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   27-MAR-2024, entry version 241.
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   SMR; P17301; -.
DR   BioGRID; 109880; 130.
DR   ComplexPortal; CPX-1801; Integrin alpha2-beta1 complex.
DR   CORUM; P17301; -.
DR   DIP; DIP-67N; -.
DR   IntAct; P17301; 44.
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   GlyCosmos; P17301; 10 sites, 33 glycans.
DR   GlyGen; P17301; 11 sites, 33 N-linked glycans (6 sites), 1 O-linked glycan (1 site).
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; 9606-ENSP00000296585; -.
DR   PeptideAtlas; P17301; -.
DR   ProteomicsDB; 53466; -.
DR   Pumba; P17301; -.
DR   ABCD; P17301; 8 sequenced antibodies.
DR   Antibodypedia; 10993; 1594 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   AGR; HGNC:6137; -.
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   OMA; IQYASQW; -.
DR   OrthoDB; 3816176at2759; -.
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; 5 hits in 1152 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 159 other cell types or tissues.
DR   ExpressionAtlas; P17301; baseline and differential.
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: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: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: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: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:0032967; P:positive regulation of collagen biosynthetic process; IEA:Ensembl.
DR   GO; GO:0010634; P:positive regulation of epithelial cell migration; 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   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; 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:SF23; INTEGRIN ALPHA-2; 1.
DR   Pfam; PF01839; FG-GAP; 2.
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; P17301; HS.
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
FT                   A-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
//