ITB8_MOUSE
ID ITB8_MOUSE Reviewed; 767 AA.
AC Q0VBD0;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Integrin beta-8 {ECO:0000305};
DE Flags: Precursor;
GN Name=Itgb8 {ECO:0000312|MGI:MGI:1338035};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=12050137; DOI=10.1242/dev.129.12.2891;
RA Zhu J., Motejlek K., Wang D., Zang K., Schmidt A., Reichardt L.F.;
RT "beta8 integrins are required for vascular morphogenesis in mouse
RT embryos.";
RL Development 129:2891-2903(2002).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16251442; DOI=10.1523/jneurosci.3467-05.2005;
RA Proctor J.M., Zang K., Wang D., Wang R., Reichardt L.F.;
RT "Vascular development of the brain requires beta8 integrin expression in
RT the neuroepithelium.";
RL J. Neurosci. 25:9940-9948(2005).
RN [5]
RP FUNCTION, AND INTERACTION WITH ITGAV.
RX PubMed=25127859; DOI=10.4049/jimmunol.1401102;
RA Edwards J.P., Thornton A.M., Shevach E.M.;
RT "Release of active TGF-beta1 from the latent TGF-beta1/GARP complex on T
RT regulatory cells is mediated by integrin beta8.";
RL J. Immunol. 193:2843-2849(2014).
CC -!- FUNCTION: Integrin alpha-V:beta-8 (ITGAV:ITGB8) is a receptor for
CC fibronectin (By similarity). It recognizes the sequence R-G-D in its
CC ligands (By similarity). Integrin alpha-V:beta-6 (ITGAV:ITGB6) mediates
CC R-G-D-dependent release of transforming growth factor beta-1 (TGF-beta-
CC 1) from regulatory Latency-associated peptide (LAP), thereby playing a
CC key role in TGF-beta-1 activation on the surface of activated
CC regulatory T-cells (Tregs) (PubMed:25127859). Required during
CC vasculogenesis (PubMed:12050137, PubMed:16251442).
CC {ECO:0000250|UniProtKB:P26012, ECO:0000269|PubMed:12050137,
CC ECO:0000269|PubMed:16251442, ECO:0000269|PubMed:25127859}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (PubMed:25127859).
CC Beta-8 (ITGB8) associates with alpha-V (ITGAV) to form ITGAV:ITGB8
CC (PubMed:25127859). ITGAV:ITGB8 interacts with TGFB1 (PubMed:25127859).
CC {ECO:0000269|PubMed:25127859}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P26012};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Expressed in endodermal cells surrounding
CC endothelium in the yolk sac and in periventricular cells of the
CC neuroepithelium in the brain. {ECO:0000269|PubMed:12050137}.
CC -!- DISRUPTION PHENOTYPE: Embryonic or perinatal lethality caused profound
CC defects in vascular development (PubMed:12050137). More than half
CC embryos die at midgestation, with evidence of insufficient
CC vascularization of the placenta and yolk sac (PubMed:12050137).
CC Surviving embryos die shortly after birth with extensive intracerebral
CC hemorrhage (PubMed:12050137). Conditional deletion in the
CC neuroepithelium results in bilateral hemorrhage at in neonates caused
CC by endothelial cell abnormalities in the developing cortex
CC (PubMed:16251442). {ECO:0000269|PubMed:12050137,
CC ECO:0000269|PubMed:16251442}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
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DR EMBL; AC140349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC142263; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC120691; AAI20692.1; -; mRNA.
DR EMBL; BC125343; AAI25344.1; -; mRNA.
DR CCDS; CCDS36580.1; -.
DR RefSeq; NP_796264.2; NM_177290.3.
DR AlphaFoldDB; Q0VBD0; -.
DR SMR; Q0VBD0; -.
DR ComplexPortal; CPX-3133; Integrin alphav-beta8 complex.
DR STRING; 10090.ENSMUSP00000026360; -.
DR GlyConnect; 2407; 4 N-Linked glycans (2 sites).
DR GlyGen; Q0VBD0; 6 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; Q0VBD0; -.
DR PhosphoSitePlus; Q0VBD0; -.
DR SwissPalm; Q0VBD0; -.
DR MaxQB; Q0VBD0; -.
DR PaxDb; Q0VBD0; -.
DR PeptideAtlas; Q0VBD0; -.
DR PRIDE; Q0VBD0; -.
DR ProteomicsDB; 343273; -.
DR ABCD; Q0VBD0; 1 sequenced antibody.
DR Antibodypedia; 25377; 183 antibodies from 29 providers.
DR DNASU; 320910; -.
DR Ensembl; ENSMUST00000026360; ENSMUSP00000026360; ENSMUSG00000025321.
DR GeneID; 320910; -.
DR KEGG; mmu:320910; -.
DR UCSC; uc007pik.1; mouse.
DR CTD; 3696; -.
DR MGI; MGI:1338035; Itgb8.
DR VEuPathDB; HostDB:ENSMUSG00000025321; -.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT00980000198528; -.
DR HOGENOM; CLU_011772_3_1_1; -.
