AGRB1_HUMAN
ID AGRB1_HUMAN Reviewed; 1584 AA.
AC O14514;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Adhesion G protein-coupled receptor B1 {ECO:0000312|HGNC:HGNC:943};
DE AltName: Full=Brain-specific angiogenesis inhibitor 1 {ECO:0000303|PubMed:9393972};
DE Contains:
DE RecName: Full=Vasculostatin-40 {ECO:0000303|PubMed:22330140};
DE Short=Vstat40 {ECO:0000303|PubMed:22330140};
DE Contains:
DE RecName: Full=Vasculostatin-120 {ECO:0000303|PubMed:15782143};
DE Short=Vstat120 {ECO:0000303|PubMed:19176395};
DE Flags: Precursor;
GN Name=ADGRB1 {ECO:0000312|HGNC:HGNC:943};
GN Synonyms=BAI1 {ECO:0000303|PubMed:9393972};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal brain;
RX PubMed=9393972; DOI=10.1038/sj.onc.1201542;
RA Nishimori H., Shiratsuchi T., Urano T., Kimura Y., Kiyono K., Tatsumi K.,
RA Yoshida S., Ono M., Kuwano M., Nakamura Y., Tokino T.;
RT "A novel brain-specific p53-target gene, BAI1, containing thrombospondin
RT type 1 repeats inhibits experimental angiogenesis.";
RL Oncogene 15:2145-2150(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [3]
RP INTERACTION WITH MAGI1.
RX PubMed=9647739; DOI=10.1006/bbrc.1998.8603;
RA Shiratsuchi T., Futamura M., Oda K., Nishimori H., Nakamura Y., Tokino T.;
RT "Cloning and characterization of BAI-associated protein 1: a PDZ domain-
RT containing protein that interacts with BAI1.";
RL Biochem. Biophys. Res. Commun. 247:597-604(1998).
RN [4]
RP INTERACTION WITH BAIAP3.
RX PubMed=9790924; DOI=10.1006/bbrc.1998.9408;
RA Shiratsuchi T., Oda K., Nishimori H., Suzuki M., Takahashi E., Tokino T.,
RA Nakamura Y.;
RT "Cloning and characterization of BAP3 (BAI-associated protein 3), a C2
RT domain-containing protein that interacts with BAI1.";
RL Biochem. Biophys. Res. Commun. 251:158-165(1998).
RN [5]
RP INTERACTION WITH BAIAP2.
RX PubMed=10343108; DOI=10.1159/000015219;
RA Oda K., Shiratsuchi T., Nishimori H., Inazawa J., Yoshikawa H.,
RA Taketani Y., Nakamura Y., Tokino T.;
RT "Identification of BAIAP2 (BAI-associated protein 2), a novel human
RT homologue of hamster IRSp53, whose SH3 domain interacts with the
RT cytoplasmic domain of BAI1.";
RL Cytogenet. Cell Genet. 84:75-82(1999).
RN [6]
RP INTERACTION WITH MAGI3.
RX PubMed=10748157; DOI=10.1074/jbc.m909741199;
RA Wu Y., Dowbenko D., Spencer S., Laura R., Lee J., Gu Q., Lasky L.A.;
RT "Interaction of the tumor suppressor PTEN/MMAC with a PDZ domain of MAGI3,
RT a novel membrane-associated guanylate kinase.";
RL J. Biol. Chem. 275:21477-21485(2000).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
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 [8]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=12074842; DOI=10.1016/s0168-0102(02)00018-4;
RA Mori K., Kanemura Y., Fujikawa H., Nakano A., Ikemoto H., Ozaki I.,
RA Matsumoto T., Tamura K., Yokota M., Arita N.;
RT "Brain-specific angiogenesis inhibitor 1 (BAI1) is expressed in human
RT cerebral neuronal cells.";
RL Neurosci. Res. 43:69-74(2002).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=12507886; DOI=10.1016/s0002-9440(10)63794-7;
RA Kaur B., Brat D.J., Calkins C.C., Van Meir E.G.;
RT "Brain angiogenesis inhibitor 1 is differentially expressed in normal brain
RT and glioblastoma independently of p53 expression.";
RL Am. J. Pathol. 162:19-27(2003).
