ITA3_BOVIN
ID ITA3_BOVIN Reviewed; 1050 AA.
AC F1MMS9;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Integrin alpha-3;
DE AltName: Full=CD49 antigen-like family member C;
DE AltName: Full=Galactoprotein B3;
DE Short=GAPB3;
DE AltName: Full=VLA-3 subunit alpha;
DE AltName: CD_antigen=CD49c;
DE Contains:
DE RecName: Full=Integrin alpha-3 heavy chain;
DE Contains:
DE RecName: Full=Integrin alpha-3 light chain;
DE Flags: Precursor;
GN Name=ITGA3;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
CC -!- FUNCTION: Integrin alpha-3/beta-1 is a receptor for fibronectin,
CC laminin, collagen, epiligrin, thrombospondin and CSPG4. Integrin alpha-
CC 3/beta-1 provides a docking site for FAP (seprase) at invadopodia
CC plasma membranes in a collagen-dependent manner and hence may
CC participate in the adhesion, formation of invadopodia and matrix
CC degradation processes, promoting cell invasion. Alpha-3/beta-1 may
CC mediate with LGALS3 the stimulation by CSPG4 of endothelial cells
CC migration. {ECO:0000250|UniProtKB:P26006}.
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-3 associates with beta-1. Interacts with HPS5. Interacts with FAP
CC (seprase); the interaction occurs at the cell surface of invadopodia
CC membrane in a collagen-dependent manner.
CC {ECO:0000250|UniProtKB:P26006}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell
CC projection, invadopodium membrane {ECO:0000250|UniProtKB:P26006};
CC Single-pass type I membrane protein {ECO:0000255}. Cell projection,
CC filopodium membrane {ECO:0000250|UniProtKB:P26006}; Single-pass type I
CC membrane protein {ECO:0000255}. Note=Enriched preferentially at
CC invadopodia, cell membrane protrusions that correspond to sites of cell
CC invasion, in a collagen-dependent manner.
CC {ECO:0000250|UniProtKB:P26006}.
CC -!- PTM: Phosphorylated on serine residues. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFC03087018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03120550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001289593.1; NM_001302664.1.
DR AlphaFoldDB; F1MMS9; -.
DR SMR; F1MMS9; -.
DR STRING; 9913.ENSBTAP00000025974; -.
DR PaxDb; F1MMS9; -.
DR PeptideAtlas; F1MMS9; -.
DR PRIDE; F1MMS9; -.
DR Ensembl; ENSBTAT00000054196; ENSBTAP00000050366; ENSBTAG00000019498.
DR GeneID; 508490; -.
DR KEGG; bta:508490; -.
DR CTD; 3675; -.
DR VEuPathDB; HostDB:ENSBTAG00000019498; -.
DR VGNC; VGNC:30315; ITGA3.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000157746; -.
DR HOGENOM; CLU_004111_1_0_1; -.
DR InParanoid; F1MMS9; -.
DR OrthoDB; 743479at2759; -.
DR TreeFam; TF105391; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000019498; Expressed in placenta and 104 other tissues.
DR ExpressionAtlas; F1MMS9; baseline.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0031527; C:filopodium membrane; ISS:UniProtKB.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
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:0050900; P:leukocyte migration; IBA:GO_Central.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:UniProtKB.
