ID I3NB57_ICTTR Unreviewed; 1077 AA.
AC I3NB57;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Integrin subunit alpha V {ECO:0000313|Ensembl:ENSSTOP00000021604.2};
GN Name=ITGAV {ECO:0000313|Ensembl:ENSSTOP00000021604.2};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000021604.2, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000021604.2}
RP IDENTIFICATION.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU003762}.
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; AGTP01034264; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3NB57; -.
DR STRING; 43179.ENSSTOP00000021604; -.
DR Ensembl; ENSSTOT00000025198.2; ENSSTOP00000021604.2; ENSSTOG00000003299.3.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000158361; -.
DR HOGENOM; CLU_004111_6_0_1; -.
DR InParanoid; I3NB57; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0035868; C:alphav-beta3 integrin-HMGB1 complex; IEA:Ensembl.
DR GO; GO:0035867; C:alphav-beta3 integrin-IGF-1-IGF1R complex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; 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:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0034682; C:integrin alphav-beta1 complex; IEA:Ensembl.
DR GO; GO:0034683; C:integrin alphav-beta3 complex; IEA:Ensembl.
DR GO; GO:0034684; C:integrin alphav-beta5 complex; IEA:Ensembl.
DR GO; GO:0034685; C:integrin alphav-beta6 complex; IEA:Ensembl.
DR GO; GO:0034686; C:integrin alphav-beta8 complex; IEA:Ensembl.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:Ensembl.
DR GO; GO:0031528; C:microvillus membrane; IEA:Ensembl.
DR GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR GO; GO:0019960; F:C-X3-C chemokine binding; IEA:Ensembl.
DR GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl.
DR GO; GO:1990430; F:extracellular matrix protein binding; IEA:Ensembl.
DR GO; GO:0017134; F:fibroblast growth factor binding; IEA:Ensembl.
DR GO; GO:0001968; F:fibronectin binding; IEA:Ensembl.
DR GO; GO:0031994; F:insulin-like growth factor I binding; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0038132; F:neuregulin binding; IEA:Ensembl.
DR GO; GO:0001846; F:opsonin binding; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0043277; P:apoptotic cell clearance; IEA:Ensembl.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0050919; P:negative chemotaxis; IEA:Ensembl.
DR GO; GO:2000536; P:negative regulation of entry of bacterium into host cell; IEA:Ensembl.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0010888; P:negative regulation of lipid storage; IEA:Ensembl.
DR GO; GO:0032369; P:negative regulation of lipid transport; IEA:Ensembl.
DR GO; GO:0050748; P:negative regulation of lipoprotein metabolic process; IEA:Ensembl.
DR GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IEA:Ensembl.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; IEA:Ensembl.
DR GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; IEA:Ensembl.
DR GO; GO:0050764; P:regulation of phagocytosis; IEA:Ensembl.
DR GO; GO:1901388; P:regulation of transforming growth factor beta activation; IEA:Ensembl.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:0071604; P:transforming growth factor beta production; IEA:Ensembl.
DR GO; GO:0046718; P:viral entry into host cell; 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; 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:SF4; INTEGRIN ALPHA-V; 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; 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 3: Inferred from homology;
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 Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU003762};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
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..30
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT CHAIN 31..1077
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT /id="PRO_5011825815"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT TRANSMEM 1023..1045
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT REPEAT 32..98
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 109..170
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 173..225
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 237..298
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 321..386
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 387..444
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 448..511
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT DOMAIN 496..654
FT /note="Integrin alpha first immunoglubulin-like"
FT /evidence="ECO:0000259|Pfam:PF08441"
FT DOMAIN 655..793
FT /note="Integrin alpha second immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20805"
FT DOMAIN 801..1012
FT /note="Integrin alpha third immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20806"
FT REGION 1056..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1077 AA; 119515 MW; 2933417066FF75F8 CRC64;
MDSPVRRRLH LCSRRLLLLA SGLLLPLCGA FNLDVDSPAE YSGPEGSYFG FAVDFFVPSA
SSRMFLLVGA PKANTTQPGI VEGGQVLKCD WSSSRRCQPI EFDATGNRDY AKDDPLEFKS
HQWFGASVRS KQDKILACAP LYHWRTELKQ EREPVGTCFL QDGTKTVEYA PCRSKNIDAD
GQGFCQGGFS IDFTKADRVL LGGPGSFYWQ GQLISDQVAE IVSKYDPNVY SIKYNNQLAT
RTAQAIFDDS YLGYSVAVGD FNGDGIDDFV SGVPRAARTL GMVGEMKIVF KNLCVTFYFT
ILHVLMFFST QVYIYDGKNM SSLHNFTGEQ MAAYFGFSVA ATDINGDDYA DVFIGAPLFM
DRGSDGKLQE VGQVSVSLQK ASGEFQTTKL NGFEVFARFG SAIAPLGDLD QDGFNDIAIA
APYGGEDKKG IVYIFNGRST GLNTVPSQIL EGQWAAQSMP PSFGYSMKGA TDIDKNGYPD
LIVGAFGVDR AVLYRARPVI TVNAGLEVYP SILNQDNKTC PLPGTALKVS CFNVRFCLKA
DGKGALPRKL NFQVELLLDK LKQKGAIRRA LFLHNRSPGH SKNMTIFRGG QMQCEELIAY
LRDESEFRDK LTPITIFMEY RLDYRTAADA TGLRPILNQF TPANLSRQAH ILLDCGEDNV
CKPKLEVSVN SDQKKIYIGD DNPLTLIVKA QNQGEGAYEA ELIISMPPQA DFIGVVRNSE
DLARLSCAFK TENQTRQVVC DLGNPMKAGT QLLAGLRFSV HQQSEMDTSV KFDLQIQSSN
LFDKVSPVVS YRVDLAVIAA VEIRGVSSPD HIFLPIPNWE HKENPETEED VGPVVQHIYE
LRNNGPSSFS KAMLNLQWPY KYNNNTLLYI LHYDIDGPMN CTSDMEINPL RIKISSLQTA
EKNDTIAGQG DRNHLITKRD LALSEGDVHT LGCGIAQCLR IVCQVGRLDR GKSAILYVKS
LLWTETFMNK ENQNHSYSLK SSASFNVIEF PYKNLPIEDI FNSTLVTTNV TWGIQPAPMP
VPVWVIILAV LAGLLLLAVL VFVMYRMGFF KRVRPPQEEQ EREQLQPHEN GEGNSET
//
