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Integrin alpha-2 (CD49 antigen-like family member B) (Collagen receptor) (Platelet membrane glycoprotein Ia) (GPIa) (VLA-2 subunit alpha) (CD antigen CD49b)

 ITA2_HUMAN              Reviewed;        1181 AA.
P17301; Q14595;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 1.
22-NOV-2017, entry version 202.
RecName: Full=Integrin alpha-2;
AltName: Full=CD49 antigen-like family member B;
AltName: Full=Collagen receptor;
AltName: Full=Platelet membrane glycoprotein Ia;
Short=GPIa;
AltName: Full=VLA-2 subunit alpha;
AltName: CD_antigen=CD49b;
Flags: Precursor;
Name=ITGA2; Synonyms=CD49B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 30-44.
TISSUE=Endothelial cell;
PubMed=2545729; DOI=10.1083/jcb.109.1.397;
Takada Y., Hemler M.E.;
"The primary structure of the VLA-2/collagen receptor alpha 2 subunit
(platelet GPIa): homology to other integrins and the presence of a
possible collagen-binding domain.";
J. Cell Biol. 109:397-407(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-691 AND GLN-1127.
SeattleSNPs variation discovery resource;
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-534.
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
PubMed=8276836;
Zutter M.M., Santoro S.A., Painter A.S., Tsung Y.L., Gafford A.;
"The human alpha 2 integrin gene promoter. Identification of positive
and negative regulatory elements important for cell-type and
developmentally restricted gene expression.";
J. Biol. Chem. 269:463-469(1994).
[5]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN ECHOVIRUS 1
AND HUMAN ECHOVIRUS 8 CAPSID PROTEINS.
PubMed=8411387;
Bergelson J.M., St John N., Kawaguchi S., Chan M., Stubdal H.,
Modlin J., Finberg R.W.;
"Infection by echoviruses 1 and 8 depends on the alpha 2 subunit of
human VLA-2.";
J. Virol. 67:6847-6852(1993).
[6]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ROTAVIRUS A VP4
PROTEIN.
PubMed=12941907; DOI=10.1128/JVI.77.18.9969-9978.2003;
Graham K.L., Halasz P., Tan Y., Hewish M.J., Takada Y., Mackow E.R.,
Robinson M.K., Coulson B.S.;
"Integrin-using rotaviruses bind alpha2beta1 integrin alpha2 I domain
via VP4 DGE sequence and recognize alphaXbeta2 and alphaVbeta3 by
using VP7 during cell entry.";
J. Virol. 77:9969-9978(2003).
[7]
INTERACTION WITH RAB21, AND MUTAGENESIS OF PHE-1159; LYS-1160;
ARG-1161; LYS-1162; GLU-1164 AND LYS-1165.
PubMed=16754960; DOI=10.1083/jcb.200509019;
Pellinen T., Arjonen A., Vuoriluoto K., Kallio K., Fransen J.A.M.,
Ivaska J.;
"Small GTPase Rab21 regulates cell adhesion and controls endosomal
traffic of beta1-integrins.";
J. Cell Biol. 173:767-780(2006).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-343.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[9]
MUTAGENESIS OF LYS-1160; ARG-1161 AND LYS-1162.
PubMed=18804435; DOI=10.1016/j.devcel.2008.08.001;
Pellinen T., Tuomi S., Arjonen A., Wolf M., Edgren H., Meyer H.,
Grosse R., Kitzing T., Rantala J.K., Kallioniemi O., Faessler R.,
Kallio M., Ivaska J.;
"Integrin trafficking regulated by Rab21 is necessary for
cytokinesis.";
Dev. Cell 15:371-385(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-343.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-343.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 168-368.
PubMed=9353312; DOI=10.1074/jbc.272.45.28512;
Emsley J., King S.L., Bergelson J.M., Liddington R.C.;
"Crystal structure of the I domain from integrin alpha2beta1.";
J. Biol. Chem. 272:28512-28517(1997).
[16]
VARIANT GLU-534, AND POLYMORPHISM.
PubMed=7901236; DOI=10.1172/JCI116849;
Santoso S., Kalb R., Walka M., Kiefel V., Mueller-Eckhardt C.,
Newman P.J.;
"The human platelet alloantigens Br(a) and Brb are associated with a
single amino acid polymorphism on glycoprotein Ia (integrin subunit
alpha 2).";
J. Clin. Invest. 92:2427-2432(1993).
[17]
VARIANT GLU-534.
