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Database: UniProt
Entry: A0A2K5LJ52_CERAT
LinkDB: A0A2K5LJ52_CERAT
Original site: A0A2K5LJ52_CERAT 
ID   A0A2K5LJ52_CERAT        Unreviewed;      1188 AA.
AC   A0A2K5LJ52;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Integrin subunit alpha 11 {ECO:0000313|Ensembl:ENSCATP00000012989.1};
GN   Name=ITGA11 {ECO:0000313|Ensembl:ENSCATP00000012989.1};
OS   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000012989.1, ECO:0000313|Proteomes:UP000233060};
RN   [1] {ECO:0000313|Ensembl:ENSCATP00000012989.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; XP_011948026.1; XM_012092636.1.
DR   AlphaFoldDB; A0A2K5LJ52; -.
DR   STRING; 9531.ENSCATP00000012989; -.
DR   Ensembl; ENSCATT00000037121.1; ENSCATP00000012989.1; ENSCATG00000030599.1.
DR   GeneID; 105600967; -.
DR   KEGG; caty:105600967; -.
DR   CTD; 22801; -.
DR   GeneTree; ENSGT00940000155465; -.
DR   OrthoDB; 3816176at2759; -.
DR   Proteomes; UP000233060; Unplaced.
DR   Bgee; ENSCATG00000030599; Expressed in heart and 3 other cell types or tissues.
DR   GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR   GO; GO:0034681; C:integrin alpha11-beta1 complex; IEA:Ensembl.
DR   GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; IEA:Ensembl.
DR   GO; GO:0038064; F:collagen receptor activity; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:Ensembl.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0006929; P:substrate-dependent cell migration; IEA:Ensembl.
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; 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:SF21; INTEGRIN ALPHA-11; 1.
DR   Pfam; PF01839; FG-GAP; 2.
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; 6.
DR   PROSITE; PS50234; VWFA; 1.
PE   3: Inferred from homology;
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   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003762};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU003762};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233060};
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..1188
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT                   /id="PRO_5014210341"
FT   TRANSMEM        1142..1166
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   REPEAT          91..151
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   DOMAIN          164..345
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   REPEAT          355..406
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          462..527
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          528..586
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          590..650
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
SQ   SEQUENCE   1188 AA;  133399 MW;  495C1143375E70C2 CRC64;
     MDLPRGLVVA WALSLWPGFT DTFNMDTRKP RVIPGSRTAF FGYTVQQHDI SGKKWLVVGA
     PLETNGHQKT GDVYKCPVIH GNCTKLNLGR VTLSNVSERK DNMRLGLSLA TNPKDNSFLA
     CSPLWSHECG SSYYTTGMCS RVNSNFRFSK TVAPALQRCQ TYMDIVIVLD GSNSIYPWVE
     VQHFLINILK KFYIGPGQIQ VGVVQYGEDV VHEFHLNDYR SVKDVVEAAS HIEQRGGTET
     RTAFGIEFAR SEAFQKGGRK GAKKVMIVIT DGESHDSPDL EKVIQQSERD NVTRYAVAVL
     GYYNRRGINP ETFLNEIKYI ASDPDDKHFF NVTDEAALKD IVDALGDRIF SLEGTNKNET
     SFGLEMSQTG FSSHVVEDGV LLGAVGAYDW NGAVLKETSA GKVIPLRESY LKEFPEELKN
     HGAYLGYTVT SVVSSRQGRV YVAGAPRFNH TGKVILFTMH NNRSLTIHQA LRGQQIGSYF
     GSEITSVDID GDGVTDVLLV GAPMYFSEGR ERGKVYVYEL RQNRFVYNGT LKDSHSYQNA
     RFGSSIASVR DLNQDSYDDV VVGAPLEDNH AGAIYIFHGF RGSILKTPKQ RITASELATG
     LQYFGCSIHG QLDLNEDGLI DLAVGALGNA VILWSRPVVQ INASLHFEPS KINIFHRDCK
     RSGRDATCLA AFLCFTPVFL APHFQTTTVG IRYNATMDER RYTPRAHLDE GGDRFTNRAV
     LLSSGQELCE RINFHVLDTA DYVKPVTFSA EYSLEDPDHG PMLDDGWPTT LRVSVPFWNG
     CNEDEHCVPD LVLDARSDLP TAMEYCQRVL RKPTQDCSAY TLSFDTTVFI IESTRRRVAV
     EATLENRGEN AYSTVLNISQ SANLQFASLI QKEDSDGNIE CVNEERRLQK KVCNVSYPFF
     RAKAKVAFRL DFEFSKSIFL HHLEIELAAG SDSNERDSTK EDNVAPLRFH LKYEADVLFT
     RRSSLSHYEV KPNSSLERYD GIGPPFSCIF RIQNLGLFPI HGVMMKITVP IATRGGNRLL
     KLRDFLTDQA NTSCNIWGNS TEYRPTPMEE DLSRAPQLNH SNSDVVSINC NIRLAPNQEI
     NFHLLGNLWL RSLKALKYKS MKIMVNAALQ RQFHSPFIFR EEDPSRQIVF EISKQEDWQV
     PIWIIVGSTL GGLLLLALLV LALWKLGFFK SARRRREPGL DPTPKVLE
//
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