Adhesion G protein-coupled receptor B1 (ADGRB1)
The protein contains 1584 amino acids for an estimated molecular weight of 173501 Da.
Phosphatidylserine receptor which enhances the engulfment of apoptotic cells (PubMed:24509909). Also mediates the binding and engulfment of Gram-negative bacteria (PubMed:26838550). Stimulates production of reactive oxygen species by macrophages in response to Gram-negative bacteria, resulting in enhanced microbicidal macrophage activity (PubMed:26838550). In the gastric mucosa, required for recognition and engulfment of apoptotic gastric epithelial cells (PubMed:24509909). Promotes myoblast fusion (By similarity). Activates the Rho pathway in a G-protein-dependent manner (PubMed:23782696). Inhibits MDM2-mediated ubiquitination and degradation of DLG4/PSD95, promoting DLG4 stability and regulating synaptic plasticity (By similarity). Required for the formation of dendritic spines by ensuring the correct localization of PARD3 and TIAM1 (By similarity). Potent inhibitor of angiogenesis in brain and may play a significant role as a mediator of the p53/TP53 signal in suppression of glioblastoma (PubMed:11875720).', 'Inhibits angiogenesis in a CD36-dependent manner.', 'Inhibits angiogenesis. (updated: Dec. 11, 2019)
Protein identification was indicated in the following studies:
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt, is predicted to be membranous by TOPCONS.
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No binding partner found
Biological Process
Adenylate cyclase-activating G protein-coupled receptor signaling pathway
Apoptotic cell clearance
Axonogenesis
Cell adhesion
Cell surface receptor signaling pathway
Defense response to Gram-negative bacterium
Engulfment of apoptotic cell
G protein-coupled receptor signaling pathway
Innate immune response
Muscle organ development
Negative regulation of angiogenesis
Negative regulation of cell population proliferation
Negative regulation of endothelial cell migration
Negative regulation of protein catabolic process
Negative regulation of protein ubiquitination
Peripheral nervous system development
Phagocytosis, recognition
Positive regulation of myoblast fusion
Positive regulation of reactive oxygen species biosynthetic process
Positive regulation of synapse assembly
Regulation of synaptic plasticity
Signal transduction
The reference OMIM entry for this protein is 602682
Brain-specific angiogenesis inhibitor 1; bai1
Angiogenesis inhibitory factor, glioma-derived; gdaif
CLONING
Angiogenesis is controlled by a local balance between stimulators and inhibitors of growth of new vessels and is suppressed under normal physiologic conditions. Studies by Folkman (1989, 1995) and others indicated that angiogenesis is essential for growth and metastasis of solid tumors. In order to obtain blood supply for their growth, tumor cells are potently angiogenic and attract new vessels as results of increased secretion of inducers and decreased production of endogenous negative regulators. Progression of a glioma to its more malignant form, glioblastoma, is associated with dramatic neovascularization. The most frequently altered gene in human glioblastomas is p53 (191170), and alteration of p53 appears to play a significant role in progression. Neovascularization might be a direct consequence of inactivation of p53, possibly due to loss of transactivation of 1 or more target genes regulated by p53. Van Meir et al. (1994) found that a glioblastoma cell line, upon introduction of wildtype, but not mutant, p53, produced a secretory inhibitor of capillary endothelial cell migration designated GDAIF. Nishimori et al. (1997) isolated a brain-specific gene, BAI1. The predicted 1,584-amino acid BAI1 protein includes a 7-span transmembrane region similar to that of the secretin receptor (182098), as well as extended extracellular and cytoplasmic domains. The extracellular region of BAI1 possesses a single arg-gly-asp (RGD) motif recognized by integrins, and 5 sequences corresponding to the thrombospondin type I (188060) repeats that can inhibit experimental angiogenesis induced by basic fibroblast growth factor (FGFB; 134920).GENE FUNCTION
Nishimori et al. (1997) found that BAI1 contains at least 1 'functional' p53-binding site within an intron, and that its expression was induced by wildtype p53. Shiratsuchi et al. (1997) found that, in spite of similar tissue specificity among BAI1, BAI2 (602683), and BAI3 (602684), only BAI1 was transcriptionally regulated by p53. BAI3 expression was absent in 2 of 9 glioblastoma cell lines examined and was significantly reduced in 3 of the remaining 7. These data suggested that members of this novel gene family may play important roles in suppression of glioblastoma. Using yeast 2-hybrid and protein interaction assays, Shiratsuchi et al. (1998) found that human BAI1 and BAP1 (MAGI1; 602625) interacted. Mutation analysis showed that a QTEV motif in the C-terminal region of BAI1 and the PDZ domains of BAP1 were required for the interaction. Park et al. (2007) identified BAI1 as a receptor upstream of ELMO (606420) and as a receptor that can bind phosphatidylserine on apoptotic cells. BAI1 is a 7-transmembrane protein belonging to the adhesion-type G protein-coupled receptor family with an extended extracellular region. Park et al. (2007) showed that BAI1 functions as an engulfment receptor in both the recognition and subsequent internalization of apoptotic cells. Through multiple lines of investigation, Park et al. (2007) identified phosphatidylserine, a key 'eat-me' signal exposed on apoptotic cells, as a ligand for BAI1. The thrombospondin type 1 repeats within the extracellular region of BAI1 mediate direct binding to phosphatidylserine. As with intracellular signaling, BAI1 forms a trimeric complex with ELMO and Dock180 (601403), and functional studies suggested that BAI1 cooperates with ELMO/Dock180/Rac (602048) to promote maximal engulfment of apoptotic cells. Last ... More on the omim web site
June 29, 2020: Protein entry updated
Automatic update: OMIM entry 602682 was added.
Jan. 22, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).