ID A0A452DIV7_BOVIN Unreviewed; 1065 AA.
AC A0A452DIV7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Integrin subunit alpha 3 {ECO:0000313|Ensembl:ENSBTAP00000025974.5};
GN Name=ITGA3 {ECO:0000313|Ensembl:ENSBTAP00000025974.5,
GN ECO:0000313|VGNC:VGNC:30315};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000025974.5, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000025974.5, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000025974.5,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000025974.5}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000025974.5};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479, 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 AlphaFoldDB; A0A452DIV7; -.
DR Ensembl; ENSBTAT00000025974.5; ENSBTAP00000025974.5; ENSBTAG00000019498.6.
DR VEuPathDB; HostDB:ENSBTAG00000019498; -.
DR VGNC; VGNC:30315; ITGA3.
DR GeneTree; ENSGT00940000157746; -.
DR OMA; RYNHTGA; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000019498; Expressed in placenta and 104 other cell types or tissues.
DR ExpressionAtlas; A0A452DIV7; baseline.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0060076; C:excitatory synapse; IEA:Ensembl.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0031527; C:filopodium membrane; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0034667; C:integrin alpha3-beta1 complex; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0048787; C:presynaptic active zone membrane; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0097062; P:dendritic spine maintenance; IEA:Ensembl.
DR GO; GO:0035640; P:exploration behavior; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0007613; P:memory; IEA:Ensembl.
DR GO; GO:0048333; P:mesodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IEA:Ensembl.
DR GO; GO:0072006; P:nephron development; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0030510; P:regulation of BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0030111; P:regulation of Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0097205; P:renal filtration; IEA:Ensembl.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:Ensembl.
DR GO; GO:0043588; P:skin development; IEA:Ensembl.
DR GO; GO:0099560; P:synaptic membrane adhesion; IEA:Ensembl.
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; 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:SF89; INTEGRIN ALPHA-3; 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 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; 5.
PE 1: Evidence at protein level;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW ECO:0000256|RuleBase:RU003762};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU003762};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003762};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A452DIV7};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU003762};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
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..32
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT CHAIN 33..1065
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT /id="PRO_5018807910"
FT TRANSMEM 991..1013
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT REPEAT 38..103
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 235..291
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 292..353
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 355..410
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 414..476
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT DOMAIN 461..613
FT /note="Integrin alpha first immunoglubulin-like"
FT /evidence="ECO:0000259|Pfam:PF08441"
FT DOMAIN 614..752
FT /note="Integrin alpha second immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20805"
FT DOMAIN 762..978
FT /note="Integrin alpha third immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20806"
FT REGION 859..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1065 AA; 118487 MW; D12CFDB8773EF8E5 CRC64;
MGPGPSRAAG VLRPLLGMLA LMVAASNRAA SAFNLDTRFL VVKEAGNPGS LFGYSVALHR
QTERQQRYLL LAGAPRDLAV PDGYTNRTGA VYLCPLTAHK NDCERMDIKE KSNPNHIIED
MWLGVTVASQ GPAGRVLVCA HRYTQVLWSG SEDQRRMVGK CYVRGNDLEL DARDDWQTYH
NEMCNSNTDY LETGMCQLGT SGGFTQNTVY FGAPGAYNWK GNSYMIQRKD WDLSEYSYKD
PEDQGNLYIG YTMQVGSAIL HPTNITIVTG APRHQHVGAV FLLSQEAGGD LRRRQVLEGT
QVGAYFGSAI ALADLNNDGW QDLLVGAPYY FERKEEVGGA IYIFMNQAGT SFPDHPSLLL
HGPSRSAFGF SVASIGDVNQ DGFQDIAVGA PFEGLGKVYI YHGSSRGLLR QPQQVIHGEQ
LGLPGLATFG YSLSGQMDVD ENFYPDLLVG SLSDRIVLLR ARPVINILHK TLVAKPSILD
PAFCTATSCV QVELCFAYNQ SAGNPNYRRN ITLAYTLEAD RDRRPPRLHF ARSQSAVFHG
FFSMPEMRCQ TLELLLMDNV RDKLRPITIS MNYSLPLRLP DRPQLGLGSL DAYPVLNQAQ
ALENHTEVQF QKECGQDNRC DSNLQMRAAF VSELGQRLSR LQYRRDLRKL LLSINVTNTP
SRKRAGEDAH EALLTLEVPP TLLLSSVRPP GACQANETIV CELGNPFKRN QRMELLIAFE
VIGVTLHTRE LQAQLQLSTS SHQDDLRPMT LPLLVDYTLQ ASLSMVNHRL QSFFGGTVMG
ESGMKTVEDV GSPLKYEFQV GPMGEGLAAL GTLVLGLEWP YEVSNGKWLL YPTEITVHGN
GSWHCQPPGD LINPLNLTLS VPGDGPPSPQ RRRRQLDPGG GQGPPPVTLA AAKKAKSEIQ
LSCGSDHTHC VWLECPIPDA PVITNVTIQA RVWNSTFIED YRDFDRVRVA SWATLFLRTG
VPTINMENKT VRFSVDIDSD LVEELPAEIE LWLVLVAVSA GLLLLGLIIL LLWKCDFFKR
THYYRIMPKY HAVRIREEER YPPPGSTLPT KKHWVTSWQT RGQYY
//
