301; -.
DR PhosphoSitePlus; P17301; -.
DR SwissPalm; P17301; -.
DR BioMuta; ITGA2; -.
DR DMDM; 124942; -.
DR EPD; P17301; -.
DR jPOST; P17301; -.
DR MassIVE; P17301; -.
DR MaxQB; P17301; -.
DR PaxDb; P17301; -.
DR PeptideAtlas; P17301; -.
DR PRIDE; P17301; -.
DR ProteomicsDB; 53466; -.
DR ABCD; P17301; 8 sequenced antibodies.
DR Antibodypedia; 10993; 1421 antibodies from 47 providers.
DR DNASU; 3673; -.
DR Ensembl; ENST00000296585.10; ENSP00000296585.5; ENSG00000164171.11.
DR GeneID; 3673; -.
DR KEGG; hsa:3673; -.
DR MANE-Select; ENST00000296585.10; ENSP00000296585.5; NM_002203.4; NP_002194.2.
DR UCSC; uc003joy.3; human.
DR CTD; 3673; -.
DR DisGeNET; 3673; -.
DR GeneCards; ITGA2; -.
DR HGNC; HGNC:6137; ITGA2.
DR HPA; ENSG00000164171; Low tissue specificity.
DR MalaCards; ITGA2; -.
DR MIM; 192974; gene+phenotype.
DR neXtProt; NX_P17301; -.
DR OpenTargets; ENSG00000164171; -.
DR Orphanet; 853; Fetal and neonatal alloimmune thrombocytopenia.
DR PharmGKB; PA204; -.
DR VEuPathDB; HostDB:ENSG00000164171; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000156303; -.
DR InParanoid; P17301; -.
DR OrthoDB; 66046at2759; -.
DR PhylomeDB; P17301; -.
DR TreeFam; TF105391; -.
DR PathwayCommons; P17301; -.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-3000157; Laminin interactions.
DR Reactome; R-HSA-3000170; Syndecan interactions.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR Reactome; R-HSA-447041; CHL1 interactions.
DR Reactome; R-HSA-75892; Platelet Adhesion to exposed collagen.
DR Reactome; R-HSA-8874081; MET activates PTK2 signaling.
DR SignaLink; P17301; -.
DR SIGNOR; P17301; -.
DR BioGRID-ORCS; 3673; 4 hits in 1074 CRISPR screens.
DR ChiTaRS; ITGA2; human.
DR EvolutionaryTrace; P17301; -.
DR GeneWiki; CD49b; -.
DR GenomeRNAi; 3673; -.
DR Pharos; P17301; Tbio.
DR PRO; PR:P17301; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P17301; protein.
DR Bgee; ENSG00000164171; Expressed in ventricular zone and 157 other tissues.
DR ExpressionAtlas; P17301; baseline and differential.
DR Genevisible; P17301; HS.
DR GO; GO:0043679; C:axon terminus; 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:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0034666; C:integrin alpha2-beta1 complex; IDA:UniProtKB.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0001540; F:amyloid-beta binding; ISS:ARUK-UCL.
DR GO; GO:0005518; F:collagen binding; IMP:UniProtKB.
DR GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; IMP:UniProtKB.
DR GO; GO:0038064; F:collagen receptor activity; IMP:UniProtKB.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; TAS:ARUK-UCL.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0043236; F:laminin binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:UniProtKB.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
DR GO; GO:0007596; P:blood coagulation; TAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IMP:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:UniProtKB.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0038065; P:collagen-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IEA:Ensembl.
DR GO; GO:0045184; P:establishment of protein localization; IEA:Ensembl.
DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR GO; GO:0048041; P:focal adhesion assembly; IEA:Ensembl.
DR GO; GO:0070365; P:hepatocyte differentiation; IEA:Ensembl.
DR GO; GO:0006971; P:hypotonic response; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0030879; P:mammary gland development; IEA:Ensembl.
DR GO; GO:0048333; P:mesodermal cell differentiation; IEP:UniProtKB.
DR GO; GO:0010694; P:positive regulation of alkaline phosphatase activity; IEA:Ensembl.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl.
DR GO; GO:0031346; P:positive regulation of cell projection organization; IEA:Ensembl.
DR GO; GO:0033343; P:positive regulation of collagen binding; IEA:Ensembl.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IEA:Ensembl.
DR GO; GO:0043388; P:positive regulation of DNA binding; IEA:Ensembl.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; IEA:Ensembl.
DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IEA:Ensembl.
DR GO; GO:0050927; P:positive regulation of positive chemotaxis; IEA:Ensembl.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IEA:Ensembl.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IEA:Ensembl.
