AGRB1_MOUSE
ID AGRB1_MOUSE Reviewed; 1582 AA.
AC Q3UHD1; Q3UH36; Q8CGM0;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Adhesion G protein-coupled receptor B1 {ECO:0000312|MGI:MGI:1933736};
DE AltName: Full=Brain-specific angiogenesis inhibitor 1 {ECO:0000303|PubMed:11245925};
DE Contains:
DE RecName: Full=Vasculostatin-120 {ECO:0000250|UniProtKB:O14514};
DE Short=Vstat120 {ECO:0000250|UniProtKB:O14514};
DE Contains:
DE RecName: Full=Vasculostatin-40 {ECO:0000250|UniProtKB:O14514};
DE Short=Vstat-40 {ECO:0000250|UniProtKB:O14514};
DE Flags: Precursor;
GN Name=Adgrb1 {ECO:0000312|MGI:MGI:1933736};
GN Synonyms=Bai1 {ECO:0000303|PubMed:11245925};
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 [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH
RP PHYHIP.
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=11245925; DOI=10.1016/s0169-328x(01)00004-3;
RA Koh J.T., Lee Z.H., Ahn K.Y., Kim J.-K., Bae C.S., Kim H.-H., Kee H.J.,
RA Kim K.K.;
RT "Characterization of mouse brain-specific angiogenesis inhibitor 1 (BAI1)
RT and phytanoyl-CoA alpha-hydroxylase-associated protein 1, a novel BAI1-
RT binding protein.";
RL Brain Res. Mol. Brain Res. 87:223-237(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PROTEIN SEQUENCE OF 1255-1268, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP FUNCTION.
RX PubMed=11875720; DOI=10.1038/sj.bjc.6600067;
RA Duda D.G., Sunamura M., Lozonschi L., Yokoyama T., Yatsuoka T., Motoi F.,
RA Horii A., Tani K., Asano S., Nakamura Y., Matsuno S.;
RT "Overexpression of the p53-inducible brain-specific angiogenesis inhibitor
RT 1 suppresses efficiently tumour angiogenesis.";
RL Br. J. Cancer 86:490-496(2002).
RN [5]
RP FUNCTION, INTERACTION WITH ELMO1 AND DOCK1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DOMAIN, AND MUTAGENESIS OF 1487-ARG--ARG-1489.
RX PubMed=17960134; DOI=10.1038/nature06329;
RA Park D., Tosello-Trampont A.-C., Elliott M.R., Lu M., Haney L.B., Ma Z.,
RA Klibanov A.L., Mandell J.W., Ravichandran K.S.;
RT "BAI1 is an engulfment receptor for apoptotic cells upstream of the
RT ELMO/Dock180/Rac module.";
RL Nature 450:430-434(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1467, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=20888903; DOI=10.1016/j.bbi.2010.09.021;
RA Sokolowski J.D., Nobles S.L., Heffron D.S., Park D., Ravichandran K.S.,
RA Mandell J.W.;
RT "Brain-specific angiogenesis inhibitor-1 expression in astrocytes and
RT neurons: implications for its dual function as an apoptotic engulfment
RT receptor.";
RL Brain Behav. Immun. 25:915-921(2011).
RN [8]
RP FUNCTION, AND DOMAIN.
RX PubMed=21245295; DOI=10.1073/pnas.1014775108;
RA Das S., Owen K.A., Ly K.T., Park D., Black S.G., Wilson J.M., Sifri C.D.,
RA Ravichandran K.S., Ernst P.B., Casanova J.E.;
RT "Brain angiogenesis inhibitor 1 (BAI1) is a pattern recognition receptor
RT that mediates macrophage binding and engulfment of Gram-negative
RT bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2136-2141(2011).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=23782696; DOI=10.1074/jbc.m113.489757;
RA Stephenson J.R., Paavola K.J., Schaefer S.A., Kaur B., Van Meir E.G.,
RA Hall R.A.;
RT "Brain-specific angiogenesis inhibitor-1 signaling, regulation, and
RT enrichment in the postsynaptic density.";
RL J. Biol. Chem. 288:22248-22256(2013).
