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Database: UniProt
Entry: ITA2_MOUSE
LinkDB: ITA2_MOUSE
Original site: 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   09-JUL-2014, entry version 126.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X CBA; TISSUE=Lung;
RX   PubMed=8081889;
RA   Edelman J.M., Chan B.M., Uniyal S., Onodera H., Wang D.Z.,
RA   Damjanovich L., Latzer D.B., Finberg R.W., Bergelson J.M.;
RT   "The mouse VLA-2 homologue supports collagen and laminin adhesion but
RT   not 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/6; 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
RT   project: 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
RT   2 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
RT   traffic of beta1-integrins.";
RL   J. Cell Biol. 173:767-780(2006).
CC   -!- FUNCTION: Integrin alpha-2/beta-1 is a collagen receptor, being
CC       responsible for adhesion of platelets and other cells to
CC       collagens, modulation of collagen and collagenase gene expression,
CC       force generation and organization of newly synthesized
CC       extracellular matrix. It is also a receptor for laminins, collagen
CC       C-propeptides and E-cadherin. Mice homozygous for a null mutation
CC       in the alpha-2 die very early in embryogenesis.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-2
CC       associates with beta-1. Interacts with HPS5 and RAB21.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins
CC       with I-domains do not undergo protease cleavage.
CC   -!- SIMILARITY: Belongs to the integrin alpha chain family.
CC   -!- SIMILARITY: Contains 7 FG-GAP repeats.
CC   -!- SIMILARITY: Contains 1 VWFA domain.
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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   UniGene; Mm.5007; -.
DR   ProteinModelPortal; Q62469; -.
DR   SMR; Q62469; 27-1166.
DR   IntAct; Q62469; 1.
DR   MINT; MINT-1866744; -.
DR   STRING; 10090.ENSMUSP00000053891; -.
DR   PhosphoSite; Q62469; -.
DR   MaxQB; Q62469; -.
DR   PaxDb; Q62469; -.
DR   PRIDE; Q62469; -.
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   eggNOG; NOG237277; -.
DR   GeneTree; ENSGT00660000095470; -.
DR   HOGENOM; HOG000059610; -.
DR   HOVERGEN; HBG006185; -.
DR   InParanoid; Q6P1C7; -.
DR   KO; K06481; -.
DR   OMA; DNILRFG; -.
DR   OrthoDB; EOG71RXHT; -.
DR   TreeFam; TF105391; -.
DR   Reactome; REACT_188576; Developmental Biology.
DR   NextBio; 289545; -.
DR   PRO; PR:Q62469; -.
DR   Bgee; Q62469; -.
DR   CleanEx; MM_ITGA2; -.
DR   Genevestigator; Q62469; -.
DR   GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR   GO; GO:0045178; C:basal part of cell; IDA:MGI.
DR   GO; GO:0009279; C:cell outer membrane; IEA:Ensembl.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR   GO; GO:0008305; C:integrin complex; IEA:InterPro.
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; TAS:Reactome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
DR   GO; GO:0006928; P:cellular component movement; IEA:Ensembl.
DR   GO; GO:0032870; P:cellular response to hormone stimulus; IEA:Ensembl.
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:0070365; P:hepatocyte differentiation; IEA:Ensembl.
DR   GO; GO:0006971; P:hypotonic response; IEA:Ensembl.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0030879; P:mammary gland development; IEA:Ensembl.
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:0042493; P:response to drug; 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:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR   GO; GO:0043589; P:skin morphogenesis; IEA:Ensembl.
DR   GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl.
DR   GO; GO:0042060; P:wound healing; IEA:Ensembl.
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; IPR002035; VWF_A.
DR   Pfam; PF01839; FG-GAP; 1.
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   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; Complete proteome; Disulfide bond;
KW   Glycoprotein; Integrin; Magnesium; Membrane; Metal-binding; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     26       By similarity.
FT   CHAIN        27   1178       Integrin alpha-2.
FT                                /FTId=PRO_0000016234.
FT   TOPO_DOM     27   1129       Extracellular (Potential).
FT   TRANSMEM   1130   1151       Helical; (Potential).
FT   TOPO_DOM   1152   1178       Cytoplasmic (Potential).
FT   REPEAT       31     89       FG-GAP 1.
FT   REPEAT       98    158       FG-GAP 2.
FT   DOMAIN      185    362       VWFA.
FT   REPEAT      363    417       FG-GAP 3.
FT   REPEAT      420    474       FG-GAP 4.
FT   REPEAT      475    536       FG-GAP 5.
FT   REPEAT      537    595       FG-GAP 6.
FT   REPEAT      601    661       FG-GAP 7.
FT   CA_BIND     496    504       Potential.
FT   CA_BIND     560    568       Potential.
FT   CA_BIND     624    632       Potential.
FT   MOTIF       480    482       Cell attachment site (Potential).
FT   MOTIF      1154   1158       GFFKR motif.
FT   CARBOHYD    102    102       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    109    109       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    429    429       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    457    457       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    472    472       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    696    696       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1054   1054       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1071   1071       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1078   1078       N-linked (GlcNAc...) (Potential).
FT   DISULFID     80     89       By similarity.
FT   DISULFID    677    734       By similarity.
FT   DISULFID    786    792       By similarity.
FT   DISULFID    862    873       By similarity.
FT   DISULFID   1016   1047       By similarity.
FT   DISULFID   1052   1057       By similarity.
FT   CONFLICT     13     13       R -> Q (in Ref. 1; CAA82877).
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
//
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