ID   ITA1_CHICK              Reviewed;         285 AA.
AC   Q90615;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Integrin alpha-1;
DE   AltName: Full=Laminin and collagen receptor;
DE   AltName: Full=VLA-1;
DE   Flags: Fragment;
GN   Name=ITGA1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Gizzard;
RX   PubMed=7521332; DOI=10.1016/s0021-9258(17)31717-9;
RA   Kern A., Briesewitz R., Bank I., Marcantonio E.E.;
RT   "The role of the I domain in ligand binding of the human integrin alpha 1
RT   beta 1.";
RL   J. Biol. Chem. 269:22811-22816(1994).
CC   -!- FUNCTION: Integrin alpha-1/beta-1 is a receptor for laminin and
CC       collagen. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R
CC       in collagen. Involved in anchorage-dependent, negative regulation of
CC       EGF-stimulated cell growth (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-1 associates
CC       with beta-1.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
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; U10114; AAA59067.1; -; mRNA.
DR   AlphaFoldDB; Q90615; -.
DR   SMR; Q90615; -.
DR   STRING; 9031.ENSGALP00000023976; -.
DR   PaxDb; Q90615; -.
DR   VEuPathDB; HostDB:geneid_395951; -.
DR   eggNOG; KOG3637; Eukaryota.
DR   InParanoid; Q90615; -.
DR   PhylomeDB; Q90615; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISS:UniProtKB.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   Pfam; PF00092; VWA; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Glycoprotein; Integrin; Membrane; Receptor;
KW   Reference proteome; Transmembrane.
FT   CHAIN           <1..>285
FT                   /note="Integrin alpha-1"
FT                   /id="PRO_0000174216"
FT   TOPO_DOM        <1..>285
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          66..279
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   CARBOHYD        2
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        208
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        232
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT   NON_TER         285
SQ   SEQUENCE   285 AA;  31503 MW;  1B05D3246CD5CA7E CRC64;
     ENMTFGTTLV TNPKGGFLAC GPLYAYKCGR LHYTTGVCSN VSSTFETVKA VAPSVQECKT
     QLDIVIVLDG SNSIYPWESV TAFLNSLLRN MDIGPQQTQV GIVQYGQTVV HEFYLNTYST
     TEEVMDAALR IRQRGGTQTM TALGIDTARE EAFTEAHGAR RGVQKVMVIV TDGESHDNYR
     LQEVIDKCED ENIQRFAIAI LGSYSRGNLS TEKFVEEIKS IASKPTEKHF FNVSDELALV
     TIVEALGERI FALEATTDQQ AASFEMEMSQ AGFSAHYSQD WVMLG