Q0VBD0 · ITB8_MOUSE
- ProteinIntegrin beta-8
- GeneItgb8
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids767 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Integrin alpha-V:beta-8 (ITGAV:ITGB8) is a receptor for fibronectin (By similarity).
It recognizes the sequence R-G-D in its ligands (By similarity).
Integrin alpha-V:beta-6 (ITGAV:ITGB6) mediates R-G-D-dependent release of transforming growth factor beta-1 (TGF-beta-1) from regulatory Latency-associated peptide (LAP), thereby playing a key role in TGF-beta-1 activation on the surface of activated regulatory T-cells (Tregs) (PubMed:25127859).
Required during vasculogenesis (PubMed:12050137, PubMed:16251442).
It recognizes the sequence R-G-D in its ligands (By similarity).
Integrin alpha-V:beta-6 (ITGAV:ITGB6) mediates R-G-D-dependent release of transforming growth factor beta-1 (TGF-beta-1) from regulatory Latency-associated peptide (LAP), thereby playing a key role in TGF-beta-1 activation on the surface of activated regulatory T-cells (Tregs) (PubMed:25127859).
Required during vasculogenesis (PubMed:12050137, PubMed:16251442).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 154 | Mg2+ (UniProtKB | ChEBI); in MIDAS binding site | ||||
Sequence: D | ||||||
Binding site | 156 | Mg2+ (UniProtKB | ChEBI); in MIDAS binding site | ||||
Sequence: S | ||||||
Binding site | 193 | Ca2+ (UniProtKB | ChEBI); in LIMBS binding site | ||||
Sequence: D | ||||||
Binding site | 249 | Ca2+ (UniProtKB | ChEBI); in LIMBS binding site | ||||
Sequence: N | ||||||
Binding site | 251 | Ca2+ (UniProtKB | ChEBI); in LIMBS binding site | ||||
Sequence: D | ||||||
Binding site | 253 | Ca2+ (UniProtKB | ChEBI); in LIMBS binding site | ||||
Sequence: P | ||||||
Binding site | 254 | Ca2+ (UniProtKB | ChEBI); in LIMBS binding site | ||||
Sequence: E | ||||||
Binding site | 254 | Mg2+ (UniProtKB | ChEBI); in MIDAS binding site | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell surface | |
Cellular Component | focal adhesion | |
Cellular Component | integrin alphav-beta8 complex | |
Cellular Component | integrin complex | |
Molecular Function | extracellular matrix protein binding | |
Molecular Function | integrin binding | |
Molecular Function | metal ion binding | |
Molecular Function | signaling receptor binding | |
Biological Process | cartilage development | |
Biological Process | cell-cell adhesion | |
Biological Process | cell-matrix adhesion | |
Biological Process | ganglioside metabolic process | |
Biological Process | hard palate development | |
Biological Process | immune response | |
Biological Process | integrin-mediated signaling pathway | |
Biological Process | Langerhans cell differentiation | |
Biological Process | negative regulation of gene expression | |
Biological Process | positive regulation of angiogenesis | |
Biological Process | positive regulation of gene expression | |
Biological Process | response to virus | |
Biological Process | transforming growth factor beta receptor signaling pathway | |
Biological Process | vasculogenesis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameIntegrin beta-8
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ0VBD0
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 22-681 | Extracellular | ||||
Sequence: GPALVLGAAWVFSLVLGLGQSEHNRCGSANVVSCARCLQLGPECGWCVQEDFVSGGSGSERCDTVSSLISKGCPVDSIEYLSVHVVTSSENEINTQVTPGEVSVQLHPGAEANFMLKVRPLKKYPVDLYYLVDVSASMHNNIEKLNSVGNDLSKKMALYSRDFRLGFGSYVDKTVSPYISIHPERIHNQCSDYNLDCMPPHGYIHVLSLTENITEFEKAVHRQKISGNIDTPEGGFDAMLQAAVCESHIGWRKEAKRLLLVMTDQTSHLALDSKLAGIVVPNDGNCHLKNNVYVKSTTMEHPSLGQLSEKLIDNNINVIFAVQGKQFHWYKDLLPLLPGAIAGEIESKAANLNNLVVEAYKKIISEVKVQLENQVHGVHFNITAICPDGARKPGISGCGNVTSNDEVLFNVTVVMKTCDIMGGKNYAIIKPIGFNETTKVHIHRSCSCQCENHRGLKGQCAEAAPDPKCPQCDDSRCHFDEDQFPSETCKPQEDQPVCSGRGVCICGKCLCHKTKLGRVYGQYCEKDDFSCPYLHGDVCAGHGECEGGRCQCFSGWEGDRCQCPSASAQHCVNSKGQVCSGRGTCVCGRCECTDPRSIGRLCEHCPTCHLSCSENWNCLQCLHPHNLSQAALDQCKSSCAVMEQHRMDQTSECLSGPSYL | ||||||
Transmembrane | 682-702 | Helical | ||||
Sequence: RIFFIIFIVTFLIGLLKVLII | ||||||
Topological domain | 703-767 | Cytoplasmic | ||||
Sequence: RQVILQWNNNKIKSSSDYRMSASKKDKLILQSVCTRAVTYRREKPEEIKMDISKLNAQEAFRCNF |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Embryonic or perinatal lethality caused profound defects in vascular development (PubMed:12050137).
