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Database: UniProt
Entry: G1PCQ7_MYOLU
LinkDB: G1PCQ7_MYOLU
Original site: G1PCQ7_MYOLU 
ID   G1PCQ7_MYOLU            Unreviewed;       937 AA.
AC   G1PCQ7;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Integrin subunit alpha 11 {ECO:0000313|Ensembl:ENSMLUP00000008213.2};
GN   Name=ITGA11 {ECO:0000313|Ensembl:ENSMLUP00000008213.2};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000008213.2, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000008213.2, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSMLUP00000008213.2}
RP   IDENTIFICATION.
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   EMBL; AAPE02041957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAPE02041958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAPE02041959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G1PCQ7; -.
DR   STRING; 59463.ENSMLUP00000008213; -.
DR   Ensembl; ENSMLUT00000009013.2; ENSMLUP00000008213.2; ENSMLUG00000008993.2.
DR   eggNOG; KOG3637; Eukaryota.
DR   GeneTree; ENSGT00940000155465; -.
DR   HOGENOM; CLU_004111_2_1_1; -.
DR   InParanoid; G1PCQ7; -.
DR   OMA; HGIGPPF; -.
DR   TreeFam; TF105391; -.
DR   Proteomes; UP000001074; Unassembled WGS sequence.
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   Gene3D; 1.20.5.930; Bicelle-embedded integrin alpha(iib) transmembrane segment; 1.
DR   Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 1.
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   SMART; SM00191; Int_alpha; 4.
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; 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   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:UP000001074};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003762};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU003762}.
FT   TRANSMEM        891..915
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT   DOMAIN          1..98
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   REPEAT          104..155
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          211..276
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          277..335
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          339..399
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
SQ   SEQUENCE   937 AA;  105391 MW;  6B01088301F6DE4F CRC64;
     SEAFQKGGRK GAKKVMIVIT DGESHDSPDL EKVIQQSERD NVTRYAVAVL GYYNRRGINP
     ETFLNEIKYI ASDPDDKHFF NVTDEAALKD IVDAGDRIFS LEGTNKNETS FGLEMSQTGF
     SSHVVEDGIL LGAVGAYDWN GAVLKETSGG KVIPLRESYL KEFPEELRNH GAYLGYTVTS
     VVSSRQGRVY VAGAPRFNHT GKAILFTMHN NRSLTIHQAL RGEQIGSYYG SEITAVDIDG
     DGVTDVLLVG APMYFSEGRE RGRVYVYNLR QNRFVYNGTL QDSHSYQNAR FGASIAWVRD
     LNQDSYNDVV VGAPLEDNHE GAIYIFHGFR GSLLKTPKQR IAASELAPGL QYFGCSIHGQ
     LDLNEDGLVD LAVGALGNAV ILWSRPVVQI NASLHFEPPK INIFHRDCKR SGRDATCLAA
     FLCFTPVFLA PHFQTATVGK HQVQCTMDER RYTRAHLDEG GDRYTNRAVL LSSGQEHCDR
     ISFHVLDTAD YVKPVTFSVE YSLEDPDHGP MLDDGWPTTL RVSVPFWNGC NEDEHCVPDL
     LLDARSDLPT AMEYCQRVLR KPAQDCSAYT LSFDTTVFII ESTRRRVAVE AMLENRGENA
     YSTVLNISQS ANLQFASLIQ REDSDGSIEC VNEERRLHKK VCNVSYPFFR AKAKVAFRLD
     FEFSKSVFLH HLEVQLTAGS DSDEEESTKE DNAALLRFHL KYEADILFTR SSSLSHYEVK
     PNSSLESYNG IGPPFHCIFK IQNLGLFPIH GVMMKITVPI ATRSGNRLLM LRDFLTDQVN
     TSCNVWGNST EYRHSPMEED LSRTPQLNHS NSDVVSINCH VRLAPNQEIN FHLLGNLWLR
     SLKALKYKLM KITVHAAVQR QFHSPFIFRE EDPSRQITFE ISKQEDWQIP IWIIVGSTLG
     GLLLLALLVL ALWKLGFFKS AKRRREPGLD PTPKALE
//
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