ITA5_XENLA
ID ITA5_XENLA Reviewed; 1050 AA.
AC Q06274;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 106.
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: Precursor;
GN Name=itga5;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7619730; DOI=10.1016/0925-4773(94)00335-k;
RA Joos T.O., Whittaker C.A., Meng F., Desimone D.W., Gnau V., Hausen P.;
RT "Integrin alpha 5 during early development of Xenopus laevis.";
RL Mech. Dev. 50:187-199(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 318-393.
RX PubMed=8404528; DOI=10.1242/dev.117.4.1239;
RA Whittaker C.A., Desimone D.W.;
RT "Integrin alpha subunit mRNAs are differentially expressed in early Xenopus
RT embryos.";
RL Development 117:1239-1249(1993).
CC -!- FUNCTION: Integrin alpha-5/beta-1 (ITGA5:ITGB1) is a receptor for
CC fibronectin. It recognizes the sequence R-G-D in its ligands.
CC ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-
CC D-dependent cell adhesion to FBN1. ITGA5:ITGB1 is a receptor for IL1B
CC and binding is essential for IL1B signaling. ITGA5:ITGB3 is a receptor
CC for soluble CD40LG and is required for CD40/CD40LG signaling (By
CC 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.
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 -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; U12683; AAA99668.1; -; mRNA.
DR EMBL; L10191; AAA16249.1; -; mRNA.
DR PIR; I51527; I51527.
DR RefSeq; NP_001081072.1; NM_001087603.1.
DR AlphaFoldDB; Q06274; -.
DR SMR; Q06274; -.
DR GeneID; 394366; -.
DR KEGG; xla:394366; -.
DR CTD; 394366; -.
DR Xenbase; XB-GENE-866304; itga5.L.
DR OrthoDB; 743479at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 394366; Expressed in egg cell and 19 other tissues.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; ISS:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell junction; Cleavage on pair of basic residues;
KW Disulfide bond; Glycoprotein; Integrin; Membrane; Metal-binding; 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-5"
FT /id="PRO_0000016255"
FT CHAIN 33..932
FT /note="Integrin alpha-5 heavy chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016256"
FT CHAIN 933..1050
FT /note="Integrin alpha-5 light chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016257"
FT TOPO_DOM 33..996
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 997..1022
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1023..1050
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 34..99
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 116..175
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 183..235
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 249..301
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 302..367
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 368..426
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 430..493
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT MOTIF 1025..1029
FT /note="GFFKR motif"
FT BINDING 270
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 272
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 274
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 324
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 330
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 398
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 454
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 456
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 458
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 460
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 462
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT CARBOHYD 75
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 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 600
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 649
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 714
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 763
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 861
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 90..99
FT /evidence="ECO:0000250"
FT DISULFID 145..166
FT /evidence="ECO:0000250"
FT DISULFID 182..195
FT /evidence="ECO:0000250"
FT DISULFID 502..513
FT /evidence="ECO:0000250"
FT DISULFID 519..575
FT /evidence="ECO:0000250"
FT DISULFID 636..642
FT /evidence="ECO:0000250"
FT DISULFID 708..721
FT /evidence="ECO:0000250"
FT DISULFID 862..910
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000250"
FT DISULFID 917..922
FT /evidence="ECO:0000250"
SQ SEQUENCE 1050 AA; 115962 MW; 10ED961535B8D918 CRC64;
MQLPRGSRVP GLVATFLFPV LCALLTFSSV RGFNLAVEQP AVYTGASGSF FGFSVDFYLP
DAQSISILVG APKANTSQPG VFEGGAVFYC PWQRNGTNCT EISFDSHGDR QRELFDTPQP
KHMESKSEQW FGATVRAHGK TILACAPRYS WRTEKEEKRS DPVGTCYLSV NNFTTFVEYS
PCRTDFSDAA GQGYCQGGFS AEFTKSGRVL LGGPGSYFWQ GQVITATQDE IQEAYYPEYF
VLEYKKQMQT RQAASSYDDS YFGYSVAVGE FSEDATEDFV VGVPKGNITY GYVTILNGTD
LRSLYNFSGE QMASYFGYSV SATDLNSDGL DDLLIGAPLF MDRTHDGRVQ EVGRVYVYLQ
GDHMESTPHL ILTGMEEYGR FGSSIASLGD LDQDGFNDIA IGAPFGGEAQ RGAVFIFNGQ
PGGVDSKPSQ VLQGQWGSSQ QPSFFGLSTR GGHDLDGNGY PDLIVGAFGV DTTLVYRGRP
IIHASASLSI SPNMFNPEEK TCTLEGNASA VSCINLSFCL NASGKHVPNS IGIKVELQLD
QTKQKGAVKR ALFLKTRQPQ LTQTIHLLNG GKEECRAMKI YLREESEFRD KLSPIYVGLN
FSLDPLAPAD AHGLMPIFNY KTKNYIEQKA QIQLDCGEDN ICVPDLKLNV SGDRKSVYLG
DENFLTLFFN AQNLGGGAYE AELYVTLPPE AEYSGIVRNN EHLLILPCAY EMENQTRLVI
CDLGNPMKAG ASLAGGLRFT VPHLRDSSHK VQFDFQIRSK NQNNSQSETV HLALNVEAHS
TVSFFGASKP DSVIFPVANW KPGRNPVTGQ EAGPEVKHVY ELVNFGPSSI SQGILELRCP
MRVNKEYAMY VMSYAVQGLT NCTSNHPANA LHLQHSPTDH PPTLNPKTVH HVERRDTARL
ISGSSNVLKC NEPHVDCFHL HCDVGPLEKQ KRAILRVNFL VWANTFMQKE NQGFTLQCDA
LYHIQKLPYK ILPHVYPKGT HQVDTAIHWA KPESSYGVPL WIIILAILIG LLLLALLIYV
LYKLGFFKRS YQYGTAMEKA ELKPQAASEA