RN [10]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23595754; DOI=10.1523/jneurosci.3978-12.2013;
RA Duman J.G., Tzeng C.P., Tu Y.K., Munjal T., Schwechter B., Ho T.S.,
RA Tolias K.F.;
RT "The adhesion-GPCR BAI1 regulates synaptogenesis by controlling the
RT recruitment of the Par3/Tiam1 polarity complex to synaptic sites.";
RL J. Neurosci. 33:6964-6978(2013).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23615608; DOI=10.1038/nature12135;
RA Hochreiter-Hufford A.E., Lee C.S., Kinchen J.M., Sokolowski J.D.,
RA Arandjelovic S., Call J.A., Klibanov A.L., Yan Z., Mandell J.W.,
RA Ravichandran K.S.;
RT "Phosphatidylserine receptor BAI1 and apoptotic cells as new promoters of
RT myoblast fusion.";
RL Nature 497:263-267(2013).
RN [12]
RP FUNCTION, INTERACTION WITH MDM2, AND DISRUPTION PHENOTYPE.
RX PubMed=25751059; DOI=10.1172/jci74603;
RA Zhu D., Li C., Swanson A.M., Villalba R.M., Guo J., Zhang Z., Matheny S.,
RA Murakami T., Stephenson J.R., Daniel S., Fukata M., Hall R.A., Olson J.J.,
RA Neigh G.N., Smith Y., Rainnie D.G., Van Meir E.G.;
RT "BAI1 regulates spatial learning and synaptic plasticity in the
RT hippocampus.";
RL J. Clin. Invest. 125:1497-1508(2015).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26838550; DOI=10.1126/scisignal.aac6250;
RA Billings E.A., Lee C.S., Owen K.A., D'Souza R.S., Ravichandran K.S.,
RA Casanova J.E.;
RT "The adhesion GPCR BAI1 mediates macrophage ROS production and microbicidal
RT activity against Gram-negative bacteria.";
RL Sci. Signal. 9:RA14-RA14(2016).
CC -!- FUNCTION: Phosphatidylserine receptor which enhances the engulfment of
CC apoptotic cells (PubMed:17960134). Also mediates the binding and
CC engulfment of Gram-negative bacteria (PubMed:21245295, PubMed:26838550,
CC PubMed:26838550). Stimulates production of reactive oxygen species by
CC macrophages in response to Gram-negative bacteria, resulting in
CC enhanced microbicidal macrophage activity (By similarity). In the
CC gastric mucosa, required for recognition and engulfment of apoptotic
CC gastric epithelial cells (By similarity). Promotes myoblast fusion
CC (PubMed:23615608). Activates the Rho pathway in a G-protein-dependent
CC manner (By similarity). Inhibits MDM2-mediated ubiquitination and
CC degradation of DLG4/PSD95, promoting DLG4 stability and regulating
CC synaptic plasticity (PubMed:25751059). Required for the formation of
CC dendritic spines by ensuring the correct localization of PARD3 and
CC TIAM1 (By similarity). Potent inhibitor of angiogenesis in brain and
CC may play a significant role as a mediator of the p53/TP53 signal in
CC suppression of glioblastoma (By similarity).
CC {ECO:0000250|UniProtKB:C0HL12, ECO:0000250|UniProtKB:O14514,
CC ECO:0000269|PubMed:11875720, ECO:0000269|PubMed:17960134,
CC ECO:0000269|PubMed:21245295, ECO:0000269|PubMed:23615608,
CC ECO:0000269|PubMed:25751059, ECO:0000269|PubMed:26838550}.
CC -!- FUNCTION: [Vasculostatin-120]: Inhibits angiogenesis in a CD36-
CC dependent manner. {ECO:0000250|UniProtKB:O14514}.
CC -!- FUNCTION: [Vasculostatin-40]: Inhibits angiogenesis.
CC {ECO:0000250|UniProtKB:O14514}.