PubMed=10744142;
Kroll H., Gardemann A., Fechter A., Haberbosch W., Santoso S.;
"The impact of the glycoprotein Ia collagen receptor subunit A1648G
gene polymorphism on coronary artery disease and acute myocardial
infarction.";
Thromb. Haemost. 83:392-396(2000).
[18]
VARIANT LEU-532.
PubMed=23368983; DOI=10.1111/vox.12019;
Bertrand G., Jallu V., Beranger T., Bianchi F., Casale C., Dufour V.,
Chenet C., Quesne J., Martageix C., Kaplan C.;
"HPA-5 typing discrepancy reveals an Ile503Leu substitution in
platelet GPIa (alpha2 integrin).";
Vox Sang. 105:73-76(2013).
-!- FUNCTION: Integrin alpha-2/beta-1 is a receptor for laminin,
collagen, collagen C-propeptides, fibronectin and E-cadherin. It
recognizes the proline-hydroxylated sequence G-F-P-G-E-R in
collagen. It is responsible for adhesion of platelets and other
cells to collagens, modulation of collagen and collagenase gene
expression, force generation and organization of newly synthesized
extracellular matrix.
-!- FUNCTION: (Microbial infection) Integrin ITGA2:ITGB1 acts as a
receptor for human rotavirus A (PubMed:12941907). Integrin
ITGA2:ITGB1 acts as a receptor for human echoviruses 1 and 8
(PubMed:8411387). {ECO:0000269|PubMed:12941907,
ECO:0000269|PubMed:8411387}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-2
associates with beta-1. Interacts with HPS5 and RAB21.
{ECO:0000269|PubMed:16754960}.
-!- SUBUNIT: (Microbial infection) Integrin ITGA2:ITGB1 interacts (via
ITAG2 I-domain) with rotavirus A VP4 protein.
{ECO:0000269|PubMed:12941907}.
-!- SUBUNIT: (Microbial infection) Integrin ITGA2:ITGB1 interacts with
human echoviruses 1 and 8 capsid proteins.
{ECO:0000269|PubMed:8411387}.
-!- INTERACTION:
P04512:- (xeno); NbExp=3; IntAct=EBI-702960, EBI-15711650;
P84092:Ap2m1 (xeno); NbExp=2; IntAct=EBI-702960, EBI-297693;
P05556:ITGB1; NbExp=3; IntAct=EBI-702960, EBI-703066;
P35968:KDR; NbExp=2; IntAct=EBI-702960, EBI-1005487;
P35282:Rab21 (xeno); NbExp=7; IntAct=EBI-702960, EBI-1993555;
Q9H0F6:SHARPIN; NbExp=5; IntAct=EBI-702960, EBI-3942966;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins
with I-domains do not undergo protease cleavage.
-!- POLYMORPHISM: Position 534 is associated with platelet-specific
alloantigen HPA-5 (Br). HPA-5A/Br(a) has Lys-534 and HPA-5B/Br(b)
has Glu-534. HPA-5B is involved in neonatal alloimmune
thrombocytopenia (NAIT or NATP). The Lys-534-Glu polymorphism may
play a role in coronary artery disease (CAD).
{ECO:0000269|PubMed:7901236}.
-!- SIMILARITY: Belongs to the integrin alpha chain family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/itga2/";
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EMBL; X17033; CAA34894.1; -; mRNA.
EMBL; AF512556; AAM34795.1; -; Genomic_DNA.
EMBL; L24121; AAA16619.2; -; Genomic_DNA.
CCDS; CCDS3957.1; -.
PIR; A33998; A33998.
RefSeq; NP_002194.2; NM_002203.3.
UniGene; Hs.482077; -.
PDB; 1AOX; X-ray; 2.10 A; A/B=169-367.
PDB; 1DZI; X-ray; 2.10 A; A=172-355.
PDB; 1PQB; Model; -; A/B=169-366.
PDB; 1V7P; X-ray; 1.90 A; C=167-366.
PDB; 4BJ3; X-ray; 3.04 A; A/B=171-368.