More than half embryos die at midgestation, with evidence of insufficient vascularization of the placenta and yolk sac (PubMed:12050137).
Surviving embryos die shortly after birth with extensive intracerebral hemorrhage (PubMed:12050137).
Conditional deletion in the neuroepithelium results in bilateral hemorrhage at in neonates caused by endothelial cell abnormalities in the developing cortex (PubMed:16251442).
More than half embryos die at midgestation, with evidence of insufficient vascularization of the placenta and yolk sac (PubMed:12050137).
Surviving embryos die shortly after birth with extensive intracerebral hemorrhage (PubMed:12050137).
Conditional deletion in the neuroepithelium results in bilateral hemorrhage at in neonates caused by endothelial cell abnormalities in the developing cortex (PubMed:16251442).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 31 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MCGSALAFLTAALLSLHNCQR | ||||||
Chain | PRO_5015296953 | 22-767 | Integrin beta-8 | |||
Sequence: GPALVLGAAWVFSLVLGLGQSEHNRCGSANVVSCARCLQLGPECGWCVQEDFVSGGSGSERCDTVSSLISKGCPVDSIEYLSVHVVTSSENEINTQVTPGEVSVQLHPGAEANFMLKVRPLKKYPVDLYYLVDVSASMHNNIEKLNSVGNDLSKKMALYSRDFRLGFGSYVDKTVSPYISIHPERIHNQCSDYNLDCMPPHGYIHVLSLTENITEFEKAVHRQKISGNIDTPEGGFDAMLQAAVCESHIGWRKEAKRLLLVMTDQTSHLALDSKLAGIVVPNDGNCHLKNNVYVKSTTMEHPSLGQLSEKLIDNNINVIFAVQGKQFHWYKDLLPLLPGAIAGEIESKAANLNNLVVEAYKKIISEVKVQLENQVHGVHFNITAICPDGARKPGISGCGNVTSNDEVLFNVTVVMKTCDIMGGKNYAIIKPIGFNETTKVHIHRSCSCQCENHRGLKGQCAEAAPDPKCPQCDDSRCHFDEDQFPSETCKPQEDQPVCSGRGVCICGKCLCHKTKLGRVYGQYCEKDDFSCPYLHGDVCAGHGECEGGRCQCFSGWEGDRCQCPSASAQHCVNSKGQVCSGRGTCVCGRCECTDPRSIGRLCEHCPTCHLSCSENWNCLQCLHPHNLSQAALDQCKSSCAVMEQHRMDQTSECLSGPSYLRIFFIIFIVTFLIGLLKVLIIRQVILQWNNNKIKSSSDYRMSASKKDKLILQSVCTRAVTYRREKPEEIKMDISKLNAQEAFRCNF | ||||||
Disulfide bond | 47↔65 | |||||
Sequence: CGSANVVSCARCLQLGPEC | ||||||
Disulfide bond | 55↔469 | |||||
Sequence: CARCLQLGPECGWCVQEDFVSGGSGSERCDTVSSLISKGCPVDSIEYLSVHVVTSSENEINTQVTPGEVSVQLHPGAEANFMLKVRPLKKYPVDLYYLVDVSASMHNNIEKLNSVGNDLSKKMALYSRDFRLGFGSYVDKTVSPYISIHPERIHNQCSDYNLDCMPPHGYIHVLSLTENITEFEKAVHRQKISGNIDTPEGGFDAMLQAAVCESHIGWRKEAKRLLLVMTDQTSHLALDSKLAGIVVPNDGNCHLKNNVYVKSTTMEHPSLGQLSEKLIDNNINVIFAVQGKQFHWYKDLLPLLPGAIAGEIESKAANLNNLVVEAYKKIISEVKVQLENQVHGVHFNITAICPDGARKPGISGCGNVTSNDEVLFNVTVVMKTCDIMGGKNYAIIKPIGFNETTKVHIHRSCSC | ||||||
Disulfide bond | 58↔83 | |||||
Sequence: CLQLGPECGWCVQEDFVSGGSGSERC | ||||||
Disulfide bond | 68↔94 | |||||
Sequence: CVQEDFVSGGSGSERCDTVSSLISKGC | ||||||
Disulfide bond | 211↔218 | |||||
Sequence: CSDYNLDC | ||||||
Glycosylation | 233 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 266↔307 | |||||
Sequence: CESHIGWRKEAKRLLLVMTDQTSHLALDSKLAGIVVPNDGNC | ||||||
Glycosylation | 402 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 407↔419 | |||||
Sequence: CPDGARKPGISGC | ||||||
Glycosylation | 421 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 431 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 439↔467 | |||||
Sequence: CDIMGGKNYAIIKPIGFNETTKVHIHRSC | ||||||
