ID ITA6_CHICK Reviewed; 1072 AA.
AC P26007;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 27-NOV-2024, entry version 146.
DE RecName: Full=Integrin alpha-6;
DE AltName: Full=VLA-6;
DE Contains:
DE RecName: Full=Integrin alpha-6 heavy chain;
DE Contains:
DE RecName: Full=Integrin alpha-6 light chain;
DE Flags: Precursor;
GN Name=ITGA6;
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].
RC STRAIN=White leghorn; TISSUE=Retina;
RX PubMed=1826298; DOI=10.1083/jcb.113.2.405;
RA de Curtis I., Quaranta V., Tamura R.N., Reichardt L.F.;
RT "Laminin receptors in the retina: sequence analysis of the chick integrin
RT alpha 6 subunit. Evidence for transcriptional and posttranslational
RT regulation.";
RL J. Cell Biol. 113:405-416(1991).
CC -!- FUNCTION: Integrin alpha-6/beta-1 (ITGA6:ITGB1) is a receptor for
CC laminin on platelets. Integrin alpha-6/beta-1 (ITGA6:ITGB1) is present
CC in oocytes and is involved in sperm-egg fusion. Integrin alpha-6/beta-4
CC (ITGA6:ITGB4) is a receptor for laminin in epithelial cells and it
CC plays a critical structural role in the hemidesmosome.
CC {ECO:0000250|UniProtKB:Q61739}.
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-6 associates with either beta-1 (ITGB1) or beta-4 (ITGB4) to form
CC ITGA6:ITGB1 and ITGA6:ITGB4, respectively.
CC {ECO:0000250|UniProtKB:Q61739}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P23229};
CC Single-pass type I membrane protein {ECO:0000255}. Cell membrane
CC {ECO:0000250|UniProtKB:P23229}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P23229}.
CC -!- DEVELOPMENTAL STAGE: Alpha-6 levels decrease with age.
CC -!- PTM: Phosphorylated in vivo.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; X56559; CAA39909.1; -; mRNA.
DR PIR; A38457; A38457.
DR RefSeq; NP_990620.1; NM_205289.1.
DR AlphaFoldDB; P26007; -.
DR SMR; P26007; -.
DR STRING; 9031.ENSGALP00000056234; -.
DR GlyCosmos; P26007; 10 sites, No reported glycans.
DR GlyGen; P26007; 10 sites.
DR PaxDb; 9031-ENSGALP00000037814; -.
DR Ensembl; ENSGALT00000081430; ENSGALP00000056234; ENSGALG00000034007.
DR Ensembl; ENSGALT00015029397; ENSGALP00015016911; ENSGALG00015012087.
DR GeneID; 396226; -.
DR KEGG; gga:396226; -.
DR CTD; 3655; -.
DR VEuPathDB; HostDB:geneid_396226; -.
DR eggNOG; KOG3637; Eukaryota.
DR InParanoid; P26007; -.
DR PhylomeDB; P26007; -.
DR Reactome; R-GGA-210991; Basigin interactions.
DR Reactome; R-GGA-216083; Integrin cell surface interactions.
DR PRO; PR:P26007; -.
DR Proteomes; UP000000539; Chromosome 7.
DR Bgee; ENSGALG00000034007; Expressed in spermatocyte and 13 other cell types or tissues.
DR GO; GO:0009986; C:cell surface; IDA:AgBase.
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:0031994; F:insulin-like growth factor I binding; ISS:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0038132; F:neuregulin binding; ISS:UniProtKB.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
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:0050900; P:leukocyte migration; IBA:GO_Central.
DR FunFam; 2.130.10.130:FF:000002; integrin alpha-6 isoform X2; 1.
DR FunFam; 2.60.40.1510:FF:000002; integrin alpha-6 isoform X2; 1.
DR FunFam; 2.60.40.1460:FF:000002; Integrin subunit alpha 6; 1.
DR FunFam; 2.60.40.1530:FF:000001; Integrin subunit alpha 7; 1.
DR FunFam; 1.20.5.930:FF:000001; Integrin subunit 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:SF9; INTEGRIN ALPHA-6; 1.
DR Pfam; PF01839; FG-GAP; 2.
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; 5.