DR InParanoid; Q0VBD0; -.
DR OMA; DFSCPYY; -.
DR OrthoDB; 473040at2759; -.
DR PhylomeDB; Q0VBD0; -.
DR TreeFam; TF105392; -.
DR Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-2173789; TGF-beta receptor signaling activates SMADs.
DR BioGRID-ORCS; 320910; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q0VBD0; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q0VBD0; protein.
DR Bgee; ENSMUSG00000025321; Expressed in pigmented layer of retina and 206 other tissues.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0034686; C:integrin alphav-beta8 complex; IDA:UniProtKB.
DR GO; GO:1990430; F:extracellular matrix protein binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0051216; P:cartilage development; ISO:MGI.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IC:ComplexPortal.
DR GO; GO:0001573; P:ganglioside metabolic process; IMP:MGI.
DR GO; GO:0060022; P:hard palate development; IGI:MGI.
DR GO; GO:0006955; P:immune response; IGI:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
DR GO; GO:0061520; P:Langerhans cell differentiation; IGI:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:1901388; P:regulation of transforming growth factor beta activation; IDA:UniProtKB.
DR GO; GO:0009615; P:response to virus; IGI:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IGI:MGI.
DR GO; GO:0001570; P:vasculogenesis; ISS:UniProtKB.
DR Gene3D; 3.40.50.410; -; 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; IPR015442; Integrin_bsu-8.
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; PTHR10082; 1.
DR PANTHER; PTHR10082:SF9; PTHR10082:SF9; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR Pfam; PF17205; PSI_integrin; 1.
DR PIRSF; PIRSF002512; Integrin_B; 1.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00187; INB; 1.
DR SMART; SM00423; PSI; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS00243; INTEGRIN_BETA; 2.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein; Integrin;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..767
FT /note="Integrin beta-8"
FT /evidence="ECO:0000255"
FT /id="PRO_5015296953"
FT TOPO_DOM 22..681
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 682..702
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 703..767
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 46..95
FT /note="PSI"
FT /evidence="ECO:0000255"
FT DOMAIN 146..384
FT /note="VWFA"
FT /evidence="ECO:0000250|UniProtKB:P26012"
FT REPEAT 471..509
FT /note="I"
FT /evidence="ECO:0000250|UniProtKB:P26012"
FT REPEAT 510..551
FT /note="II"
FT /evidence="ECO:0000250|UniProtKB:P26012"
FT REPEAT 552..591
FT /note="III"
FT /evidence="ECO:0000250|UniProtKB:P26012"
FT REPEAT 592..628
FT /note="IV"
FT /evidence="ECO:0000250|UniProtKB:P26012"
FT REGION 471..628
FT /note="Cysteine-rich tandem repeats"
FT /evidence="ECO:0000250|UniProtKB:P26012"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 647
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..469
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 55..65
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 58..94
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 68..83
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 211..218
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 266..307
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 407..419
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 467..471
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 481..493
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 490..519
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 525..530
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 527..560
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 532..545
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 566..571
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 573..582
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 606..611
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 608..656
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 613..623
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 626..629
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 633..642
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
SQ SEQUENCE 767 AA; 84519 MW; 792F58A21EDB448C CRC64;
MCGSALAFLT AALLSLHNCQ RGPALVLGAA WVFSLVLGLG QSEHNRCGSA NVVSCARCLQ
LGPECGWCVQ EDFVSGGSGS ERCDTVSSLI SKGCPVDSIE YLSVHVVTSS ENEINTQVTP
GEVSVQLHPG AEANFMLKVR PLKKYPVDLY YLVDVSASMH NNIEKLNSVG NDLSKKMALY
SRDFRLGFGS YVDKTVSPYI SIHPERIHNQ CSDYNLDCMP PHGYIHVLSL TENITEFEKA
VHRQKISGNI DTPEGGFDAM LQAAVCESHI GWRKEAKRLL LVMTDQTSHL ALDSKLAGIV
VPNDGNCHLK NNVYVKSTTM EHPSLGQLSE KLIDNNINVI FAVQGKQFHW YKDLLPLLPG
AIAGEIESKA ANLNNLVVEA YKKIISEVKV QLENQVHGVH FNITAICPDG ARKPGISGCG
NVTSNDEVLF NVTVVMKTCD IMGGKNYAII KPIGFNETTK VHIHRSCSCQ CENHRGLKGQ
CAEAAPDPKC PQCDDSRCHF DEDQFPSETC KPQEDQPVCS GRGVCICGKC LCHKTKLGRV
YGQYCEKDDF SCPYLHGDVC AGHGECEGGR CQCFSGWEGD RCQCPSASAQ HCVNSKGQVC
SGRGTCVCGR CECTDPRSIG RLCEHCPTCH LSCSENWNCL QCLHPHNLSQ AALDQCKSSC
AVMEQHRMDQ TSECLSGPSY LRIFFIIFIV TFLIGLLKVL IIRQVILQWN NNKIKSSSDY
RMSASKKDKL ILQSVCTRAV TYRREKPEEI KMDISKLNAQ EAFRCNF