RN [10]
RP FUNCTION (VASCULOSTATIN-120), SUBCELLULAR LOCATION (VASCULOSTATIN-120),
RP PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF SER-927.
RX PubMed=15782143; DOI=10.1038/sj.onc.1208317;
RA Kaur B., Brat D.J., Devi N.S., Van Meir E.G.;
RT "Vasculostatin, a proteolytic fragment of brain angiogenesis inhibitor 1,
RT is an antiangiogenic and antitumorigenic factor.";
RL Oncogene 24:3632-3642(2005).
RN [11]
RP FUNCTION (VASCULOSTATIN-120), AND INTERACTION WITH CD36
RP (VASCULOSTATIN-120).
RX PubMed=19176395; DOI=10.1158/0008-5472.can-08-1166;
RA Kaur B., Cork S.M., Sandberg E.M., Devi N.S., Zhang Z., Klenotic P.A.,
RA Febbraio M., Shim H., Mao H., Tucker-Burden C., Silverstein R.L.,
RA Brat D.J., Olson J.J., Van Meir E.G.;
RT "Vasculostatin inhibits intracranial glioma growth and negatively regulates
RT in vivo angiogenesis through a CD36-dependent mechanism.";
RL Cancer Res. 69:1212-1220(2009).
RN [12]
RP PROTEOLYTIC PROCESSING.
RX PubMed=22333914; DOI=10.1038/emboj.2012.26;
RA Arac D., Boucard A.A., Bolliger M.F., Nguyen J., Soltis S.M., Sudhof T.C.,
RA Brunger A.T.;
RT "A novel evolutionarily conserved domain of cell-adhesion GPCRs mediates
RT autoproteolysis.";
RL EMBO J. 31:1364-1378(2012).
RN [13]
RP FUNCTION (VASCULOSTATIN-40), SUBCELLULAR LOCATION (VASCULOSTATIN-40 AND
RP VASCULOSTATIN-120), PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF
RP 323-ARG--GLN-325; 326-SER--ARG-328 AND SER-927.
RX PubMed=22330140; DOI=10.1038/onc.2012.1;
RA Cork S.M., Kaur B., Devi N.S., Cooper L., Saltz J.H., Sandberg E.M.,
RA Kaluz S., Van Meir E.G.;
RT "A proprotein convertase/MMP-14 proteolytic cascade releases a novel 40 kDa
RT vasculostatin from tumor suppressor BAI1.";
RL Oncogene 31:5144-5152(2012).
RN [14]
RP FUNCTION, INTERACTION WITH ARRB2 AND DLG4, AND UBIQUITINATION.
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 [15]
RP INTERACTION WITH PARD3 AND TIAM1.
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-609, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=24509909; DOI=10.1096/fj.13-243238;
RA Das S., Sarkar A., Ryan K.A., Fox S., Berger A.H., Juncadella I.J.,
RA Bimczok D., Smythies L.E., Harris P.R., Ravichandran K.S., Crowe S.E.,
RA Smith P.D., Ernst P.B.;
RT "Brain angiogenesis inhibitor 1 is expressed by gastric phagocytes during
RT infection with Helicobacter pylori and mediates the recognition and
RT engulfment of human apoptotic gastric epithelial cells.";
RL FASEB J. 28:2214-2224(2014).
RN [18]
RP ROLE OF N-TERMINAL STALK IN ACTIVITY.