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 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell membrane; Cleavage on pair of basic residues;
KW Disulfide bond; Glycoprotein; Integrin; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000250|UniProtKB:P23229"
FT CHAIN 19..1072
FT /note="Integrin alpha-6"
FT /id="PRO_0000016264"
FT CHAIN 19..898
FT /note="Integrin alpha-6 heavy chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016265"
FT CHAIN 902..1072
FT /note="Integrin alpha-6 light chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016266"
FT TOPO_DOM 19..1010
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1011..1036
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1037..1072
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 23..88
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 94..160
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 170..223
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 238..295
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 296..357
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 358..413
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 414..476
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT MOTIF 1039..1043
FT /note="GFFKR motif"
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 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 384
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 388
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 MOD_RES 1070
FT /note="Phosphoserine; by CaMK2"
FT /evidence="ECO:0000255"
FT LIPID 1038
FT /note="S-palmitoyl cysteine; by DHHC3"
FT /evidence="ECO:0000250"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
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 609
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 730
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 747
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 780
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 957
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 79..88
FT /evidence="ECO:0000250"
FT DISULFID 125..148
FT /evidence="ECO:0000250"
FT DISULFID 169..182
FT /evidence="ECO:0000250"
FT DISULFID 498..557
FT /evidence="ECO:0000250"
FT DISULFID 625..631
FT /evidence="ECO:0000250"
FT DISULFID 725..736
FT /evidence="ECO:0000250"
FT DISULFID 880..927
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000250"
FT DISULFID 933..938
FT /evidence="ECO:0000250"
SQ SEQUENCE 1072 AA; 119200 MW; 6DE2B99ECD8B3E44 CRC64;
MAAALLLYLP LLPGLAGAFN LDAENVIGRR GEPGSLFGFS LAMHRQLQPQ EKRLLLVGAP
REKAFPSQQA NRTGGLYSCD ITSSDTRCTR VVFDEDTDPK MESKEDQWMG VTVQSQGPGG
NVVTCAHRYE KRQYVNTVQE TRDIIGRCYV LSQDLTIKDD MDNGVWSFCD GRLRGHEKFG
SCQQGVAATF TRDYHYIVFG APGTYNWKGV VRAEQKNQTF YDLGIFDDGP YEVGDESRQD
KNLVPVPANS YLGFSLDSGK GIVSQDEMTF VSGAPRANHS GAVVLLKKEK NQRALSLEHM
FEGEGLASSF GYDVAVVDLN SDGWQDIVVG APQYFDRSGD IGGAVYIYIN QRGKWEGIKP
IRLNGTADSM FGLAVENVGD INQDGYPDIA VGAPYDGFGK VYIYHGSKNG INTEPAQILD
GEKTGTNFFG YSIAGNMDLD KNSYPDIAVG SLSDSVSVFR SRPVISITKS ITVQPDKLDL
KKKNPEDPSE IWMDVKACFQ YTANPRNLNP RIKINYTFEA ENERRQLGLP SRVRFKDYLS
DQFTASTTLI GQNSKRCVTA KLVLQEKIKD KLRPIPIAVS VNIAGLESGS SSTRKERALP
DLIPILNSNE SETKITKVEF LKEGCGEDNE CHSNLKLQYR FCTREGNEDR FTYLPIENGI
PVLVLKDQKD IALEITVTNN PSDARNPQKD GEDAYEAKLI ATFPDSLTYS AFREMRGYPE
KQLTCGANQN GSQAECELGN PFKRNSNVTF YLILSTTKVN VDTTDLDINL KLETTSTQVN
STAITASAKV VLELLLSLTG VAKPSQVYFG GNIVGESAMK SEDNIGNLIE YEFRVTNLGR
PLKTFGTASL DIQWPKEISN GKWLLYLMKI ESKGLEKVSC QPQNEINVLH VAESHNSRRK
REIAEKQLTD SKTFSLFSER KYKTLDCKVN AQCVDIRCPL KGFDSKASIL LRSRLWNSTF
LEEFSKMNYL DILVRASISV PAAAKNVKLT NEAAQVRVTV FPAKPVALYT GVPWWIIAVA
IFAGVLMLAL LVFLLWKCGF FKRSKKDHYD ATYHKAEIHA QPSDKERLTS DA
//
