ID A0A3Q0D521_MESAU Unreviewed; 1073 AA.
AC A0A3Q0D521;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 18-JUN-2025, entry version 27.
DE RecName: Full=Integrin alpha-6 {ECO:0000256|ARBA:ARBA00068408};
DE AltName: Full=CD49 antigen-like family member F {ECO:0000256|ARBA:ARBA00080506};
DE AltName: Full=Integrin alpha-7 {ECO:0000256|ARBA:ARBA00068411};
DE AltName: Full=VLA-6 {ECO:0000256|ARBA:ARBA00079514};
GN Name=Itga6 {ECO:0000313|RefSeq:XP_021088332.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021088332.1};
RN [1] {ECO:0000313|RefSeq:XP_021088332.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=28071753;
RA McCann K.E., Sinkiewicz D.M., Norvelle A., Huhman K.L.;
RT "De novo assembly, annotation, and characterization of the whole brain
RT transcriptome of male and female Syrian hamsters.";
RL Sci. Rep. 7:40472-40472(2017).
RN [2] {ECO:0000313|RefSeq:XP_021088332.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
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. ITGA6:ITGB4
CC binds to NRG1 (via EGF domain) and this binding is essential for NRG1-
CC ERBB signaling. ITGA6:ITGB4 binds to IGF1 and this binding is essential
CC for IGF1 signaling. ITGA6:ITGB4 binds to IGF2 and this binding is
CC essential for IGF2 signaling. {ECO:0000256|ARBA:ARBA00054656}.
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. ITGA6:ITGB1 is found in a
CC complex with CD9; interaction takes place in oocytes and is involved in
CC sperm-egg fusion. ITGA6:ITGB4 is found in a ternary complex with NRG1
CC and ERBB3. ITGA6:ITGB4 is found in a ternary complex with IGF1 and
CC IGF1R. ITGA6:ITGB4 interacts with IGF2. Interacts with ADAM9. Interacts
CC with RAB21. Interacts with MDK. ITGA6:ITGB1 interacts with MDK; this
CC interaction mediates MDK-induced neurite outgrowth. Interacts with
CC CD82; this interaction down-regulates ITGA6-mediated cell adhesion.
CC {ECO:0000256|ARBA:ARBA00062424}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004193};
CC Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004251}. Membrane
CC {ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein
CC {ECO:0000256|RuleBase:RU003762}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family.
CC {ECO:0000256|ARBA:ARBA00008054, ECO:0000256|RuleBase:RU003762}.
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DR RefSeq; XP_021088332.1; XM_021232673.1.
DR RefSeq; XP_040601502.1; XM_040745568.1.
DR AlphaFoldDB; A0A3Q0D521; -.
DR GeneID; 101839961; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:TreeGrafter.
DR GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR GO; GO:0005178; F:integrin binding; IEA:TreeGrafter.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:TreeGrafter.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:TreeGrafter.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:TreeGrafter.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0050900; P:leukocyte migration; IEA:TreeGrafter.
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; 4.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE 3: Inferred from homology;
KW ADP-ribosylation {ECO:0000256|ARBA:ARBA00022765};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW ECO:0000256|RuleBase:RU003762};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU003762};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003762};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU003762};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU003762};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003762};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU003762}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT CHAIN 24..1073
FT /note="Integrin alpha-6"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT /id="PRO_5017853940"
FT TRANSMEM 1013..1037
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT REPEAT 30..95
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 301..363
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 364..419
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 420..479
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT DOMAIN 464..624
FT /note="Integrin alpha first immunoglubulin-like"
FT /evidence="ECO:0000259|Pfam:PF08441"
FT DOMAIN 626..791
FT /note="Integrin alpha second immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20805"
FT DOMAIN 797..1003
FT /note="Integrin alpha third immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20806"
SQ SEQUENCE 1073 AA; 119311 MW; D253E13348597DB4 CRC64;
MAVAGRLCLL YLSAGLLARL GAAFNLDTRE DNVIRKSGDP GSLFGFSLAM HQQLQPEDKR
LLLVGAPRAE ALPLQRANRT GGLYSCDITS RGPCTRIEFD NDADPMSESK EDQWMGVTVQ
SQGPGGKVVT CAHRYEKRQH VNTKQESRDI FGRCYVLSQN LRIEDDMDGG DWSFCDGRLR
GHEKFGSCQQ GVAATFTKDF HYIVFGAPGT YNWKGIVRVE QKNNTFFDMN IFEDGPYEVG
GETDHDESLV PVPANSYLGF SLDSGKGIVS KDDITFVSGA PRANHSGAVV LLKRDMKSAH
LLPEHIFDGE GLASSFGYDV AVVDLNADGW QDIVIGAPQY FDRDGEVGGA VYIYINQQGK
WSNVKPVRLN GTKDSMFGIS VKNIGDINQD GYPDIAVGAP YDDLGKVFIY HGSPAGINTK
PTQVLEGTSP YFGYSIAGNM DLDKNSYPDV AVGSLSDSVT IFRSRPVINI LKTVTVTPSR
IDLRQKSLCG SPSGICLKVK ACFEYTAKPS DYNPPISILG ILEAEKERRK SGLSSRVQFR
NQGSEPKYTQ ELTLNRQKQR ACMEEILWLQ ENIRDKLRPI PITASVEIQE TSSRRRVNSL
PEVLPILNSN EAKTVQTDVH FLKEGCGDDN VCNSNLKLEY KFCTREGSQD KFSYLPIQKG
IPELVLKDQK DIALEITVTN GPSDPRNPRK DGDDAHEAKL IATFPDTLTY SAYRELRAFP
EKQLSCVANQ NGSQADCELG NPFKRNSSVT FYLVLSTTEV TFDTTDLDIN LKLETTSNQD
NLAPITAKAK VVIELLLSVS GVAKPSQVYF GGTVVGEQAM KSEDEVGSLI EYEFRVINLG
KPLKNLGTAT LNIQWPKEIS NGKWLLYLVK VESKGLEQII CEPHSEINFL KLKESHNSRK
KREIPEKQID DSRKFSLFSE RKYQTLNCSV NVKCVNIRCP LRGLDSKASL VLRSRLWNST
FLEEYSKLNY LDILVRASID VAAAAQNIKL PHAGTQVRVT VFPSKTAAQY SGIAWWIILL
AVLAGILMLA LLVFLLWKCG FFKRNKKDHY DTTYHKAEIH TQPSDKERLT SDA
//