RX PubMed=26710850; DOI=10.1074/jbc.m115.689349;
RA Kishore A., Purcell R.H., Nassiri-Toosi Z., Hall R.A.;
RT "Stalk-dependent and stalk-independent signaling by the adhesion G protein-
RT coupled receptors GPR56 (ADGRG1) and BAI1 (ADGRB1).";
RL J. Biol. Chem. 291:3385-3394(2016).
RN [19]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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:24509909). Also mediates the binding and
CC engulfment of Gram-negative bacteria (PubMed:26838550). Stimulates
CC production of reactive oxygen species by macrophages in response to
CC Gram-negative bacteria, resulting in enhanced microbicidal macrophage
CC activity (PubMed:26838550). In the gastric mucosa, required for
CC recognition and engulfment of apoptotic gastric epithelial cells
CC (PubMed:24509909). Promotes myoblast fusion (By similarity). Activates
CC the Rho pathway in a G-protein-dependent manner (PubMed:23782696).
CC Inhibits MDM2-mediated ubiquitination and degradation of DLG4/PSD95,
CC promoting DLG4 stability and regulating synaptic plasticity (By
CC similarity). Required for the formation of dendritic spines by ensuring
CC the correct localization of PARD3 and TIAM1 (By similarity). Potent
CC inhibitor of angiogenesis in brain and may play a significant role as a
CC mediator of the p53/TP53 signal in suppression of glioblastoma
CC (PubMed:11875720). {ECO:0000250|UniProtKB:C0HL12,
CC ECO:0000250|UniProtKB:Q3UHD1, ECO:0000269|PubMed:11875720,
CC ECO:0000269|PubMed:23782696, ECO:0000269|PubMed:24509909,
CC ECO:0000269|PubMed:26838550}.
CC -!- FUNCTION: [Vasculostatin-120]: Inhibits angiogenesis in a CD36-
CC dependent manner. {ECO:0000269|PubMed:15782143,
CC ECO:0000269|PubMed:19176395}.
CC -!- FUNCTION: [Vasculostatin-40]: Inhibits angiogenesis.
CC {ECO:0000269|PubMed:22330140}.
CC -!- SUBUNIT: Interacts with ELMO1 and DOCK (By similarity). When bound to
CC ELMO1 and DOCK1, acts as a module to promote apoptotic cell engulfment
CC (By similarity). Interacts with MDM2; the interaction results in
CC inhibition of MDM2-mediated ubiquitination and degradation of
CC DLG4/PSD95 (By similarity). Interacts with PARD3 and TIAM1; the
CC interaction is required for correct dendritic. localization of PARD3
CC and TIAM1 and for dendritic spine formation (PubMed:23595754).
CC Interacts with MAGI1 (PubMed:9647739). Interacts with MAGI3
CC (PubMed:10748157). Interacts with BAIAP2 (PubMed:10343108). Interacts
CC with PHYHIP (By similarity). Interacts with DLG4 (via PDZ domain)
CC (PubMed:23782696). Vasculostatin-120: Interacts with CD36
CC (PubMed:19176395). Vasculostatin-120: Interacts with ARRB2
CC (PubMed:23782696). Interacts with BAIAP3; this interaction is direct
CC (PubMed:9790924). {ECO:0000250|UniProtKB:Q3UHD1,
CC ECO:0000269|PubMed:10343108, ECO:0000269|PubMed:10748157,
CC ECO:0000269|PubMed:19176395, ECO:0000269|PubMed:23595754,
CC ECO:0000269|PubMed:23782696, ECO:0000269|PubMed:9647739,
CC ECO:0000269|PubMed:9790924}.
CC -!- INTERACTION:
CC O14514; Q92556-1: ELMO1; NbExp=2; IntAct=EBI-1995178, EBI-15668002;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12074842,
CC ECO:0000269|PubMed:26838550}; Multi-pass membrane protein
CC {ECO:0000255}. Cell projection, phagocytic cup
CC {ECO:0000250|UniProtKB:Q3UHD1}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:Q3UHD1}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:C0HL12}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q3UHD1}.