DR GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
DR GO; GO:0051971; P:positive regulation of transmission of nerve impulse; IEA:Ensembl.
DR GO; GO:0014075; P:response to amine; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0033591; P:response to L-ascorbic acid; IEA:Ensembl.
DR GO; GO:0014850; P:response to muscle activity; IEA:Ensembl.
DR GO; GO:0071107; P:response to parathyroid hormone; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0043589; P:skin morphogenesis; IEA:Ensembl.
DR GO; GO:0006929; P:substrate-dependent cell migration; IMP:UniProtKB.
DR Gene3D; 2.130.10.130; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
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; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01839; FG-GAP; 2.
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 SUPFAM; SSF69179; SSF69179; 3.
DR SUPFAM; SSF69318; SSF69318; 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; Calcium; Cell adhesion; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Host cell receptor for virus entry;
KW Host-virus interaction; Integrin; Magnesium; Membrane; Metal-binding;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:2545729"
FT CHAIN 30..1181
FT /note="Integrin alpha-2"
FT /id="PRO_0000016233"
FT TOPO_DOM 30..1132
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1133..1154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1155..1181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 34..92
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 101..161
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT DOMAIN 188..365
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REPEAT 366..420
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 423..475
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 477..539
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 540..598
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 602..664
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REGION 1155..1161
FT /note="Interaction with HPS5"
FT MOTIF 1157..1161
FT /note="GFFKR motif"
FT BINDING 499
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 501
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 503
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 507
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 563
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 565
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 567
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 571
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 627
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 629
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 631
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 635
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16263699,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 699
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1057
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1074
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1081
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 83..92
FT /evidence="ECO:0000250"
FT DISULFID 680..737
FT /evidence="ECO:0000250"
FT DISULFID 789..795
FT /evidence="ECO:0000250"
FT DISULFID 865..876
FT /evidence="ECO:0000250"
FT DISULFID 1019..1050
FT /evidence="ECO:0000250"
FT DISULFID 1055..1060
FT /evidence="ECO:0000250"
FT VARIANT 532
FT /note="I -> L (in dbSNP:rs199808499)"
FT /evidence="ECO:0000269|PubMed:23368983"
FT /id="VAR_076939"
FT VARIANT 534
FT /note="E -> K (in alloantigen HPA-5B; dbSNP:rs1801106)"
FT /evidence="ECO:0000269|PubMed:10744142,
FT ECO:0000269|PubMed:2545729, ECO:0000269|PubMed:7901236"
FT /id="VAR_003977"
FT VARIANT 691
FT /note="N -> K (in dbSNP:rs3212557)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_029146"
FT VARIANT 927
FT /note="N -> S (in dbSNP:rs2287870)"
FT /id="VAR_021855"
FT VARIANT 1127
FT /note="K -> Q (in dbSNP:rs3212645)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_020036"
FT MUTAGEN 1159
FT /note="F->A: No significant reduction of RAB21-binding by
FT co-immunoprecipitation assay; when associated with A-1160
FT and A-1162."
FT /evidence="ECO:0000269|PubMed:16754960"
FT MUTAGEN 1160
FT /note="K->A: No effect on RAB21-binding. Significant
FT reduction of RAB21-binding; when associated with A-1161.
FT Shows defective cytokinesis on collagen, but not on
FT fibronectin; when associated with A-1161."
FT /evidence="ECO:0000269|PubMed:16754960,
FT ECO:0000269|PubMed:18804435"
FT MUTAGEN 1161
FT /note="R->A: Significant reduction of RAB21-binding; when
FT associated with A-1160. Shows defective cytokinesis on
FT collagen, but not on fibronectin; when associated with A-
FT 1160."
FT /evidence="ECO:0000269|PubMed:16754960,
FT ECO:0000269|PubMed:18804435"
FT MUTAGEN 1162
FT /note="K->A: No significant reduction of RAB21-binding by
FT co-immunoprecipitation assay; when associated with A-1159
FT and A-1160."
FT /evidence="ECO:0000269|PubMed:16754960,
FT ECO:0000269|PubMed:18804435"
FT MUTAGEN 1162
FT /note="K->P: Markedly weakens RAB21-binding. Shows
FT defective cytokinesis on collagen, but not on fibronectin."
FT /evidence="ECO:0000269|PubMed:16754960,
FT ECO:0000269|PubMed:18804435"
FT MUTAGEN 1164
FT /note="E->A: Significant reduction of RAB21-binding; when
FT associated with A-1160; A-1161 and A-1165."
