ITA8_CHICK
ID ITA8_CHICK Reviewed; 1044 AA.
AC P26009;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Integrin alpha-8;
DE Contains:
DE RecName: Full=Integrin alpha-8 heavy chain;
DE Contains:
DE RecName: Full=Integrin alpha-8 light chain;
DE Flags: Precursor;
GN Name=ITGA8;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=1714374; DOI=10.1002/j.1460-2075.1991.tb07776.x;
RA Bossy B., Bossy-Wetzel E., Reichardt L.F.;
RT "Characterization of the integrin alpha 8 subunit: a new integrin beta 1-
RT associated subunit, which is prominently expressed on axons and on cells in
RT contact with basal laminae in chick embryos.";
RL EMBO J. 10:2375-2385(1991).
RN [2]
RP FUNCTION.
RX PubMed=7541634; DOI=10.1016/0896-6273(95)90268-6;
RA Varnum-Finney B., Venstrom K., Mueller U., Kypta R., Backus C., Chiquet M.,
RA Reichardt L.F.;
RT "The integrin receptor alpha 8 beta 1 mediates interactions of embryonic
RT chick motor and sensory neurons with tenascin-C.";
RL Neuron 14:1213-1222(1995).
RN [3]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=9712662; DOI=10.1523/jneurosci.18-17-06928.1998;
RA Zhang Z., Galileo D.S.;
RT "Retroviral transfer of antisense integrin alpha6 or alpha8 sequences
RT results in laminar redistribution or clonal cell death in developing
RT brain.";
RL J. Neurosci. 18:6928-6938(1998).
CC -!- FUNCTION: Integrin alpha-8/beta-1 functions in the genesis of kidney
CC and probably of other organs by regulating the recruitment of
CC mesenchymal cells into epithelial structures. It recognizes the
CC sequence R-G-D in a wide array of ligands including TNC, FN1, SPP1,
CC TGFB1, TGFB3 and VTN. NPNT is probably its functional ligand in kidney
CC genesis (By similarity). Neuronal receptor for TNC it mediates cell-
CC cell interactions and regulates neurite outgrowth of sensory and motor
CC neurons. {ECO:0000250, ECO:0000269|PubMed:1714374,
CC ECO:0000269|PubMed:7541634, ECO:0000269|PubMed:9712662}.
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-8 associates with beta-1.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC Cell membrane {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Prominently expressed on axons and on cells in
CC contact with basal laminae in embryos.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing tectum (at protein level).
CC {ECO:0000269|PubMed:9712662}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; X58519; CAA41409.1; -; mRNA.
DR PIR; S16516; S16516.
DR RefSeq; NP_990619.1; NM_205288.2.
DR AlphaFoldDB; P26009; -.
DR SMR; P26009; -.
DR STRING; 9031.ENSGALP00000014220; -.
DR PaxDb; P26009; -.
DR GeneID; 396225; -.
DR KEGG; gga:396225; -.
DR CTD; 8516; -.
DR VEuPathDB; HostDB:geneid_396225; -.
DR eggNOG; KOG3637; Eukaryota.
DR InParanoid; P26009; -.
DR OrthoDB; 743479at2759; -.
DR PhylomeDB; P26009; -.
DR PRO; PR:P26009; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
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:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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:0007399; P:nervous system development; 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; PF00357; Integrin_alpha; 1.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 6.
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 Calcium; Cell adhesion; Cell membrane; Cleavage on pair of basic residues;
KW Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW Integrin; Membrane; Metal-binding; Neurogenesis; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1044
FT /note="Integrin alpha-8"
FT /id="PRO_0000016313"
FT CHAIN 24..887
FT /note="Integrin alpha-8 heavy chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016314"
FT CHAIN 888..1044
FT /note="Integrin alpha-8 light chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016315"
FT TOPO_DOM 24..991
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 992..1015
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1016..1044
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 28..90
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 104..165
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 170..222
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 236..288
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 289..354
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 355..413
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 417..480
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT MOTIF 437..439
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 265
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 311
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 313
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 315
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 317
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 319
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 377
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 379
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 381
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 383
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 385
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="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 443
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 445
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 447
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 449
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 587
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 701
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 719
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 751
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 762
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 818
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 877
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 904
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 952
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 986
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 81..88
FT /evidence="ECO:0000250"
FT DISULFID 132..153
FT /evidence="ECO:0000250"
FT DISULFID 169..182
FT /evidence="ECO:0000250"
FT DISULFID 489..500
FT /evidence="ECO:0000250"
FT DISULFID 506..562
FT /evidence="ECO:0000250"
FT DISULFID 623..629
FT /evidence="ECO:0000250"
FT DISULFID 695..708
FT /evidence="ECO:0000250"
FT DISULFID 849..905
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000250"
FT DISULFID 910..915
FT /evidence="ECO:0000250"
SQ SEQUENCE 1044 AA; 116142 MW; 3D59A318B51320CE CRC64;
MPRRQPPRPL LLLSALLCAP ASAFNLDEEK LTVYSGPPGS YFGYSVDFYI PDPSTVSVLV
GAPRANTTQP DIVEGGAVYH CGWPAARCRQ IPFDNTNNRK IKVNGTREPI EFKTNQWFGA
TVKAHKEKVV ACAPLYHWRT LKDSPEKDPV GTCYVAIQNF SAYAEYSPCR NSNADPEGQG
FCQAGFSLDF YKNGDLIVGG PGSFYWQGQV ITASIADIIT NYSFKDILRK LAHEKQTGVA
PPTYDDNYMG YSVAAGEFTG DSEEELVAGV PRGAQNFGYV SIINSSDLTF IQNFTGEQMA
SYFGYTVAVS DVNNDGLDDI LVGAPLFMER EFESKPKEVG QVYLYLQESA FLFRDPQILT
GTEVFGRFGS AITHLGDLNQ DGYNDIAVGA PFAGEDRRGK VLIYNGYSNG LKTDPSQVLN
GAWASQSMPS GFGFTLRGDS DVDKNDYPDL IVGAFGAGKA VVYRARPVVT VNALLILNPM
IVNPDNKTCQ PPGSPLFVAC FTVRVCAAFE GQSISDEIVL KGELQLDSLK QKGAVKRTLF
FDYHQSHHYF SIVMERQKKL YCQDFLVYLR DETEFRDKLS PININLNYSL DESHFKDSLL
VKPILNYYQR PSVTEQAYIL VDCGEDNLCI PDLHLSAVPD KDQLIIGEEN CVMLIINPRN
DGEGAYEAEL HIKIPPEADY TGVERNNKAL RVLSCDYKME NETRMVVCDL GNPMVAGANF
STGIRFSVQH FENSDFSINF ELQIKSSNKI NSTSNLVNLH INITAAAQVQ VRGVSHPPQI
ILPLHNWEPK DEPTKEEEIG PLVEHIYELH NIGPSAINNT VLHVGWPVSS GEEFLLYILH
IQTHGPLHCQ TSSPINIMQI NFAIPQDTPE LAAFLYNSTI SHYIRRREVA VAEPYRRNSA
KILNCTNVKC ILISCNVGQL ERGKSAALKI RSRLWAETFL QRKNDPYTLS SNVSFKVKNM
PYKVQPAKLP EGSIAIRTSV IWSTPNVSFV IPLWVIILAI MLGLLVLAVL TLALWKCGFF
DRARPPQDDM ADREQLTNNK TTDA