CC -!- SUBUNIT: Interacts with ELMO1 and DOCK1 (PubMed:17960134). When bound
CC to ELMO1 and DOCK1, acts as a module to promote apoptotic cell
CC engulfment (PubMed:17960134). Interacts with MDM2; the interaction
CC results in inhibition of MDM2-mediated ubiquitination and degradation
CC of DLG4/PSD95 (PubMed:25751059). Interacts with PARD3 and TIAM1; the
CC interaction is required for correct dendritic localization of PARD3 and
CC TIAM1 and for dendritic spine formation (By similarity). Interacts with
CC MAGI1, MAGI3 and BAIAP2 (By similarity). Interacts with PHYHIP
CC (PubMed:11245925). Interacts with DLG4 (via PDZ domain) (By
CC similarity). Vasculostatin-120: Interacts with CD36 (By similarity).
CC Vasculostatin-120: Interacts with ARRB2 (By similarity). Interacts with
CC BAIAP3; this interaction is direct (By similarity).
CC {ECO:0000250|UniProtKB:C0HL12, ECO:0000250|UniProtKB:O14514,
CC ECO:0000269|PubMed:11245925, ECO:0000269|PubMed:17960134,
CC ECO:0000269|PubMed:25751059}.
CC -!- INTERACTION:
CC Q3UHD1; Q92556-1: ELMO1; Xeno; NbExp=9; IntAct=EBI-911280, EBI-15668002;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17960134,
CC ECO:0000269|PubMed:20888903}; Multi-pass membrane protein
CC {ECO:0000255}. Cell projection, phagocytic cup
CC {ECO:0000269|PubMed:17960134}. Cell junction, focal adhesion
CC {ECO:0000269|PubMed:20888903}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:C0HL12}. Postsynaptic density
CC {ECO:0000269|PubMed:23595754, ECO:0000269|PubMed:23782696}.
CC -!- SUBCELLULAR LOCATION: [Vasculostatin-120]: Secreted
CC {ECO:0000250|UniProtKB:O14514}.
CC -!- SUBCELLULAR LOCATION: [Vasculostatin-40]: Secreted
CC {ECO:0000250|UniProtKB:O14514}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UHD1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UHD1-2; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: In brain, widespread expression in all neuropil-
CC rich zones including spinal cord gray matter, cerebellar molecular
CC layer, cerebral cortex, thalamic nuclei and basal ganglia with no
CC expression in white matter (at protein level) (PubMed:20888903). In the
CC cerebellar molecular layer, highly expressed in interneuron processes
CC whereas Purkinje cells and their dendrites show weaker expression (at
CC protein level) (PubMed:20888903). In the olfactory bulb, highly
CC expressed in glomeruli (at protein level) (PubMed:20888903). In the
CC retina, highly concentrated in the outer and inner plexiform layers (at
CC protein level) (PubMed:20888903). Expressed in brain (PubMed:11245925).
CC Enriched in hippocampus and cortex (PubMed:23595754). Also detected in
CC other tissues including bone marrow and spleen (PubMed:17960134).
CC {ECO:0000269|PubMed:11245925, ECO:0000269|PubMed:17960134,
CC ECO:0000269|PubMed:20888903, ECO:0000269|PubMed:23595754}.
CC -!- DOMAIN: The TSP type-1 repeats in the extracellular domain mediate
CC binding to phosphatidylserine (PubMed:17960134). They are also required
CC for bacterial recognition and binding to bacterial outer membrane
CC lipopolysaccharide (PubMed:21245295). {ECO:0000269|PubMed:17960134,
CC ECO:0000269|PubMed:21245295}.
CC -!- PTM: Proteolytically cleaved to produce vasculostatin-40 and
CC vasculostatin-120. Vasculostatin-40 is the major form and is produced
CC through proteolytic cleavage by MMP14 between residues 321 and 329 with
CC cleavage likely to be between Ser-326 and Leu-327.
CC {ECO:0000250|UniProtKB:O14514}.
CC -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:O14514}.