FT /evidence="ECO:0000269|PubMed:16754960"
FT MUTAGEN 1165
FT /note="K->A: Significant reduction of RAB21-binding; when
FT associated with A-1160; A-1161 and A-1164."
FT /evidence="ECO:0000269|PubMed:16754960"
FT CONFLICT 17
FT /note="L -> V (in Ref. 3; AAA16619)"
FT /evidence="ECO:0000305"
FT STRAND 173..180
FT /evidence="ECO:0007829|PDB:1V7P"
FT HELIX 188..200
FT /evidence="ECO:0007829|PDB:1V7P"
FT STRAND 208..224
FT /evidence="ECO:0007829|PDB:1V7P"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:1V7P"
FT HELIX 232..241
FT /evidence="ECO:0007829|PDB:1V7P"
FT HELIX 252..262
FT /evidence="ECO:0007829|PDB:1V7P"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:1V7P"
FT STRAND 274..284
FT /evidence="ECO:0007829|PDB:1V7P"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:1V7P"
FT HELIX 292..301
FT /evidence="ECO:0007829|PDB:1V7P"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:1V7P"
FT HELIX 313..317
FT /evidence="ECO:0007829|PDB:1V7P"
FT HELIX 323..332
FT /evidence="ECO:0007829|PDB:1V7P"
FT HELIX 337..340
FT /evidence="ECO:0007829|PDB:1V7P"
FT STRAND 341..347
FT /evidence="ECO:0007829|PDB:1V7P"
FT HELIX 348..353
FT /evidence="ECO:0007829|PDB:1V7P"
FT HELIX 354..362
FT /evidence="ECO:0007829|PDB:1V7P"
SQ SEQUENCE 1181 AA; 129296 MW; 06DD2DE59EAB39ED CRC64;
MGPERTGAAP LPLLLVLALS QGILNCCLAY NVGLPEAKIF SGPSSEQFGY AVQQFINPKG
NWLLVGSPWS GFPENRMGDV YKCPVDLSTA TCEKLNLQTS TSIPNVTEMK TNMSLGLILT
RNMGTGGFLT CGPLWAQQCG NQYYTTGVCS DISPDFQLSA SFSPATQPCP SLIDVVVVCD
ESNSIYPWDA VKNFLEKFVQ GLDIGPTKTQ VGLIQYANNP RVVFNLNTYK TKEEMIVATS
QTSQYGGDLT NTFGAIQYAR KYAYSAASGG RRSATKVMVV VTDGESHDGS MLKAVIDQCN
HDNILRFGIA VLGYLNRNAL DTKNLIKEIK AIASIPTERY FFNVSDEAAL LEKAGTLGEQ
IFSIEGTVQG GDNFQMEMSQ VGFSADYSSQ NDILMLGAVG AFGWSGTIVQ KTSHGHLIFP
KQAFDQILQD RNHSSYLGYS VAAISTGEST HFVAGAPRAN YTGQIVLYSV NENGNITVIQ
AHRGDQIGSY FGSVLCSVDV DKDTITDVLL VGAPMYMSDL KKEEGRVYLF TIKEGILGQH
QFLEGPEGIE NTRFGSAIAA LSDINMDGFN DVIVGSPLEN QNSGAVYIYN GHQGTIRTKY
SQKILGSDGA FRSHLQYFGR SLDGYGDLNG DSITDVSIGA FGQVVQLWSQ SIADVAIEAS
FTPEKITLVN KNAQIILKLC FSAKFRPTKQ NNQVAIVYNI TLDADGFSSR VTSRGLFKEN
NERCLQKNMV VNQAQSCPEH IIYIQEPSDV VNSLDLRVDI SLENPGTSPA LEAYSETAKV
FSIPFHKDCG EDGLCISDLV LDVRQIPAAQ EQPFIVSNQN KRLTFSVTLK NKRESAYNTG
IVVDFSENLF FASFSLPVDG TEVTCQVAAS QKSVACDVGY PALKREQQVT FTINFDFNLQ
NLQNQASLSF QALSESQEEN KADNLVNLKI PLLYDAEIHL TRSTNINFYE ISSDGNVPSI
VHSFEDVGPK FIFSLKVTTG SVPVSMATVI IHIPQYTKEK NPLMYLTGVQ TDKAGDISCN
ADINPLKIGQ TSSSVSFKSE NFRHTKELNC RTASCSNVTC WLKDVHMKGE YFVNVTTRIW
NGTFASSTFQ TVQLTAAAEI NTYNPEIYVI EDNTVTIPLM IMKPDEKAEV PTGVIIGSII
AGILLLLALV AILWKLGFFK RKYEKMTKNP DEIDETTELS S
