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Database: UniProt
Entry: E9PXZ3_MOUSE
LinkDB: E9PXZ3_MOUSE
Original site: E9PXZ3_MOUSE 
ID   E9PXZ3_MOUSE            Unreviewed;      1166 AA.
AC   E9PXZ3;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=Integrin, alpha 10 {ECO:0000313|Ensembl:ENSMUSP00000112393.2};
GN   Name=Itga10 {ECO:0000313|Ensembl:ENSMUSP00000112393.2,
GN   ECO:0000313|MGI:MGI:2153482};
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 {ECO:0000313|Ensembl:ENSMUSP00000112393.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000112393.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000112393.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0000313|Ensembl:ENSMUSP00000112393.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000112393.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC       ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
CC   -!- SIMILARITY: Belongs to the integrin alpha chain family.
CC       {ECO:0000256|ARBA:ARBA00008054, ECO:0000256|RuleBase:RU003762}.
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DR   RefSeq; NP_001289400.1; NM_001302471.1.
DR   AlphaFoldDB; E9PXZ3; -.
DR   SMR; E9PXZ3; -.
DR   STRING; 10090.ENSMUSP00000112393; -.
DR   PeptideAtlas; E9PXZ3; -.
DR   ProteomicsDB; 346662; -.
DR   DNASU; 213119; -.
DR   Ensembl; ENSMUST00000119365.8; ENSMUSP00000112393.2; ENSMUSG00000090210.8.
DR   GeneID; 213119; -.
DR   KEGG; mmu:213119; -.
DR   UCSC; uc012ctz.1; mouse.
DR   AGR; MGI:2153482; -.
DR   CTD; 8515; -.
DR   MGI; MGI:2153482; Itga10.
DR   VEuPathDB; HostDB:ENSMUSG00000090210; -.
DR   GeneTree; ENSGT00940000158423; -.
DR   HOGENOM; CLU_004111_2_0_1; -.
DR   OMA; SRNITRY; -.
DR   OrthoDB; 3816176at2759; -.
DR   BioGRID-ORCS; 213119; 5 hits in 61 CRISPR screens.
DR   ChiTaRS; Itga10; mouse.
DR   Proteomes; UP000000589; Chromosome 3.
DR   Bgee; ENSMUSG00000090210; Expressed in humerus cartilage element and 132 other cell types or tissues.
DR   ExpressionAtlas; E9PXZ3; baseline and differential.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0034680; C:integrin alpha10-beta1 complex; ISO:MGI.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR   GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; ISO:MGI.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
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; 2.
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; IPR013649; Integrin_alpha_Ig-like_1.
DR   InterPro; IPR048285; Integrin_alpha_Ig-like_2.
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:SF26; INTEGRIN ALPHA-10; 1.
DR   Pfam; PF01839; FG-GAP; 1.
DR   Pfam; PF08441; Integrin_A_Ig_1; 1.
DR   Pfam; PF20805; Integrin_A_Ig_2; 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; 4.
DR   PROSITE; PS00242; INTEGRIN_ALPHA; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   1: Evidence at protein level;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW   ECO:0000256|RuleBase:RU003762};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU003762};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003762};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Proteomics identification {ECO:0007829|ProteomicsDB:E9PXZ3};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU003762};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU003762};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003762};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU003762}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT   CHAIN           23..1166
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT                   /id="PRO_5001424267"
FT   TRANSMEM        1120..1144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT   REPEAT          24..85
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   DOMAIN          167..350
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   REPEAT          472..534
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          535..593
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          597..657
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
SQ   SEQUENCE   1166 AA;  127764 MW;  F921BF67850BFD72 CRC64;
     MESLSIPHLL LPLALLTGLC SSFNLDEHHP RLFTGPPEAE FGYSVLQHVG GGQRWMLVGA
     PWDGPSGDRR GDVYRCSIGG FHSAPCTKGH LGDYQLGNSS QPAVNMHLGM SLLETDADGG
     FMACAPLWSR ACGSSVFSSG ICARVDASFR PQGSLAPTAQ RCPTYMDVVI VLDGSNSIYP
     WSEVQTFLRR LVGRLFIDPE QIQVGLVQYG ENPVHEWSLG DFRTKEEVVR AARNLSRREG
     RETRTAQAIM VACTEGFSQS RGGRPEAARL LVVVTDGESH DGEELPAALK ACEAGRVTRY
     GIAVLGHYLR RQRDPSSFLR EIRAIASDPD ERFFFNVTDE AALTDIVDAL GDRIFGLEGS
     RGENESSFGL EMSEIGFSIH RLQDGILFGM VGAYDWGGSV LWLEEGRRLF PPQAALEDEF
     PPALQNHAAY LGYSVSSMLL PGGRRLFLSG APRFRHRGKV IAFQLKKDGV VRVAQSLQGD
     QIGSYFGSEL CPLDTDKDGI TNILLVAAPM FLGPQNKETG RVYVYMVGQQ NLLMLQGTLQ
     PDRSQDSRFG FAMAALPDLN HDGFTDVAVG APLEDGHRGA LYLYHGTQTG IRPHPTQRIA
     AVSMPQALRY FGRSVDGRLD LDGDDLVDVA VGAHGAAVLF SSQPIIHLIP TLDVMPPHIS
     VVQKDCKRRG QEAACLTAAL CFQVVSQTPG RWDRRFYIRF SASLDEWTAG ARAVFDGSGQ
     RLSPRQLQLS VGNVTCEQLH FHALDTSDYL RPVALTVTFA LDNTTKPGPV LAEGSSTTIR
     KLIPFSKDCG PDNECVTDLV LQADMDIRGS RKSPFVVQGG RQKVLVSATL ENKKENAYNT
     SLSLSFSRNL HLASLTPQAK SVKVECAVPS PHTRLCTVGH PVFQTGAKVS FLLEFEFSCT
     FLLSQVFVRL TASSSSLEMN ETLQDNTAQT SAYIRYEPHL VFSSESTLHR YEVHPYRTLP
     MGPGPEFKTT LRVQNLGCHV VSGLVISALL PAVAHGGNYF LSLSQVISGN ASCTVQNLTE
     PPGFPVHPEE LQHASRLNGS NSRCQVVRCH LGLLAKGTEI SVRLLRLVHN EFFRRAKFKS
     VTVVSTFKLG TEEGSVLLLN EASRSSESHL EVIQTHPTLI SLWILVGSVL GGLLLLALLV
     FCLWKLGFFT RKKIPKEEES EEKLEQ
//
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