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 01-MAY-2013, entry version 114.
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;
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 IPI; IPI00126077; -.
DR PIR; S44142; S44142.
DR RefSeq; NP_032422.2; NM_008396.2.
DR UniGene; Mm.5007; -.
DR ProteinModelPortal; Q62469; -.
DR SMR; Q62469; 42-1077.
DR STRING; 10090.ENSMUSP00000053891; -.
DR PhosphoSite; Q62469; -.
DR PaxDb; Q62469; -.
DR PRIDE; Q62469; -.
DR Ensembl; ENSMUST00000056117; ENSMUSP00000053891; ENSMUSG00000015533.
DR GeneID; 16398; -.
DR KEGG; mmu:16398; -.
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; NILRFGI; -.
DR OrthoDB; EOG45B1DV; -.
DR Reactome; REACT_127416; Developmental Biology.
DR NextBio; 289545; -.
DR ArrayExpress; Q62469; -.
DR Bgee; Q62469; -.
DR CleanEx; MM_ITGA2; -.
DR Genevestigator; Q62469; -.
DR GermOnline; ENSMUSG00000015533; Mus musculus.
DR GO; GO:0045178; C:basal part of cell; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
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 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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