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Database: UniProt
Entry: Q0VBD0
LinkDB: Q0VBD0
Original site: Q0VBD0 
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   10-APR-2019, entry version 128.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=12050137;
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
RT   in 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
RT   T 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
CC       its ligands (By similarity). Integrin alpha-V:beta-6 (ITGAV:ITGB6)
CC       mediates R-G-D-dependent release of transforming growth factor
CC       beta-1 (TGF-beta-1) from regulatory Latency-associated peptide
CC       (LAP), thereby playing a key role in TGF-beta-1 activation on the
CC       surface of activated regulatory T-cells (Tregs) (PubMed:25127859).
CC       Required during 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
CC       (PubMed:25127859). Beta-8 (ITGB8) associates with alpha-V (ITGAV)
CC       to form ITGAV:ITGB8 (PubMed:25127859). ITGAV:ITGB8 interacts with
CC       TGFB1 (PubMed:25127859). {ECO:0000269|PubMed:25127859}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:P26012}; Single-pass type I membrane
CC       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
CC       profound defects in vascular development (PubMed:12050137). More
CC       than half embryos die at midgestation, with evidence of
CC       insufficient vascularization of the placenta and yolk sac
CC       (PubMed:12050137). Surviving embryos die shortly after birth with
CC       extensive intracerebral hemorrhage (PubMed:12050137). Conditional
CC       deletion in the neuroepithelium results in bilateral hemorrhage at
CC       postnatal day 0 caused by endothelial cell abnormalities in the
CC       developing cortex (PubMed:16251442). {ECO:0000269|PubMed:12050137,
CC       ECO:0000269|PubMed:16251442}.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000305}.
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   UniGene; Mm.217000; -.
DR   ProteinModelPortal; Q0VBD0; -.
DR   SMR; Q0VBD0; -.
DR   ComplexPortal; CPX-3133; Integrin alphav-beta8 complex.
DR   STRING; 10090.ENSMUSP00000026360; -.
DR   iPTMnet; Q0VBD0; -.
DR   PhosphoSitePlus; Q0VBD0; -.
DR   SwissPalm; Q0VBD0; -.
DR   MaxQB; Q0VBD0; -.
DR   PaxDb; Q0VBD0; -.
DR   PeptideAtlas; Q0VBD0; -.
DR   PRIDE; Q0VBD0; -.
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   eggNOG; KOG1226; Eukaryota.
DR   eggNOG; ENOG410XP60; LUCA.
DR   GeneTree; ENSGT00950000182617; -.
DR   HOGENOM; HOG000252936; -.
DR   HOVERGEN; HBG006190; -.
DR   InParanoid; Q0VBD0; -.
DR   KO; K06591; -.
DR   OMA; SASAQHC; -.
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   Proteomes; UP000000589; Chromosome 12.
DR   Bgee; ENSMUSG00000025321; Expressed in 220 organ(s), highest expression level in camera-type eye.
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:0008305; C:integrin complex; IBA:GO_Central.
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; IEA:InterPro.
DR   GO; GO:0001573; P:ganglioside metabolic process; IMP:MGI.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
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:0001570; P:vasculogenesis; ISS:UniProtKB.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR013032; EGF-like_CS.
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; Complete proteome; Disulfide bond;
KW   Glycoprotein; Integrin; Membrane; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   CHAIN        22    767       Integrin beta-8. {ECO:0000255}.
FT                                /FTId=PRO_5015296953.
FT   TOPO_DOM     22    681       Extracellular. {ECO:0000305}.
FT   TRANSMEM    682    702       Helical. {ECO:0000255}.
FT   TOPO_DOM    703    767       Cytoplasmic. {ECO:0000305}.
FT   DOMAIN       46     95       PSI. {ECO:0000255}.
FT   DOMAIN      146    384       VWFA. {ECO:0000250|UniProtKB:P26012}.
FT   REPEAT      471    509       I. {ECO:0000250|UniProtKB:P26012}.
FT   REPEAT      510    551       II. {ECO:0000250|UniProtKB:P26012}.
FT   REPEAT      552    591       III. {ECO:0000250|UniProtKB:P26012}.
FT   REPEAT      592    628       IV. {ECO:0000250|UniProtKB:P26012}.
FT   REGION      471    628       Cysteine-rich tandem repeats.
FT                                {ECO:0000250|UniProtKB:P26012}.
FT   CARBOHYD    233    233       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    402    402       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    421    421       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    431    431       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    456    456       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    647    647       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     47    469       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID     55     65       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID     58     94       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID     68     83       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    211    218       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    266    307       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    407    419       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    467    471       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    481    493       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    490    519       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    525    530       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    527    560       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    532    545       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    566    571       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    573    582       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    606    611       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    608    656       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    613    623       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    626    629       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    633    642       {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
//
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