DR Gene3D; 2.130.10.130; -; 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; IPR018184; Integrin_alpha_C_CS.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SUPFAM; SSF69179; SSF69179; 3.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE 3: Inferred from homology;
KW Calcium; Cell adhesion; Cell junction; Cell membrane; Cell projection;
KW Cleavage on pair of basic residues; Disulfide bond; Glycoprotein; Integrin;
KW Lipoprotein; Membrane; Metal-binding; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..1050
FT /note="Integrin alpha-3"
FT /id="PRO_0000412820"
FT CHAIN 33..871
FT /note="Integrin alpha-3 heavy chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000412821"
FT CHAIN 875..1050
FT /note="Integrin alpha-3 light chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000412822"
FT TOPO_DOM 33..990
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 991..1011
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1012..1050
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 38..103
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 108..170
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 184..234
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 235..291
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 292..353
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 355..410
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 414..476
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REGION 859..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1020
FT /note="Interaction with HPS5"
FT /evidence="ECO:0000250"
FT MOTIF 1016..1020
FT /note="GFFKR motif"
FT BINDING 314
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 316
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 318
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 322
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 377
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 379
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 381
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 385
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 438
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 440
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 442
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 444
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 446
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT LIPID 1015
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 604
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 696
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 840
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 856
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 925
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 934
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 968
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 94..103
FT /evidence="ECO:0000250"
FT DISULFID 139..161
FT /evidence="ECO:0000250"
FT DISULFID 184..196
FT /evidence="ECO:0000250"
FT DISULFID 484..489
FT /evidence="ECO:0000250"
FT DISULFID 495..549
FT /evidence="ECO:0000250"
FT DISULFID 614..620
FT /evidence="ECO:0000250"
FT DISULFID 693..701
FT /evidence="ECO:0000250"
FT DISULFID 845..903
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000250"
FT DISULFID 910..915
FT /evidence="ECO:0000250"
SQ SEQUENCE 1050 AA; 116407 MW; 64F107D7DA201DF8 CRC64;
MGPGPSRAAG VLRPLLGMLA LMVAASNRAA SAFNLDTRFL VVKEAGNPGS LFGYSVALHR
QTERQQRYLL LAGAPRDLAV PDGYTNRTGA VYLCPLTAHK NDCERMDIKE KSNPNHIIED
MWLGVTVASQ GPAGRVLVCA HRYTQVLWSG SEDQRRMVGK CYVRGNDLEL DARDDWQTYH
NEMCNSNTDY LETGMCQLGT SGGFTQNTVY FGAPGAYNWK GNSYMIQRKD WDLSEYSYKD
PEDQGNLYIG YTMQVGSAIL HPTNITIVTG APRHQHVGAV FLLSQEAGGD LRRRQVLEGT
QVGAYFGSAI ALADLNNDGW QDLLVGAPYY FERKEEVGGA IYIFMNQAGT SFPDHPSLLL
HGPSRSAFGF SVASIGDVNQ DGFQDIAVGA PFEGLGKVYI YHGSSRGLLR QPQQVIHGEQ
LGLPGLATFG YSLSGQMDVD ENFYPDLLVG SLSDRIVLLR ARPVINILHK TLVAKPSILD
PAFCTATSCV QVELCFAYNQ SAGNPNYRRN ITLAYTLEAD RDRRPPRLHF ARSQSAVFHG
FFSMPEMRCQ TLELLLMDNV RDKLRPITIS MNYSLPLRLP DRPQLGLGSL DAYPVLNQAQ
ALENHTEVQF QKECGQDNRC DSNLQMRAAF VSELGQRLSR LQYRRDLRKL LLSINVTNTP
SRKRAGEDAH EALLTLEVPP TLLLSSVRPP GACQANETIV CELGNPFKRN QRMELLIAFE
VIGVTLHTRE LQAQLQLSTS SHQDDLRPMT LPLLVDYTLQ ASLSMVNHRL QSFFGGTVMG
ESGMKTVEDV GSPLKYEFQV GPMGEGLAAL GTLVLGLEWP YEVSNGKWLL YPTEITVHGN
GSWHCQPPGD LINPLNLTLS VPGDGPPSPQ RRRRQLDPGG GQGPPPVTLA AAKKAKSEIQ
LSCGSDHTHC VWLECPIPDA PVITNVTIQA RVWNSTFIED YRDFDRVRVA SWATLFLRTG
VPTINMENKT VRFSVDIDSD LVEELPAEIE LWLVLVAVSA GLLLLGLIIL LLWKCGFFKR
ARTRALYEAK RQKAEMKSQP SETERLTEDY