Glycosylation | 456 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 471↔493 | |||||
Sequence: CENHRGLKGQCAEAAPDPKCPQC | ||||||
Disulfide bond | 510↔525 | |||||
Sequence: CKPQEDQPVCSGRGVC | ||||||
Disulfide bond | 519↔530 | |||||
Sequence: CSGRGVCICGKC | ||||||
Disulfide bond | 532↔545 | |||||
Sequence: CHKTKLGRVYGQYC | ||||||
Disulfide bond | 552↔566 | |||||
Sequence: CPYLHGDVCAGHGEC | ||||||
Disulfide bond | 560↔571 | |||||
Sequence: CAGHGECEGGRC | ||||||
Disulfide bond | 573↔582 | |||||
Sequence: CFSGWEGDRC | ||||||
Disulfide bond | 584↔608 | |||||
Sequence: CPSASAQHCVNSKGQVCSGRGTCVC | ||||||
Disulfide bond | 592↔606 | |||||
Sequence: CVNSKGQVCSGRGTC | ||||||
Disulfide bond | 600↔611 | |||||
Sequence: CSGRGTCVCGRC | ||||||
Disulfide bond | 613↔623 | |||||
Sequence: CTDPRSIGRLC | ||||||
Disulfide bond | 626↔629 | |||||
Sequence: CPTC | ||||||
Disulfide bond | 633↔660 | |||||
Sequence: CSENWNCLQCLHPHNLSQAALDQCKSSC | ||||||
Disulfide bond | 639↔656 | |||||
Sequence: CLQCLHPHNLSQAALDQC | ||||||
Glycosylation | 647 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Developmental stage
Expressed in endodermal cells surrounding endothelium in the yolk sac and in periventricular cells of the neuroepithelium in the brain.
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 46-95 | PSI | ||||
Sequence: RCGSANVVSCARCLQLGPECGWCVQEDFVSGGSGSERCDTVSSLISKGCP | ||||||
Domain | 146-384 | VWFA | ||||
Sequence: PVDLYYLVDVSASMHNNIEKLNSVGNDLSKKMALYSRDFRLGFGSYVDKTVSPYISIHPERIHNQCSDYNLDCMPPHGYIHVLSLTENITEFEKAVHRQKISGNIDTPEGGFDAMLQAAVCESHIGWRKEAKRLLLVMTDQTSHLALDSKLAGIVVPNDGNCHLKNNVYVKSTTMEHPSLGQLSEKLIDNNINVIFAVQGKQFHWYKDLLPLLPGAIAGEIESKAANLNNLVVEAYKKI | ||||||
Domain | 471-509 | EGF-like 1 | ||||
Sequence: CENHRGLKGQCAEAAPDPKCPQCDDSRCHFDEDQFPSET | ||||||
Domain | 510-551 | EGF-like 2 | ||||
Sequence: CKPQEDQPVCSGRGVCICGKCLCHKTKLGRVYGQYCEKDDFS | ||||||
Domain | 552-591 | EGF-like 3 | ||||
Sequence: CPYLHGDVCAGHGECEGGRCQCFSGWEGDRCQCPSASAQH | ||||||
Domain | 592-628 | EGF-like 4 | ||||
Sequence: CVNSKGQVCSGRGTCVCGRCECTDPRSIGRLCEHCPT |
Domain
The VWFA domain (or beta I domain) contains two cation-binding sites: the ligand-associated metal ion-binding site (LIMBS or SyMBS) and the metal ion-dependent adhesion site (MIDAS). Unlike in the other beta integrins, the cation-binding site adjacent MIDAS site (ADMIDAS) in ITGB8 is not functional due to the presence of two Asn residues instead of 2 Asp residues. This domain is also part of the ligand-binding site.
Sequence similarities
Belongs to the integrin beta chain family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length767
- Mass (Da)84,519
- Last updated2006-09-05 v1
- Checksum792F58A21EDB448C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC140349 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC142263 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC120691 EMBL· GenBank· DDBJ | AAI20692.1 EMBL· GenBank· DDBJ | mRNA | ||
BC125343 EMBL· GenBank· DDBJ | AAI25344.1 EMBL· GenBank· DDBJ | mRNA |