ID   ITA11_MOUSE             Reviewed;        1188 AA.
AC   P61622;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Integrin alpha-11;
DE   Flags: Precursor;
GN   Name=Itga11;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-331.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA   Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
CC   -!- FUNCTION: Integrin alpha-11/beta-1 is a receptor for collagen.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-11
CC       associates with beta-1 (By similarity). Interacts with RAB21 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with
CC       I-domains do not undergo protease cleavage.
CC   -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR   EMBL; BC058716; AAH58716.1; -; mRNA.
DR   CCDS; CCDS23265.1; -.
DR   AlphaFoldDB; P61622; -.
DR   SMR; P61622; -.
DR   ComplexPortal; CPX-3125; Integrin alpha11-beta1 complex.
DR   STRING; 10090.ENSMUSP00000034774; -.
DR   GlyGen; P61622; 16 sites.
DR   iPTMnet; P61622; -.
DR   PhosphoSitePlus; P61622; -.
DR   MaxQB; P61622; -.
DR   PaxDb; P61622; -.
DR   PeptideAtlas; P61622; -.
DR   PRIDE; P61622; -.
DR   ProteomicsDB; 301681; -.
DR   UCSC; uc009qal.2; mouse.
DR   MGI; MGI:2442114; Itga11.
DR   eggNOG; KOG3637; Eukaryota.
DR   InParanoid; P61622; -.
DR   PhylomeDB; P61622; -.
DR   Reactome; R-MMU-216083; Integrin cell surface interactions.
DR   ChiTaRS; Itga11; mouse.
DR   PRO; PR:P61622; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P61622; protein.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR   GO; GO:0034681; C:integrin alpha11-beta1 complex; ISO:MGI.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR   GO; GO:0005518; F:collagen binding; ISO:MGI.
DR   GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; ISO:MGI.
DR   GO; GO:0038064; F:collagen receptor activity; 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; ISO:MGI.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR   GO; GO:0038065; P:collagen-activated signaling pathway; ISO:MGI.
DR   GO; GO:0010761; P:fibroblast migration; IMP:MGI.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
DR   GO; GO:0006929; P:substrate-dependent cell migration; IMP:MGI.
DR   Gene3D; 2.130.10.130; -; 2.
DR   Gene3D; 3.40.50.410; -; 1.
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; IPR028994; Integrin_alpha_N.
DR   InterPro; IPR032695; Integrin_dom_sf.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   Pfam; PF01839; FG-GAP; 2.
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   SUPFAM; SSF69179; SSF69179; 3.
DR   SUPFAM; SSF69318; SSF69318; 1.
DR   PROSITE; PS51470; FG_GAP; 7.
DR   PROSITE; PS50234; VWFA; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cell adhesion; Disulfide bond; Glycoprotein; Integrin; Magnesium;
KW   Membrane; Metal-binding; Receptor; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..1188
FT                   /note="Integrin alpha-11"
FT                   /id="PRO_0000016319"
FT   TOPO_DOM        23..1141
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1142..1164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1165..1188
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          24..85
FT                   /note="FG-GAP 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          91..151
FT                   /note="FG-GAP 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   DOMAIN          164..345
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   REPEAT          355..406
FT                   /note="FG-GAP 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          411..461
FT                   /note="FG-GAP 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          462..527
FT                   /note="FG-GAP 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          528..586
FT                   /note="FG-GAP 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          590..650
FT                   /note="FG-GAP 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   BINDING         488
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         490
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         492
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         496
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         551
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         553
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         555
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         559
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         613
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         615
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         617
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         621
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        331
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19656770"
FT   CARBOHYD        358
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        449
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        462
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        528
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        642
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        694
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        857
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        894
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        973
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1031
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1039
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1059
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        76..83
FT                   /evidence="ECO:0000250"
FT   DISULFID        121..139
FT                   /evidence="ECO:0000255"
FT   DISULFID        129..159
FT                   /evidence="ECO:0000255"
FT   DISULFID        659..668
FT                   /evidence="ECO:0000250"
FT   DISULFID        674..729
FT                   /evidence="ECO:0000250"
FT   DISULFID        781..787
FT                   /evidence="ECO:0000250"
FT   DISULFID        881..893
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1188 AA;  133012 MW;  0B0313C90D65422E CRC64;
     MDFPRGLLVA WTLSLWPGFT DTFNMDTRNP RVIAGPSAAF FGYTVQQHDI SGKKWLVVGA
     PMETNGHQKT GDVYKCPVTQ GNCTKLNLGR VTLSNVSERK DNMRLGLSLA TNPKDNSFLA
     CSPLWSHECG SSYYTTGMCS RANSNFRFSK TVAPALQRCQ TYMDIVIVLD GSNSIYPWVE
     VQHFLINILK KFYIGPGQIQ VGIVQYGEDA VHEFHLNDYR SVKDVVEAAS HIEQRGGTET
     RTAFGIEFAR SEAFQKGGRK GAKKVMIVIT DGESHDSPDL EKVIRQSEKD NVTRYAVAVL
     GYYNRRGINP ETFLNEIKYI ASDPDDKHFF NVTDEAALKD IVDALGDRIF SLEGTNKNET
     SFGLEMSQTG FSSHVVEDGI LLGAVGAYDW NGAVLKETSA GKVIPHRESY LKEFPEELKN
     HAAYLGYTVT SVVSSRQGRV YVAGAPRFNH TGKVILFSMH NNRSLTIHQA LRGEQIGSYF
     GSEITSVDVN DDRVTDVLLV GAPMYFSEGR ERGKVYVYNL RQNRFVYNGT LKDSHSYQNA
     RFGSCIASVQ DLNQDSYNDV VVGAPLEDSH RGAIYIFHGF QTNILKKPMQ RITASELAPG
     LQHFGCSIHG QLDLNEDGLV DLAVGALGNA VVLWARPVVQ INASLHFEPS KINIFHKDCK
     RNGRDATCLA AFLCFIPIFL APHFQTATVG IRYNATMDER RYMPRAHLDE GGDQFTNRAV
     LLSSGQEHCQ RINFHVLDTA DYVKPVAFSV EYSLEDPDNG PMLDNGWPTT LRVSVPFWNG
     CNEDEHCVPD LVLDARSDLP TAMEYCQRVL GRPAQDCSSY TLSFDTTVFI IESTRRRVAV
     EATLENRGEN AYSAVLNISQ SENLQFASLI QKDDSDNSIE CVNEERRLHK KVCNVSYPFF
     RAKAKVAFRL DFEFSKSVFL HHLQIHLGAG SDSHEQDSTA DDNTALLRFH LKYEADVLFT
     RSSSLSHFEV KANSSLESYD GIGPPFNCVF KVQNLGFFPI HGVMMKITVP IATRGGNRLL
     MLRDFFTDQG NTSCNIWGNS TEYRSTPTEE DLSHAPQRNH SNSDVVSIIC NLRLAPSQET
     SFYLVGNLWL TSLKALKYRS LKITVNAALQ RQFHSPFIFR EEDPSRQVTF EISKQEDWQV
     PIWIIVGSTL GGLLLLALLV LALWKLGFFK SAKRKREPGL GPIPKELK