CC -!- DISRUPTION PHENOTYPE: Viable and fertile with normal brain anatomy but
CC mutants display severe deficits in hippocampus-dependent spatial
CC learning and memory that are accompanied by enhanced long-term
CC potentiation, impaired long-term depression, a thinning of the
CC postsynaptic density at hippocampal synapses, reduced protein levels of
CC Dlg4 and increased Dlg4 polyubiquitination (PubMed:25751059). Smaller
CC myofibers than wild-type animals and impaired muscle regeneration after
CC injury (PubMed:23615608). Impaired bacterial clearance following E.coli
CC infection (PubMed:26838550). RNAi-mediated knockdown in embryos results
CC in greatly reduced dendritic spine density and small but significant
CC increases in spine length and decreases in spine diameter
CC (PubMed:23595754). {ECO:0000269|PubMed:23595754,
CC ECO:0000269|PubMed:23615608, ECO:0000269|PubMed:25751059,
CC ECO:0000269|PubMed:26838550}.
CC -!- MISCELLANEOUS: [Isoform 2]: Observed very weakly in the kidney,
CC skeletal muscle, skin, stomach, thymus and brain from embryonic day 18.
CC By neonatal day 1, the expression is targeted only to the brain.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC subfamily. {ECO:0000305}.
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DR EMBL; AY168408; AAN86966.1; -; mRNA.
DR EMBL; AK147494; BAE27949.1; -; mRNA.
DR EMBL; AK147456; BAE27923.1; -; mRNA.
DR EMBL; AK147459; BAE27926.1; -; mRNA.
DR EMBL; AK147607; BAE28021.1; -; mRNA.
DR CCDS; CCDS70635.1; -. [Q3UHD1-1]
DR RefSeq; NP_778156.2; NM_174991.3. [Q3UHD1-1]
DR PDB; 6IDX; X-ray; 1.70 A; C=1471-1495.
DR PDB; 7R84; X-ray; 1.34 A; A/B/C/D=409-462.
DR PDB; 7R85; X-ray; 1.45 A; A=409-462.
DR PDB; 7R86; X-ray; 1.65 A; C/D=409-462.
DR PDBsum; 6IDX; -.
DR PDBsum; 7R84; -.
DR PDBsum; 7R85; -.
DR PDBsum; 7R86; -.
DR AlphaFoldDB; Q3UHD1; -.
DR SMR; Q3UHD1; -.
DR BioGRID; 223612; 6.
DR DIP; DIP-37711N; -.
DR IntAct; Q3UHD1; 4.
DR STRING; 10090.ENSMUSP00000046097; -.
DR GlyGen; Q3UHD1; 7 sites.
DR iPTMnet; Q3UHD1; -.
DR PhosphoSitePlus; Q3UHD1; -.
DR MaxQB; Q3UHD1; -.
DR PaxDb; Q3UHD1; -.
DR PeptideAtlas; Q3UHD1; -.
DR PRIDE; Q3UHD1; -.
DR ProteomicsDB; 296086; -. [Q3UHD1-1]
DR Antibodypedia; 7346; 411 antibodies from 32 providers.
DR DNASU; 107831; -.
DR Ensembl; ENSMUST00000042035; ENSMUSP00000046097; ENSMUSG00000034730. [Q3UHD1-1]
DR GeneID; 107831; -.
DR KEGG; mmu:107831; -.
DR UCSC; uc007wco.1; mouse. [Q3UHD1-1]
DR CTD; 575; -.
DR MGI; MGI:1933736; Adgrb1.
DR VEuPathDB; HostDB:ENSMUSG00000034730; -.
DR eggNOG; ENOG502QRTN; Eukaryota.
DR GeneTree; ENSGT00940000157432; -.
DR HOGENOM; CLU_003751_1_0_1; -.
DR InParanoid; Q3UHD1; -.
DR OMA; GVACQGP; -.
DR OrthoDB; 27621at2759; -.
DR PhylomeDB; Q3UHD1; -.
DR TreeFam; TF331634; -.
DR BioGRID-ORCS; 107831; 3 hits in 67 CRISPR screens.
DR PRO; PR:Q3UHD1; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q3UHD1; protein.
DR Bgee; ENSMUSG00000034730; Expressed in superior frontal gyrus and 129 other tissues.