CC -!- SUBCELLULAR LOCATION: [Vasculostatin-120]: Secreted
CC {ECO:0000269|PubMed:15782143, ECO:0000269|PubMed:22330140}.
CC -!- SUBCELLULAR LOCATION: [Vasculostatin-40]: Secreted
CC {ECO:0000269|PubMed:22330140}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level)
CC (PubMed:12074842, PubMed:12507886). Expressed on mononuclear phagocytes
CC and monocyte-derived macrophages in the gastric mucosa (at protein
CC level) (PubMed:24509909). Expressed in normal pancreatic tissue but not
CC in pancreatic tumor tissue (PubMed:11875720). Reduced or no expression
CC is observed in some glioblastomas (PubMed:12507886).
CC {ECO:0000269|PubMed:11875720, ECO:0000269|PubMed:12074842,
CC ECO:0000269|PubMed:12507886, ECO:0000269|PubMed:24509909}.
CC -!- INDUCTION: By p53/TP53.
CC -!- DOMAIN: The TSP type-1 repeats in the extracellular domain mediate
CC binding to phosphatidylserine. They are also required for bacterial
CC recognition and binding to bacterial outer membrane lipopolysaccharide.
CC {ECO:0000250|UniProtKB:Q3UHD1}.
CC -!- PTM: Proteolytically cleaved to produce vasculostatin-40 and
CC vasculostatin-120 (PubMed:15782143, PubMed:22333914, PubMed:22330140).
CC Vasculostatin-40 is the major form and is produced through proteolytic
CC cleavage by MMP14 between residues 321 and 329 with cleavage likely to
CC be between Ser-326 and Leu-327 (PubMed:22330140).
CC {ECO:0000269|PubMed:15782143, ECO:0000269|PubMed:22330140,
CC ECO:0000269|PubMed:22333914}.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:23782696}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB005297; BAA23647.1; -; mRNA.
DR EMBL; AC139676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS64985.1; -.
DR PIR; T00026; T00026.
DR RefSeq; NP_001693.2; NM_001702.2.
DR RefSeq; XP_011515501.1; XM_011517199.2.
DR AlphaFoldDB; O14514; -.
DR SMR; O14514; -.
DR BioGRID; 107051; 76.
DR DIP; DIP-40884N; -.
DR IntAct; O14514; 8.
DR MINT; O14514; -.
DR STRING; 9606.ENSP00000430945; -.
DR MEROPS; P02.041; -.
DR GlyGen; O14514; 7 sites.
DR iPTMnet; O14514; -.
DR PhosphoSitePlus; O14514; -.
DR BioMuta; ADGRB1; -.
DR EPD; O14514; -.
DR jPOST; O14514; -.
DR MassIVE; O14514; -.
DR PaxDb; O14514; -.
DR PeptideAtlas; O14514; -.
DR PRIDE; O14514; -.
DR ProteomicsDB; 48061; -.
DR Antibodypedia; 7346; 411 antibodies from 32 providers.
DR CPTC; O14514; 3 antibodies.
DR DNASU; 575; -.
DR Ensembl; ENST00000323289.6; ENSP00000313046.5; ENSG00000181790.12.
DR Ensembl; ENST00000517894.6; ENSP00000430945.1; ENSG00000181790.12.
DR GeneID; 575; -.
DR KEGG; hsa:575; -.
DR MANE-Select; ENST00000517894.6; ENSP00000430945.1; NM_001702.3; NP_001693.2.
DR UCSC; uc003ywm.4; human.
DR CTD; 575; -.
DR DisGeNET; 575; -.
DR GeneCards; ADGRB1; -.
DR HGNC; HGNC:943; ADGRB1.
DR HPA; ENSG00000181790; Tissue enriched (brain).
DR MIM; 602682; gene.
DR neXtProt; NX_O14514; -.
DR OpenTargets; ENSG00000181790; -.
DR PharmGKB; PA25247; -.
