ID H0WNK8_OTOGA Unreviewed; 768 AA.
AC H0WNK8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=ITGB8 {ECO:0000313|Ensembl:ENSOGAP00000003416.2};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000003416.2, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000003416.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251,
CC ECO:0000256|RuleBase:RU000633}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU000633}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family.
CC {ECO:0000256|ARBA:ARBA00007449, ECO:0000256|RuleBase:RU000633}.
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DR EMBL; AAQR03057271; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03057272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003788538.1; XM_003788490.1.
DR AlphaFoldDB; H0WNK8; -.
DR STRING; 30611.ENSOGAP00000003416; -.
DR Ensembl; ENSOGAT00000003842.2; ENSOGAP00000003416.2; ENSOGAG00000003839.2.
DR GeneID; 100960579; -.
DR KEGG; oga:100960579; -.
DR CTD; 3696; -.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT01090000259987; -.
DR HOGENOM; CLU_011772_3_1_1; -.
DR InParanoid; H0WNK8; -.
DR OMA; SKIDNPC; -.
DR OrthoDB; 5475862at2759; -.
DR TreeFam; TF105392; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0034686; C:integrin alphav-beta8 complex; IEA:Ensembl.
DR GO; GO:1990430; F:extracellular matrix protein binding; IEA:Ensembl.
DR GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0001573; P:ganglioside metabolic process; IEA:Ensembl.
DR GO; GO:0060022; P:hard palate development; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0061520; P:Langerhans cell differentiation; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:1901388; P:regulation of transforming growth factor beta activation; IEA:Ensembl.
DR GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1.
DR Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR PANTHER; PTHR10082:SF9; INTEGRIN BETA-8; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR Pfam; PF17205; PSI_integrin; 1.
DR PIRSF; PIRSF002512; Integrin_B; 2.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00187; INB; 1.
DR SMART; SM00423; PSI; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF69179; Integrin domains; 1.
DR SUPFAM; SSF103575; Plexin repeat; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS00243; INTEGRIN_BETA; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell adhesion {ECO:0000256|RuleBase:RU000633};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR002512-1};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU000633};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005225};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000633};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..42
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 43..768
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003544763"
FT TRANSMEM 681..702
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 572..583
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS00022"
FT DISULFID 47..469
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 55..65
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 58..94
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 68..83
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 211..218
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 266..307
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 407..419
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 467..471
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 491..520
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 526..531
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 528..561
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 533..546
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 567..572
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 574..583
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 607..612
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 609..657
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 614..624
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 627..630
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 634..643
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 768 AA; 85386 MW; E34608682134C905 CRC64;
MCGSALAFFT SALVCLQNCW RGSASLLRAA WVFSLVLGLG QGEDNRCTSS NAASCTKCLA
LGPECGWCVQ EDFISGGSRS ERCDTVSNLI SKGCSVDSIE YPSVHVIIPT ENEINTQVTP
GEVSIQLRPG AEANFMLKIH PLKKYPVDLY YLVDVSASMH NNIEKLNSVG NDLSRKMAFF
SRDFRLGFGS YVDKTVSPYI SIHPERIHNQ CSDYNLDCMP PHGYIHVLSL TENITEFEKA
VHRQKISGNI DTPEGGFDAM LQAAVCESHI GWRKEAKRLL LVMTDQTSHL ALDSKLAGIV
VPNDGNCHLK NNVYVKSTTM EHPSLGQLSE KLIDNNINVI FAVQGKQFHW YKDLLPLLPG
TIAREIESKA ANLNNLVVEA YQKLLSEVKV QVENQVPGVY FNITTICPDG TRKPGTEGCG
NVTSDDEVLF NVTVTMKTCD VTGGKNYAII KPIGFNETTK IHIHRNCSCQ CEDNSRPTGK
YVDETSLDSK CFQCDENKCH FEEDQLSSES CKSHRDQPVC SGRGVCVCGQ CVCQQMKFGK
VYGKYCEKDD FSCPYYHGNL CAGHGECEAG RCQCFSGWEG DRCQCPSASV QQCVNSKGQV
CSGRGTCVCG RCECTDPRSI GRFCEHCPTC HTACKENWNC VQCLHPHNLS QAILDQCKSS
CALMEQQYVD QTSECFSSLS YLRIFFIIFI VTFLIGLLKV LIIRQVILQW TSNKIKSSSD
YRVSASKKDK LILQSVCTRA VTYRREKPEE IKMDISKLNA HETFGCNF
//
