ITA2_MOUSE
ID ITA2_MOUSE Reviewed; 1178 AA.
AC Q62469; Q62163; Q6P1C7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 182.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6 X CBA; TISSUE=Lung;
RX PubMed=8081889; DOI=10.3109/15419069409004432;
RA Edelman J.M., Chan B.M., Uniyal S., Onodera H., Wang D.Z., Damjanovich L.,
RA Latzer D.B., Finberg R.W., Bergelson J.M.;
RT "The mouse VLA-2 homologue supports collagen and laminin adhesion but not
RT virus binding.";
RL Cell Adhes. Commun. 2:131-143(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 450-1178.
RC TISSUE=Lung;
RX PubMed=7521231; DOI=10.1002/aja.1001990405;
RA Wu J.E., Santoro S.A.;
RT "Complex patterns of expression suggest extensive roles for the alpha 2
RT beta 1 integrin in murine development.";
RL Dev. Dyn. 199:292-314(1994).
RN [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Integrin alpha-2/beta-1 is a collagen receptor, being
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 It is also a receptor for laminins, collagen C-propeptides and E-
CC cadherin. Mice homozygous for a null mutation in the alpha-2 die very
CC early in embryogenesis.
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 -!- 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}.
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DR EMBL; Z29987; CAA82877.1; -; mRNA.
DR EMBL; CH466568; EDL18370.1; -; Genomic_DNA.
DR EMBL; BC065139; AAH65139.1; -; mRNA.
DR EMBL; X75427; CAA53178.1; -; mRNA.
DR CCDS; CCDS26787.1; -.
DR PIR; S44142; S44142.
DR RefSeq; NP_032422.2; NM_008396.2.
DR AlphaFoldDB; Q62469; -.
DR SMR; Q62469; -.
DR BioGRID; 200814; 4.
DR ComplexPortal; CPX-3115; Integrin alpha2-beta1 complex.
DR STRING; 10090.ENSMUSP00000053891; -.
DR GlyConnect; 2396; 1 N-Linked glycan (1 site).
DR GlyGen; Q62469; 9 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q62469; -.
DR PhosphoSitePlus; Q62469; -.
DR CPTAC; non-CPTAC-3831; -.
DR EPD; Q62469; -.
DR MaxQB; Q62469; -.
DR PaxDb; Q62469; -.
DR PeptideAtlas; Q62469; -.
DR PRIDE; Q62469; -.
DR ProteomicsDB; 269344; -.
DR Antibodypedia; 10993; 1421 antibodies from 47 providers.
DR DNASU; 16398; -.
DR Ensembl; ENSMUST00000056117; ENSMUSP00000053891; ENSMUSG00000015533.
DR GeneID; 16398; -.
DR KEGG; mmu:16398; -.
DR UCSC; uc007rxw.1; mouse.
DR CTD; 3673; -.
DR MGI; MGI:96600; Itga2.
DR VEuPathDB; HostDB:ENSMUSG00000015533; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000156303; -.
DR HOGENOM; CLU_004111_2_1_1; -.
DR InParanoid; Q62469; -.
DR OMA; IWNRTFA; -.
DR OrthoDB; 66046at2759; -.
DR PhylomeDB; Q62469; -.
DR TreeFam; TF105391; -.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-3000157; Laminin interactions.
DR Reactome; R-MMU-3000170; Syndecan interactions.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR BioGRID-ORCS; 16398; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Itga2; mouse.
DR PRO; PR:Q62469; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q62469; protein.
DR Bgee; ENSMUSG00000015533; Expressed in gastrula and 154 other tissues.
DR ExpressionAtlas; Q62469; baseline and differential.
DR Genevisible; Q62469; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0045178; C:basal part of cell; IDA:MGI.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0034666; C:integrin alpha2-beta1 complex; ISO:MGI.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001540; F:amyloid-beta binding; IDA:ARUK-UCL.
DR GO; GO:0005518; F:collagen binding; ISO:MGI.
DR GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; ISO:MGI.
DR GO; GO:0038064; F:collagen receptor activity; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0043236; F:laminin binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0031589; P:cell-substrate adhesion; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; ISO:MGI.
DR GO; GO:0045184; P:establishment of protein localization; ISO:MGI.
DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR GO; GO:0048041; P:focal adhesion assembly; ISO:MGI.
DR GO; GO:0070365; P:hepatocyte differentiation; IEA:Ensembl.
DR GO; GO:0006971; P:hypotonic response; ISO:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
DR GO; GO:0030879; P:mammary gland development; IEA:Ensembl.
DR GO; GO:0048333; P:mesodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0010694; P:positive regulation of alkaline phosphatase activity; ISO:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:MGI.
DR GO; GO:0031346; P:positive regulation of cell projection organization; ISO:MGI.