PDB; 5HJ2; X-ray; 2.15 A; A/B/C/D/E/F=170-366.
PDB; 5THP; X-ray; 3.01 A; C/F/I/L/O/R=170-366.
PDBsum; 1AOX; -.
PDBsum; 1DZI; -.
PDBsum; 1PQB; -.
PDBsum; 1V7P; -.
PDBsum; 4BJ3; -.
PDBsum; 5HJ2; -.
PDBsum; 5THP; -.
ProteinModelPortal; P17301; -.
SMR; P17301; -.
BioGrid; 109880; 31.
CORUM; P17301; -.
DIP; DIP-67N; -.
IntAct; P17301; 20.
MINT; MINT-5004079; -.
STRING; 9606.ENSP00000296585; -.
BindingDB; P17301; -.
ChEMBL; CHEMBL4998; -.
GuidetoPHARMACOLOGY; 2441; -.
iPTMnet; P17301; -.
PhosphoSitePlus; P17301; -.
SwissPalm; P17301; -.
BioMuta; ITGA2; -.
DMDM; 124942; -.
EPD; P17301; -.
MaxQB; P17301; -.
PaxDb; P17301; -.
PeptideAtlas; P17301; -.
PRIDE; P17301; -.
DNASU; 3673; -.
Ensembl; ENST00000296585; ENSP00000296585; ENSG00000164171.
GeneID; 3673; -.
KEGG; hsa:3673; -.
UCSC; uc003joy.3; human.
CTD; 3673; -.
DisGeNET; 3673; -.
EuPathDB; HostDB:ENSG00000164171.10; -.
GeneCards; ITGA2; -.
H-InvDB; HIX0032121; -.
HGNC; HGNC:6137; ITGA2.
HPA; CAB017690; -.
HPA; HPA060991; -.
HPA; HPA063556; -.
MalaCards; ITGA2; -.
MIM; 192974; gene+phenotype.
neXtProt; NX_P17301; -.
Orphanet; 853; Fetal and neonatal alloimmune thrombocytopenia.
PharmGKB; PA204; -.
eggNOG; ENOG410IPB9; Eukaryota.
eggNOG; ENOG4110534; LUCA.
HOGENOM; HOG000059610; -.
HOVERGEN; HBG006185; -.
InParanoid; P17301; -.
KO; K06481; -.
OrthoDB; EOG091G00TK; -.
PhylomeDB; P17301; -.
TreeFam; TF105391; -.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-3000157; Laminin interactions.
Reactome; R-HSA-3000170; Syndecan interactions.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-447041; CHL1 interactions.
Reactome; R-HSA-75892; Platelet Adhesion to exposed collagen.
Reactome; R-HSA-8874081; MET activates PTK2 signaling.
SignaLink; P17301; -.
SIGNOR; P17301; -.
ChiTaRS; ITGA2; human.
EvolutionaryTrace; P17301; -.
GeneWiki; CD49b; -.
GenomeRNAi; 3673; -.
PRO; PR:P17301; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000164171; -.
CleanEx; HS_ITGA2; -.
ExpressionAtlas; P17301; baseline and differential.
Genevisible; P17301; HS.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0043679; C:axon terminus; IEA:Ensembl.
GO; GO:0045178; C:basal part of cell; IEA:Ensembl.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0034666; C:integrin alpha2-beta1 complex; IDA:UniProtKB.
GO; GO:0008305; C:integrin complex; TAS:ProtInc.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0001540; F:amyloid-beta binding; ISS:ARUK-UCL.
GO; GO:0005518; F:collagen binding; IMP:UniProtKB.
GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; IMP:UniProtKB.
GO; GO:0038064; F:collagen receptor activity; IMP:UniProtKB.
GO; GO:0043395; F:heparan sulfate proteoglycan binding; TAS:ARUK-UCL.
GO; GO:0005178; F:integrin binding; IEA:Ensembl.
GO; GO:0043236; F:laminin binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0032403; F:protein complex binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
GO; GO:0007596; P:blood coagulation; TAS:ProtInc.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0033627; P:cell adhesion mediated by integrin; IMP:UniProtKB.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB.
GO; GO:0031589; P:cell-substrate adhesion; IMP:UniProtKB.
GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0038065; P:collagen-activated signaling pathway; IMP:UniProtKB.
GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IEA:Ensembl.
GO; GO:0045184; P:establishment of protein localization; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0048041; P:focal adhesion assembly; IEA:Ensembl.
GO; GO:0070365; P:hepatocyte differentiation; IEA:Ensembl.
GO; GO:0006971; P:hypotonic response; IEA:Ensembl.
GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0030879; P:mammary gland development; IEA:Ensembl.
GO; GO:0048333; P:mesodermal cell differentiation; IEP:UniProtKB.
GO; GO:0010694; P:positive regulation of alkaline phosphatase activity; IEA:Ensembl.
GO; GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl.
GO; GO:0031346; P:positive regulation of cell projection organization; IEA:Ensembl.
GO; GO:0033343; P:positive regulation of collagen binding; IEA:Ensembl.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IEA:Ensembl.
GO; GO:0043388; P:positive regulation of DNA binding; IEA:Ensembl.
GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
GO; GO:0002687; P:positive regulation of leukocyte migration; IEA:Ensembl.
GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IEA:Ensembl.
GO; GO:0050927; P:positive regulation of positive chemotaxis; IEA:Ensembl.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IEA:Ensembl.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0045987; P:positive regulation of smooth muscle contraction; IEA:Ensembl.
GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
GO; GO:0051971; P:positive regulation of transmission of nerve impulse; IEA:Ensembl.
GO; GO:0014075; P:response to amine; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0033591; P:response to L-ascorbic acid; IEA:Ensembl.
GO; GO:0014850; P:response to muscle activity; IEA:Ensembl.
GO; GO:0071107; P:response to parathyroid hormone; IEA:Ensembl.
GO; GO:0043589; P:skin morphogenesis; IEA:Ensembl.
GO; GO:0006929; P:substrate-dependent cell migration; IMP:UniProtKB.
InterPro; IPR013517; FG-GAP.
InterPro; IPR013519; Int_alpha_beta-p.
InterPro; IPR000413; Integrin_alpha.
InterPro; IPR013649; Integrin_alpha-2.
InterPro; IPR018184; Integrin_alpha_C_CS.
InterPro; IPR032695; Integrin_dom_sf.
InterPro; IPR002035; VWF_A.
InterPro; IPR036465; vWFA_dom_sf.
Pfam; PF01839; FG-GAP; 2.
Pfam; PF08441; Integrin_alpha2; 1.
Pfam; PF00092; VWA; 1.
PRINTS; PR01185; INTEGRINA.
SMART; SM00191; Int_alpha; 5.
SMART; SM00327; VWA; 1.
SUPFAM; SSF53300; SSF53300; 1.
SUPFAM; SSF69179; SSF69179; 3.
PROSITE; PS51470; FG_GAP; 7.
PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PROSITE; PS50234; VWFA; 1.
1: Evidence at protein level;
3D-structure; Calcium; Cell adhesion; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Host cell receptor for virus entry; Host-virus interaction; Integrin;
Magnesium; Membrane; Metal-binding; Polymorphism; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 29 {ECO:0000269|PubMed:2545729}.
CHAIN 30 1181 Integrin alpha-2.
/FTId=PRO_0000016233.
TOPO_DOM 30 1132 Extracellular. {ECO:0000255}.
TRANSMEM 1133 1154 Helical. {ECO:0000255}.
TOPO_DOM 1155 1181 Cytoplasmic. {ECO:0000255}.
REPEAT 34 92 FG-GAP 1. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 101 161 FG-GAP 2. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
DOMAIN 188 365 VWFA. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
REPEAT 366 420 FG-GAP 3. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 423 475 FG-GAP 4. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 477 539 FG-GAP 5. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 540 598 FG-GAP 6. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 602 664 FG-GAP 7. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
CA_BIND 499 507 {ECO:0000255}.
CA_BIND 563 571 {ECO:0000255}.
CA_BIND 627 635 {ECO:0000255}.
REGION 1155 1161 Interaction with HPS5.
MOTIF 1157 1161 GFFKR motif.
CARBOHYD 105 105 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 112 112 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 343 343 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
CARBOHYD 432 432 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 460 460 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 475 475 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 699 699 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1057 1057 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1074 1074 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1081 1081 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 83 92 {ECO:0000250}.
DISULFID 680 737 {ECO:0000250}.