DR VEuPathDB; HostDB:ENSG00000181790; -.
DR eggNOG; ENOG502QRTN; Eukaryota.
DR GeneTree; ENSGT00940000157432; -.
DR HOGENOM; CLU_003751_1_0_1; -.
DR InParanoid; O14514; -.
DR OMA; GVACQGP; -.
DR OrthoDB; 27621at2759; -.
DR PhylomeDB; O14514; -.
DR TreeFam; TF331634; -.
DR PathwayCommons; O14514; -.
DR SignaLink; O14514; -.
DR BioGRID-ORCS; 575; 7 hits in 1053 CRISPR screens.
DR ChiTaRS; ADGRB1; human.
DR GeneWiki; Brain-specific_angiogenesis_inhibitor_1; -.
DR GenomeRNAi; 575; -.
DR Pharos; O14514; Tbio.
DR PRO; PR:O14514; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; O14514; protein.
DR Bgee; ENSG00000181790; Expressed in right frontal lobe and 111 other tissues.
DR ExpressionAtlas; O14514; baseline and differential.
DR Genevisible; O14514; HS.
DR GO; GO:0005911; C:cell-cell junction; TAS:ProtInc.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:GDB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0001891; C:phagocytic cup; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:UniProtKB.
DR GO; GO:0001530; F:lipopolysaccharide binding; ISS:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
DR GO; GO:0001786; F:phosphatidylserine binding; ISS: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; IMP:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; TAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:UniProtKB.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IMP:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:GDB.
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; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; IDA:UniProtKB.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISS:UniProtKB.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0007422; P:peripheral nervous system development; TAS:ProtInc.
DR GO; GO:0006910; P:phagocytosis, recognition; ISS:UniProtKB.
DR GO; GO:1901741; P:positive regulation of myoblast fusion; ISS:UniProtKB.
DR GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IMP:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
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 Cell junction; Cell membrane; Cell projection; 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..30
FT /evidence="ECO:0000255"
FT CHAIN 31..1584
FT /note="Adhesion G protein-coupled receptor B1"
FT /id="PRO_0000012863"
FT CHAIN 31..926
FT /note="Vasculostatin-120"
FT /evidence="ECO:0000269|PubMed:15782143"
FT /id="PRO_0000441805"
FT CHAIN 31..?327
FT /note="Vasculostatin-40"
FT /evidence="ECO:0000305|PubMed:22330140"
FT /id="PRO_0000441804"
FT TOPO_DOM 31..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..1584
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 146..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000269|PubMed:26710850"
FT REGION 1365..1584
FT /note="Involved in interaction with MAGI1"
FT /evidence="ECO:0000269|PubMed:9647739"
FT REGION 1385..1475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1501..1548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1581..1584
FT /note="Indispensable for interaction with MAGI1"
FT /evidence="ECO:0000269|PubMed:9647739"
FT COMPBIAS 1391..1444
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1452..1471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1501..1543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 926..927
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:15782143"
FT MOD_RES 609
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHD1"
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 323..325
FT /note="RSQ->AAA: Abolishes processing of vasculostatin-40."
FT /evidence="ECO:0000269|PubMed:22330140"
FT MUTAGEN 326..328
FT /note="SLR->AAA: Does not affect processing of
FT vasculostatin-40."
FT /evidence="ECO:0000269|PubMed:22330140"
FT MUTAGEN 927
FT /note="S->A: Abolishes cleavage and production of
FT vasculostatin-120."
FT /evidence="ECO:0000269|PubMed:15782143"
FT MUTAGEN 927
FT /note="S->D: Increased levels of vasculostatin-120 and
FT decreased levels of vasculostatin-40."