DR ExpressionAtlas; Q3UHD1; baseline and differential.
DR Genevisible; Q3UHD1; MM.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0001891; C:phagocytic cup; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0043277; P:apoptotic cell clearance; ISO:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IMP:UniProtKB.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0006911; P:phagocytosis, engulfment; IMP:UniProtKB.
DR GO; GO:0006910; P:phagocytosis, recognition; IMP:UniProtKB.
DR GO; GO:1901741; P:positive regulation of myoblast fusion; IMP:UniProtKB.
DR GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; ISS:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0051963; P:regulation of synapse assembly; ISO:MGI.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:UniProtKB.
DR Gene3D; 2.20.100.10; -; 5.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR043838; AGRB_N.
DR InterPro; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR008077; GPCR_2_brain_angio_inhib.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF19188; AGRB_N; 1.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF02793; HRM; 1.
DR Pfam; PF00090; TSP_1; 5.
DR PRINTS; PR01694; BAIPRECURSOR.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00209; TSP1; 5.
DR SUPFAM; SSF82895; SSF82895; 5.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50092; TSP1; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW Cell projection; Direct protein sequencing; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Immunity; Innate immunity;
KW Membrane; Myogenesis; Neurogenesis; Phagocytosis; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Secreted; Signal; Synapse; Transducer;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..1582
FT /note="Adhesion G protein-coupled receptor B1"
FT /id="PRO_0000245046"
FT CHAIN 34..926
FT /note="Vasculostatin-120"
FT /evidence="ECO:0000250|UniProtKB:O14514"
FT /id="PRO_0000441807"
FT CHAIN 34..327
FT /note="Vasculostatin-40"
FT /evidence="ECO:0000250|UniProtKB:O14514"
FT /id="PRO_0000441806"
FT TOPO_DOM 34..948
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 949..969
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 970..980
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 981..1001
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1002..1008
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1009..1029
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1030..1052
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1053..1073
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1074..1093
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1094..1114
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1115..1136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1137..1157
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1158..1166
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1167..1187
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1188..1582
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 261..315
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 354..407
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 409..462
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 467..520
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 522..575
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 881..938
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 313..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..943
FT /note="N-terminal stalk following vasculostatin-120
FT cleavage which is not required for signaling activity"
FT /evidence="ECO:0000250|UniProtKB:O14514"
FT REGION 1363..1582
FT /note="Involved in interaction with MAGI1"
FT /evidence="ECO:0000250|UniProtKB:O14514"
FT REGION 1382..1549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1579..1582
FT /note="Indispensable for interaction with MAGI1"
FT /evidence="ECO:0000250|UniProtKB:O14514"
FT COMPBIAS 1389..1434
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1455..1469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1470..1541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 926..927
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:O14514"
FT MOD_RES 609
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O14514"
FT MOD_RES 1467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 692
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 844
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 877
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 881
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 273..309
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 277..314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 288..299
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 366..400
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 370..406
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 381..390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 421..456
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 425..461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 436..446
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 479..514
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 483..519
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 494..504
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 534..569
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 538..574
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 549..559
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 581..616
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 604..634
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 884..921
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 909..923
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT MUTAGEN 1487..1489
FT /note="RKR->AAA: Reduced binding to ELMO1 and failure to
FT promote engulfment of apoptotic thymocytes."