DISULFID 789 795 {ECO:0000250}.
DISULFID 865 876 {ECO:0000250}.
DISULFID 1019 1050 {ECO:0000250}.
DISULFID 1055 1060 {ECO:0000250}.
VARIANT 532 532 I -> L. {ECO:0000269|PubMed:23368983}.
/FTId=VAR_076939.
VARIANT 534 534 K -> E (in alloantigen HPA-5B;
dbSNP:rs1801106).
{ECO:0000269|PubMed:10744142,
ECO:0000269|PubMed:15372022,
ECO:0000269|PubMed:7901236}.
/FTId=VAR_003977.
VARIANT 691 691 N -> K (in dbSNP:rs3212557).
{ECO:0000269|Ref.2}.
/FTId=VAR_029146.
VARIANT 927 927 N -> S (in dbSNP:rs2287870).
/FTId=VAR_021855.
VARIANT 1127 1127 K -> Q (in dbSNP:rs3212645).
{ECO:0000269|Ref.2}.
/FTId=VAR_020036.
MUTAGEN 1159 1159 F->A: No significant reduction of RAB21-
binding by co-immunoprecipitation assay;
when associated with A-1160 and A-1162.
{ECO:0000269|PubMed:16754960}.
MUTAGEN 1160 1160 K->A: No effect on RAB21-binding.
Significant reduction of RAB21-binding;
when associated with A-1161. Shows
defective cytokinesis on collagen, but
not on fibronectin; when associated with
A-1161. {ECO:0000269|PubMed:16754960,
ECO:0000269|PubMed:18804435}.
MUTAGEN 1161 1161 R->A: Significant reduction of RAB21-
binding; when associated with A-1160.
Shows defective cytokinesis on collagen,
but not on fibronectin; when associated
with A-1160.
{ECO:0000269|PubMed:16754960,
ECO:0000269|PubMed:18804435}.
MUTAGEN 1162 1162 K->A: No significant reduction of RAB21-
binding by co-immunoprecipitation assay;
when associated with A-1159 and A-1160.
{ECO:0000269|PubMed:16754960,
ECO:0000269|PubMed:18804435}.
MUTAGEN 1162 1162 K->P: Markedly weakens RAB21-binding.
Shows defective cytokinesis on collagen,
but not on fibronectin.
{ECO:0000269|PubMed:16754960,
ECO:0000269|PubMed:18804435}.
MUTAGEN 1164 1164 E->A: Significant reduction of RAB21-
binding; when associated with A-1160; A-
1161 and A-1165.
{ECO:0000269|PubMed:16754960}.
MUTAGEN 1165 1165 K->A: Significant reduction of RAB21-
binding; when associated with A-1160; A-
1161 and A-1164.
{ECO:0000269|PubMed:16754960}.
CONFLICT 17 17 L -> V (in Ref. 3; AAA16619).
{ECO:0000305}.
STRAND 173 180 {ECO:0000244|PDB:1V7P}.
HELIX 188 200 {ECO:0000244|PDB:1V7P}.
STRAND 208 224 {ECO:0000244|PDB:1V7P}.
TURN 226 228 {ECO:0000244|PDB:1V7P}.
HELIX 232 241 {ECO:0000244|PDB:1V7P}.
HELIX 252 262 {ECO:0000244|PDB:1V7P}.
HELIX 266 268 {ECO:0000244|PDB:1V7P}.
STRAND 274 284 {ECO:0000244|PDB:1V7P}.
HELIX 289 291 {ECO:0000244|PDB:1V7P}.
HELIX 292 301 {ECO:0000244|PDB:1V7P}.
STRAND 304 311 {ECO:0000244|PDB:1V7P}.
HELIX 313 317 {ECO:0000244|PDB:1V7P}.
HELIX 323 332 {ECO:0000244|PDB:1V7P}.
HELIX 337 340 {ECO:0000244|PDB:1V7P}.
STRAND 341 347 {ECO:0000244|PDB:1V7P}.
HELIX 348 353 {ECO:0000244|PDB:1V7P}.
HELIX 354 362 {ECO:0000244|PDB:1V7P}.
SEQUENCE 1181 AA; 129295 MW; 7E1B7ED968A94070 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 TIKKGILGQH
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


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