FT /evidence="ECO:0000269|PubMed:22330140"
FT CONFLICT 1010
FT /note="V -> M (in Ref. 1; BAA23647)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1584 AA; 173501 MW; A604E634DDD741F7 CRC64;
MRGQAAAPGP VWILAPLLLL LLLLGRRARA AAGADAGPGP EPCATLVQGK FFGYFSAAAV
FPANASRCSW TLRNPDPRRY TLYMKVAKAP VPCSGPGRVR TYQFDSFLES TRTYLGVESF
DEVLRLCDPS APLAFLQASK QFLQMRRQQP PQHDGLRPRA GPPGPTDDFS VEYLVVGNRN
PSRAACQMLC RWLDACLAGS RSSHPCGIMQ TPCACLGGEA GGPAAGPLAP RGDVCLRDAV
AGGPENCLTS LTQDRGGHGA TGGWKLWSLW GECTRDCGGG LQTRTRTCLP APGVEGGGCE
GVLEEGRQCN REACGPAGRT SSRSQSLRST DARRREELGD ELQQFGFPAP QTGDPAAEEW
SPWSVCSSTC GEGWQTRTRF CVSSSYSTQC SGPLREQRLC NNSAVCPVHG AWDEWSPWSL
CSSTCGRGFR DRTRTCRPPQ FGGNPCEGPE KQTKFCNIAL CPGRAVDGNW NEWSSWSACS
ASCSQGRQQR TRECNGPSYG GAECQGHWVE TRDCFLQQCP VDGKWQAWAS WGSCSVTCGA
GSQRRERVCS GPFFGGAACQ GPQDEYRQCG TQRCPEPHEI CDEDNFGAVI WKETPAGEVA
AVRCPRNATG LILRRCELDE EGIAYWEPPT YIRCVSIDYR NIQMMTREHL AKAQRGLPGE
GVSEVIQTLV EISQDGTSYS GDLLSTIDVL RNMTEIFRRA YYSPTPGDVQ NFVQILSNLL
AEENRDKWEE AQLAGPNAKE LFRLVEDFVD VIGFRMKDLR DAYQVTDNLV LSIHKLPASG
ATDISFPMKG WRATGDWAKV PEDRVTVSKS VFSTGLTEAD EASVFVVGTV LYRNLGSFLA
LQRNTTVLNS KVISVTVKPP PRSLRTPLEI EFAHMYNGTT NQTCILWDET DVPSSSAPPQ
LGPWSWRGCR TVPLDALRTR CLCDRLSTFA ILAQLSADAN MEKATLPSVT LIVGCGVSSL
TLLMLVIIYV SVWRYIRSER SVILINFCLS IISSNALILI GQTQTRNKVV CTLVAAFLHF
FFLSSFCWVL TEAWQSYMAV TGHLRNRLIR KRFLCLGWGL PALVVAISVG FTKAKGYSTM
NYCWLSLEGG LLYAFVGPAA AVVLVNMVIG ILVFNKLVSK DGITDKKLKE RAGASLWSSC
VVLPLLALTW MSAVLAVTDR RSALFQILFA VFDSLEGFVI VMVHCILRRE VQDAVKCRVV
DRQEEGNGDS GGSFQNGHAQ LMTDFEKDVD LACRSVLNKD IAACRTATIT GTLKRPSLPE
EEKLKLAHAK GPPTNFNSLP ANVSKLHLHG SPRYPGGPLP DFPNHSLTLK RDKAPKSSFV
GDGDIFKKLD SELSRAQEKA LDTSYVILPT ATATLRPKPK EEPKYSIHID QMPQTRLIHL
STAPEASLPA RSPPSRQPPS GGPPEAPPAQ PPPPPPPPPP PPQQPLPPPP NLEPAPPSLG
DPGEPAAHPG PSTGPSTKNE NVATLSVSSL ERRKSRYAEL DFEKIMHTRK RHQDMFQDLN
RKLQHAAEKD KEVLGPDSKP EKQQTPNKRP WESLRKAHGT PTWVKKELEP LQPSPLELRS
VEWERSGATI PLVGQDIIDL QTEV
