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   02-SEP-2026, entry version 140.
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}.
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; X58519; CAA41409.1; -; mRNA.
DR   PIR; S16516; S16516.
DR   RefSeq; NP_990619.2; NM_205288.3.
DR   AlphaFoldDB; P26009; -.
DR   SMR; P26009; -.
DR   FunCoup; P26009; 211.
DR   STRING; 9031.ENSGALP00000065785; -.
DR   GlyCosmos; P26009; 17 sites, No reported glycans.
DR   GlyGen; P26009; 17 sites.
DR   PaxDb; 9031-ENSGALP00000065785; -.
DR   GeneID; 396225; -.
DR   KEGG; gga:396225; -.
DR   CTD; 8516; -.
DR   VEuPathDB; HostDB:geneid_396225; -.
DR   eggNOG; KOG3637; Eukaryota.
DR   InParanoid; P26009; -.
DR   OrthoDB; 5317514at2759; -.
DR   PhylomeDB; P26009; -.
DR   PRO; PR:P26009; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR   GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR   FunFam; 2.130.10.130:FF:000003; Integrin alpha V; 1.
DR   FunFam; 2.60.40.1510:FF:000001; Integrin alpha V; 1.
DR   FunFam; 1.20.5.930:FF:000001; Integrin subunit alpha V; 1.
DR   FunFam; 2.60.40.1460:FF:000001; Integrin, alpha V; 1.
DR   Gene3D; 1.20.5.930; Bicelle-embedded integrin alpha(iib) transmembrane segment; 1.
DR   Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 1.
DR   Gene3D; 2.60.40.1460; Integrin domains. Chain A, domain 2; 1.
DR   Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR   Gene3D; 2.60.40.1530; ntegrin, alpha v. Chain A, domain 4; 1.
DR   InterPro; IPR013517; FG-GAP.
DR   InterPro; IPR013519; Int_alpha_beta-p.
DR   InterPro; IPR000413; Integrin_alpha.
DR   InterPro; IPR018184; Integrin_alpha_C_CS.
DR   InterPro; IPR013649; Integrin_alpha_Ig-like_1.
DR   InterPro; IPR048285; Integrin_alpha_Ig-like_2.
DR   InterPro; IPR048286; Integrin_alpha_Ig-like_3.
DR   InterPro; IPR028994; Integrin_alpha_N.
DR   InterPro; IPR032695; Integrin_dom_sf.
DR   PANTHER; PTHR23220; INTEGRIN ALPHA; 1.
DR   PANTHER; PTHR23220:SF5; INTEGRIN ALPHA-8; 1.
DR   Pfam; PF01839; FG-GAP; 3.
DR   Pfam; PF08441; Integrin_A_Ig_1; 1.
DR   Pfam; PF20805; Integrin_A_Ig_2; 1.
DR   Pfam; PF20806; Integrin_A_Ig_3; 1.
DR   Pfam; PF00357; Integrin_alpha; 1.
DR   PRINTS; PR01185; INTEGRINA.
DR   SMART; SM00191; Int_alpha; 6.
DR   SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR   SUPFAM; SSF69179; Integrin domains; 3.
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
//