ITA4_XENLA
ID ITA4_XENLA Reviewed; 1032 AA.
AC Q91687; Q06273;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Integrin alpha-4;
DE AltName: Full=Integrin alpha-IV;
DE AltName: Full=VLA-4 subunit alpha;
DE Flags: Precursor;
GN Name=itga4;
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=8787760; DOI=10.1242/dev.122.9.2873;
RA Ramos J.W., Whittaker C.A., Desimone D.W.;
RT "Integrin-dependent adhesive activity is spatially controlled by inductive
RT signals at gastrulation.";
RL Development 122:2873-2883(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 308-379.
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: Fibronectin and V-CAM adhesion receptor.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; U54497; AAA98673.1; -; mRNA.
DR EMBL; L10188; AAA16248.1; -; mRNA.
DR PIR; I51526; I51526.
DR RefSeq; NP_001081444.1; NM_001087975.1.
DR AlphaFoldDB; Q91687; -.
DR SMR; Q91687; -.
DR PRIDE; Q91687; -.
DR GeneID; 397839; -.
DR KEGG; xla:397839; -.
DR CTD; 397839; -.
DR Xenbase; XB-GENE-960094; itga4.S.
DR OrthoDB; 189377at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 397839; Expressed in neurula embryo and 10 other tissues.
DR GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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; Disulfide bond; Glycoprotein; Integrin; Membrane;
KW Metal-binding; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..1032
FT /note="Integrin alpha-4"
FT /id="PRO_0000016246"
FT TOPO_DOM 35..974
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 975..998
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 999..1032
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 36..100
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 113..177
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 186..237
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 238..291
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 292..351
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 353..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 MOTIF 1001..1005
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 320
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 376
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 384
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 SITE 590..591
FT /note="Cleavage"
FT CARBOHYD 81
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 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 660
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 746
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 857
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 91..101
FT /evidence="ECO:0000250"
FT DISULFID 144..165
FT /evidence="ECO:0000250"
FT DISULFID 183..198
FT /evidence="ECO:0000250"
FT DISULFID 485..494
FT /evidence="ECO:0000250"
FT DISULFID 500..556
FT /evidence="ECO:0000250"
FT DISULFID 622..627
FT /evidence="ECO:0000250"
FT DISULFID 698..712
FT /evidence="ECO:0000250"
FT DISULFID 853..889
FT /evidence="ECO:0000250"
FT DISULFID 896..901
FT /evidence="ECO:0000250"
SQ SEQUENCE 1032 AA; 115215 MW; 6486797D83AAE69E CRC64;
MIRDLGKVGK VSLLLDHIWT GILLYTVILT PADCYNIDES SPMLFKGSPG SLFGFSVVLH
SNGEGNWIVV GAPQSSWTTK NVSNPGAILK CKIQQNPNRT CDGLELGNQN GAKCGKTCKE
EQDNQWLGVS LSRQPTKDGQ ILACGHRWKN THFMLSDHKL PYGVCYGIPA DFRTELSKRI
CPCYKDHVRK FGDRYGSCQA GISTFYVEDV IIMGAPGSFY WTGSIFVYNT TENTIKSYVD
LNNAVKFGSY LGYSVGAGHF RTPNGYDVIG GAPQQEQTGR VYIFTYEEKQ LTILFEAGGK
KLGSYFGAAV CAADLNGDGL SDLLVGAPIQ STIREEGRVF VYMNTGSGAM EELKFELSGS
DLYAARFGET IANLGDIDND GFEDVAIAAP QEGDLEGAVY IYNGREKGIT PSFSQRLQGS
KFGYGLRMFG QSLSNVLDID GNGYQDVAIG AFLSDSAVLL RTRPVIIIDA FLKLPSTVNK
TKFECMENGV AVVCMNVTVC FAYQGLDVPG YIVMFYNITS DVRRKSGTPA RFYFVSNGSS
DVISGTVEIR QKSANCKTHQ AFMRKDTRDI FTPIHMESSY YLGKHIVSKR SADDFQPLQP
VLQQKEGKGN VITNKVYFAR YCNLPNCSAD LQITGKRSFP KPFESKTYLA VGGMKSLMIN
ITLFNGGDDA FQTVLRLRLP KGLYFVKVFD LLEKEINCAV NKEENEQTRL DCSVGHFYVD
AFSKQEFSFL LDSSALIRAE EDLVINATVA CANELIQDTM WNNEVSFIVP TRYEIDLNVL
GTVSPFSFVF GPREDKPDDS CIMEEIEYTF NVINAGSSLV PAAKLQISLP NTFAPNDIKL
FNILAVKTTV GECYFDNSTR DCETPKNTRS KIGDLFAFFS RPDKRWLYCI KDDPSCLQIL
CLFGDMERES KATVEVQLEI SHSHLERDEA MLIQFFTTAQ AGFEDSFKII NLNQDHHAYV
VLEALHNLKP KKHVIYMIIG ISLLLGILLF SLLTYILWKV GFFRRKYQPI GTEETSRRES
WNYLNKDEKE VK