DR GO; GO:0033343; P:positive regulation of collagen binding; ISO:MGI.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISO:MGI.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISO:MGI.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:MGI.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISO:MGI.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; ISO:MGI.
DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; ISO:MGI.
DR GO; GO:0050927; P:positive regulation of positive chemotaxis; ISO:MGI.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; ISO:MGI.
DR GO; GO:0045727; P:positive regulation of translation; ISO:MGI.
DR GO; GO:0051971; P:positive regulation of transmission of nerve impulse; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0006929; P:substrate-dependent cell migration; ISO:MGI.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
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; PF00357; Integrin_alpha; 1.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR Pfam; PF00092; VWA; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR 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 Calcium; Cell adhesion; Disulfide bond; Glycoprotein; Integrin; Magnesium;
KW Membrane; Metal-binding; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT CHAIN 27..1178
FT /note="Integrin alpha-2"
FT /id="PRO_0000016234"
FT TOPO_DOM 27..1129
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1130..1151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1152..1178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 31..89
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 98..158
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT DOMAIN 185..362
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REPEAT 363..417
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 420..472
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 474..536
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 537..595
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 601..661
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT MOTIF 480..482
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1154..1158
FT /note="GFFKR motif"
FT BINDING 496
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
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 504
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 560
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 562
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 564
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 568
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 624
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 626
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 628
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 632
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 696
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1054
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1071
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1078
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 80..89
FT /evidence="ECO:0000250"
FT DISULFID 677..734
FT /evidence="ECO:0000250"
FT DISULFID 786..792
FT /evidence="ECO:0000250"
FT DISULFID 862..873
FT /evidence="ECO:0000250"
FT DISULFID 1016..1047
FT /evidence="ECO:0000250"
FT DISULFID 1052..1057
FT /evidence="ECO:0000250"
FT CONFLICT 13
FT /note="R -> Q (in Ref. 1; CAA82877)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1178 AA; 128955 MW; 62FAEA820242A9B6 CRC64;
MGPGQAGGAL LLRLLMLVQG ILNCLAYNVG LPGAKIFSGP SSEQFGYSVQ QLTNPQGNWL
LVGSPWSGFP ENRMGDVYKC PVDLPTATCE KLNLQNSASI SNVTEIKTNM SLGLTLTRNP
GTGGFLTCGP LWAHQCGNQY YATGICSDVS PDFQFLTSFS PAVQACPSLV DVVVVCDESN
SIYPWEAVKN FLVKFVTGLD IGPKKTQVAL IQYANEPRII FNLNDFETKE DMVQATSETR
QHGGDLTNTF RAIEFARDYA YSQTSGGRPG ATKVMVVVTD GESHDGSKLK TVIQQCNDDE
ILRFGIAVLG YLNRNALDTK NLIKEIKAIA STPTERYFFN VADEAALLEK AGTLGEQIFS
IEGTVQGGDN FQMEMAQVGF SADYAPQNDI LMLGAVGAFD WSGTLVQETS HKPVIFPKQA
FDQVLQDRNH SSFLGYSVAA ISTEDGVHFV AGAPRANYTG QIVLYSVNKQ GNVTVIQSHR
GDQIGSYFGS VLCSVDVDKD TITDVLLVGA PTYMNDLKKE EGKVYLFTIT KGILNQHQFL
EGPEGTGNAR FGSAIAALSD INMDGFNDVI VGSPVENENS GAVYIYNGHQ GTIRTKYSQK
ILGSNGAFRR HLQFFGRSLD GYGDLNGDSI TDVSIGALGQ VIQLWSQSIA DVAIEALFTP
DKITLLNKDA KITLKLCFRA EFRPAGQNNQ VAILFNMTLD ADGHSSRVTS RGVFRENSER
FLQKNMVVNE VQKCSEHHIS IQKPSDVVNP LDLRVDISLE NPGTSPALEA YSETVKVFSI
PFYKECGSDG ICISDLILDV QQLPAIQTQS FIVSNQNKRL TFSVILKNRG ESAYNTVVLA
EFSENLFFAS FSMPVDGTEV TCEVGSSQKS VTCDVGYPAL KSEQQVTFTI NFDFNLQNLQ
NQAAINFQAF SESQETNKAD NSVSLTIPLL YDAELHLTRS TNINFYEISS DENAPSVIKS
VEDIGPKFIF SLKVTAGSAP VSMALVTIHI PQYTKEKNPL LYLTGIQTDQ AGDISCTAEI
NPLKLPHTAP SVSFKNENFR HTKELDCRTT SCSNITCWLK DLHMKAEYFI NVTTRVWNRT
FAASTFQTVQ LTAAAEIDTH NPQLFVIEEN AVTIPLMIMK PTEKAEVPTG VIIGSIIAGI
LLLLAMTAGL WKLGFFKRQY KKMGQNPDEM DETTELNS