FT /evidence="ECO:0000269|PubMed:17960134"
FT CONFLICT 264
FT /note="W -> L (in Ref. 1; AAN86966)"
FT /evidence="ECO:0000305"
FT CONFLICT 275..286
FT /note="RDCGGGLQTRTR -> AGLRGRPANSNP (in Ref. 1; AAN86966)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="E -> K (in Ref. 1; AAN86966)"
FT /evidence="ECO:0000305"
FT CONFLICT 821
FT /note="D -> G (in Ref. 2; BAE28021)"
FT /evidence="ECO:0000305"
FT STRAND 424..434
FT /evidence="ECO:0007829|PDB:7R84"
FT STRAND 450..456
FT /evidence="ECO:0007829|PDB:7R84"
FT TURN 1474..1477
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 1480..1484
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 1486..1493
FT /evidence="ECO:0007829|PDB:6IDX"
SQ SEQUENCE 1582 AA; 173297 MW; 6D1AA6D46E2E223B CRC64;
MRGQAAAPGP IWILAPLLLL LLLLGRWARA ASGADIGPGT EQCTTLVQGK FFGYFSAAAV
FPANASRCSW TLRNPDPRRY TLYMKVAKAP APCSGPGRVR TYQFDSFLES TRTYLGVESF
DEVLRLCDSS APLAFLQASK QFLQMQRQQP PQDGDLGPQG EFPSSSDDFS VEYLVVGNRN
PSHAACQMLC RWLDACLAGS RSSHPCGIMQ TPCACLGGDV GDPASSPLVP RGDVCLRDGV
AGGPENCLTS LTQDRGGHGS AGGWKLWSLW GECTRDCGGG LQTRTRTCLP TLGVEGGGCE
GVLEEGRLCN RKACGPTGRS SSRSQSLRST DARRREEFGD ELQQFGFPSP QTGDPAAEEW
SPWSVCSSTC GEGWQTRTRF CVSSSYSTQC SGPLREQRLC NNSAVCPVHG AWDEWSPWSL
CSSTCGRGFR DRTRTCRPPQ FGGNPCEGPE KQTKFCNIAL CPGRAVDGNW NEWSSWSTCS
ASCSQGRQQR TRECNGPSYG GAECQGHWVE TRDCFLQQCP VDGKWQAWAS WGSCSVTCGG
GSQRRERVCS GPFFGGAACQ GPQDEYRQCG AQRCPEPHEI CDEDNFGAVV WKETPAGEVA
AVRCPRNATG LILRRCELDE EGIAFWEPPT YIRCVSIDYR NIQMMTREHL AKAQRGLPGE
GVSEVIQTLL EISQDGTSYS GDLLSTIDVL RNMTEIFRRA YYSPTPGDVQ NFVQIISNLL
AEENRDKWEE AQLMGPNAKE LFRLVEDFVD VIGFRMKDLR DAYQVTDNLV LSIHKLPASG
ATDISFPMKG WRATGDWAKV PEDRVTVSKS VFSTGLAEAD DSSVFVVGTV LYRNLGSFLA
LQRNTTVLNS KVISVTVKPP PRSLLTPLEI EFAHMYNGTT NQTCILWDET DGPSSSAPPQ
LGPWSWRGCR TVPLDALRTR CLCDRLSTFA ILAQLSADAT MDKVTVPSVT LIVGCGVSSL
TLLMLVIIYV SVWRYIRSER SVILINFCLS IISSNALILI GQTQTRNKVV CTLVAAFLHF
FFLSSFCWVL TEAWQSYMAV TGRLRSRLVR KRFLCLGWGL PALVVAISVG FTKAKGYSTM
NYCWLSLEGG LLYAFVGPAA AVVLVNMVIG ILVFNKLVSK DGITDKKLKE RAGASLWSSC
VVLPLLALTW MSAVLAVTDR RSALFQILFA VFDSLEGFVI VMVHCILRRE VQDAVKCRVV
DRQEEGNGDS GGSFQNGHAQ LMTDFEKDVD LACRSVLNKD IAACRTATIT GTFKRPSLPE
EEKMKLAKGP PPTFNSLPAN VSKLHLHGSP RYPGGPLPDF PNHSLTLKKD KAPKSSFIGD
GDIFKKLDSE LSRAQEKALD TSYVILPTAT ATLRPKPKEE PKYSINIDQM PQTRLIHLSM
APDASFPTRS PPAREPPGGA PPEVPPVQPP PPPPPPPPPP QQPIPPPPTL EPAPPSLGDT
GEPAAHPGPS SGAGAKNENV ATLSVSSLER RKSRYAELDF EKIMHTRKRH QDMFQDLNRK
LQHAAEKEKE VPGADSKPEK QQTPNKRAWE SLRKPHGTPA WVKKELEPLP PSPLELRSVE
WEKAGATIPL VGQDIIDLQT EV
