ITA3_CRIGR
ID ITA3_CRIGR Reviewed; 1051 AA.
AC P17852;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 3.
DT 03-AUG-2022, entry version 119.
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 Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Fibroblast;
RX PubMed=1691184; DOI=10.1016/s0021-9258(19)39252-x;
RA Tsuji T., Yamamoto F., Miura Y., Takio K., Titani K., Pawar S., Osawa T.,
RA Hakomori S.;
RT "Characterization through cDNA cloning of galactoprotein b3 (Gap b3), a
RT cell surface membrane glycoprotein showing enhanced expression on oncogenic
RT transformation. Identification of Gap b3 as a member of the integrin
RT superfamily.";
RL J. Biol. Chem. 265:7016-7021(1990).
RN [2]
RP ALTERNATIVE SPLICING.
RX PubMed=1946438; DOI=10.1073/pnas.88.22.10183;
RA Tamura R.N., Cooper H.M., Collo G., Quaranta V.;
RT "Cell type-specific integrin variants with alternative alpha chain
RT cytoplasmic domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:10183-10187(1991).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Alpha-3A;
CC IsoId=P17852-1; Sequence=Displayed;
CC Name=2; Synonyms=Alpha-3B;
CC IsoId=P17852-2; Sequence=VSP_002720;
CC -!- PTM: Isoform 1, but not isoform 2, is phosphorylated on serine
CC residues.
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; J05281; AAA56794.1; -; mRNA.
DR PIR; A35761; A35761.
DR AlphaFoldDB; P17852; -.
DR SMR; P17852; -.
DR STRING; 10029.XP_003504003.1; -.
DR eggNOG; KOG3637; Eukaryota.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031527; C:filopodium membrane; ISS:UniProtKB.
DR GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Cell junction; Cell membrane;
KW Cell projection; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Integrin;
KW Lipoprotein; Membrane; Metal-binding; Phosphoprotein; Receptor; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT CHAIN 33..1051
FT /note="Integrin alpha-3"
FT /id="PRO_0000016235"
FT CHAIN 33..872
FT /note="Integrin alpha-3 heavy chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016236"
FT CHAIN 876..1051
FT /note="Integrin alpha-3 light chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016237"
FT TOPO_DOM 33..991
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 992..1019
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1020..1051
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 110..171
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 185..235
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 236..292
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 293..354
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 356..411
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 415..477
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REGION 860..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1017..1021
FT /note="GFFKR motif"
FT BINDING 315
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 317
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 319
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 323
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 378
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 380
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 382
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 439
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 441
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 443
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 445
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 447
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 605
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 656
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 697
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 841
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 923
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 926
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 935
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 969
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 94..103
FT /evidence="ECO:0000250"
FT DISULFID 140..162
FT /evidence="ECO:0000250"
FT DISULFID 185..197
FT /evidence="ECO:0000250"
FT DISULFID 485..490
FT /evidence="ECO:0000250"
FT DISULFID 496..550
FT /evidence="ECO:0000250"
FT DISULFID 615..621
FT /evidence="ECO:0000250"
FT DISULFID 694..702
FT /evidence="ECO:0000250"
FT DISULFID 846..904
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000250"
FT DISULFID 911..916
FT /evidence="ECO:0000250"
FT VAR_SEQ 1021..1051
FT /note="RARTRALYEAKRQKAEMKSQPSETERLTDDY -> PTRYYRIMPKYHAVRIR
FT EEERYPPPGSTLPTKKHWVTSWQIRDRYY (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_002720"
SQ SEQUENCE 1051 AA; 116456 MW; 96A8983E8DCD9D5D CRC64;
MGPGPRCAPG DPGWMLGALA LMVAASGRFA FAFNLDTRFL VVKEAVNPGS LFGYSVALHR
QTERQQRYLL LAGAPRDLSV ADGYTNRTGA VYLCPLTALK DDCERMDISE KSDPDHHIIE
DMWLGVTVAS QGPAGRVLVC AHRYTQVLWS GMEDQRRMVG KCYVRGNDLQ LDPGDDWQTY
HNEMCNSNTD YLQTGMCQLG TSGGFTQNTV YFGAPGAYNW KGNSYMIQRK DWDLSEYSYK
GSEDQGNLYI GYTVQVGSAV LHPTYITVVA GAPRHQHMGA VFLLSQESGG DLKRKQVLEG
TQVGAYFGSA IALADLNNDG WQDLLVGAPY YFERKEEVGG AVYVFMNQAG TSFPDQPSLL
LHGPSRSAFG ISIASIGDIN QDGFQDIAVG APFEGLGKVY IYHSSSGGLL RQPQQIVHGD
KLGLPGLSTF GYSLSGKMDV DDNSYPDLLV GSLSDHIVLL RARPVINILQ RTLVARPAVL
DPSLCTPTSC VQVELCFAYN QSAGNPSYRR NITLAYTLEA DRDRRPPRLR FARSQSAVFH
GFLSMPETHC QTLELLLMDN VRDKLRPIVI AMNYSLPLRM PDRLKLGMRS LDAYPVLNQA
QALENHTEVH FQKECGPDNK CDSNLQMRAA FVSEQLQPLS RLQYSRDTKK LFLSINVTNT
PSRERAGEDA HEALLTLEVP PALLLSSVRP SGTCQANETI LCELGNPFKR NQRMELLIAF
EVIGVTLHTR DLKAQLQLST SSHQDNLQPM TLILQVDYTL QASLSLMTHR LQSFFGGTVM
GEAGMKTVED VGSPLKYEFQ VSPVGDGLAA LGTLVLGLEW PYEVTNGKWL LYPTEIIIHS
NESWPCQPPG NLVNPLNLIL SDPGDKPHSP QRRRRQLDPG GDQGSPPVTL AAAKKAKSET
VLTCASGRAR CVWLECPIPD TSNVTNVTVK ARVWNSTFIE DYRDFDRVRV DGWATLFLRT
SIPTINMENK TTWFSVDIDS ELVEELPAEI ELWLVLVAVS AGLLLLGLII ILLWKCGFFK
RARTRALYEA KRQKAEMKSQ PSETERLTDD Y
