ITA5_BOVIN
ID ITA5_BOVIN Reviewed; 385 AA.
AC Q27977;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Integrin alpha-5;
DE AltName: Full=Fibronectin receptor subunit alpha;
DE AltName: Full=Integrin alpha-F;
DE AltName: Full=VLA-5;
DE Contains:
DE RecName: Full=Integrin alpha-5 heavy chain;
DE Contains:
DE RecName: Full=Integrin alpha-5 light chain;
DE Flags: Fragment;
GN Name=ITGA5;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7545439; DOI=10.1095/biolreprod53.1.153;
RA Maclaren L.A., Wildeman A.G.;
RT "Fibronectin receptors in preimplantation development: cloning, expression,
RT and localization of the alpha 5 and beta 1 integrin subunits in bovine
RT trophoblast.";
RL Biol. Reprod. 53:153-165(1995).
CC -!- FUNCTION: Integrin alpha-5/beta-1 (ITGA5:ITGB1) is a receptor for
CC fibronectin and fibrinogen. It recognizes the sequence R-G-D in its
CC ligands. ITGA5:ITGB1 binds to PLA2G2A via a site (site 2) which is
CC distinct from the classical ligand-binding site (site 1) and this
CC induces integrin conformational changes and enhanced ligand binding to
CC site 1. ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and
CC mediates R-G-D-dependent cell adhesion to FBN1. ITGA5:ITGB1 is a
CC receptor for IL1B and binding is essential for IL1B signaling.
CC ITGA5:ITGB3 is a receptor for soluble CD40LG and is required for
CC CD40/CD40LG signaling (By similarity). {ECO:0000250|UniProtKB:P08648}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit
CC is composed of a heavy and a light chain linked by a disulfide bond.
CC Alpha-5 associates with beta-1. Interacts with HPS5 and NISCH.
CC Interacts with RAB21 and COMP. Interacts with CIB1. ITGA5:ITGB1
CC interacts with CCN3. ITGA5:ITGB1 interacts with FBN1. ITGA5:ITGB1
CC interacts with IL1B. ITGA5:ITGB1 interacts with ACE2. Interacts with
CC ANGPT2. {ECO:0000250|UniProtKB:P08648}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC Cell junction, focal adhesion {ECO:0000250|UniProtKB:P08648}. Cell
CC surface {ECO:0000250|UniProtKB:P08648}.
CC -!- PTM: Proteolytic cleavage by PCSK5 mediates activation of the
CC precursor. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; U10866; AAA80572.1; -; mRNA.
DR PIR; I46060; I46060.
DR AlphaFoldDB; Q27977; -.
DR SMR; Q27977; -.
DR STRING; 9913.ENSBTAP00000018261; -.
DR PaxDb; Q27977; -.
DR PRIDE; Q27977; -.
DR eggNOG; KOG3637; Eukaryota.
DR InParanoid; Q27977; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; ISS:UniProtKB.
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 InterPro; IPR013649; Integrin_alpha-2.
DR InterPro; IPR032695; Integrin_dom_sf.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR SUPFAM; SSF69179; SSF69179; 2.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell junction; Cleavage on pair of basic residues;
KW Disulfide bond; Glycoprotein; Integrin; Membrane; Metal-binding; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN <1..>385
FT /note="Integrin alpha-5"
FT /id="PRO_0000016247"
FT CHAIN <1..252
FT /note="Integrin alpha-5 heavy chain"
FT /id="PRO_0000409493"
FT CHAIN 253..>385
FT /note="Integrin alpha-5 light chain"
FT /id="PRO_0000016248"
FT TOPO_DOM <1..353
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..>385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1..7
FT /evidence="ECO:0000250"
FT DISULFID 74..87
FT /evidence="ECO:0000250"
FT DISULFID 226..269
FT /evidence="ECO:0000250"
FT DISULFID 274..279
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 385
SQ SEQUENCE 385 AA; 42943 MW; EBE199BCEF51D9C8 CRC64;
CGEENICVPD LQLEVFGEQN HVYLGDKNSL NLTFHAQNVG EGGAYEAELR VTAPPEAEYS
GLVRHPGNFS SLSCDYFAVN QSRLLVCDLG NPMKAGASLW GGLRFTVPHL RDIKKTIQFD
FQILSKNLNN VQSDVVSFRL SVEAQAQVSL NGVSKPEAVL FPMSDWHPQD QPQEEGDVGP
AVHHVYELIN LGPSSISQGV LELSCPHALD GQQLLYVTRV TGLSNCTTSH PPNPEGLELD
PEGSQHHRLQ RRMFLGRSPA SSGPQILKCP EAECFKLRCE LGPLHRQESR SLQLHFRVWA
KAFLQREHQP FSLQCEAVYE ALKMPYKILP RQLPQKALQV ATAVQWIKAE GSHGVPLWII
ILAILIGLLL LGLLIYILYN LFFFK
