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   27-MAR-2024, entry version 200.
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}.
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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   GlyCosmos; O14514; 7 sites, No reported glycans.
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; 9606-ENSP00000430945; -.
DR   PeptideAtlas; O14514; -.
DR   ProteomicsDB; 48061; -.
DR   Antibodypedia; 7346; 443 antibodies from 32 providers.
DR   CPTC; O14514; 3 antibodies.
DR   DNASU; 575; -.
DR   Ensembl; ENST00000517894.6; ENSP00000430945.1; ENSG00000181790.13.
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   AGR; HGNC:943; -.
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; SAMPRWG; -.
DR   OrthoDB; 4181250at2759; -.
DR   PhylomeDB; O14514; -.
DR   TreeFam; TF331634; -.
DR   PathwayCommons; O14514; -.
DR   SignaLink; O14514; -.
DR   BioGRID-ORCS; 575; 9 hits in 1134 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 112 other cell types or tissues.
DR   ExpressionAtlas; O14514; baseline and differential.
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:0016020; C:membrane; TAS:GDB.
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   CDD; cd15990; 7tmB2_BAI1; 1.
DR   Gene3D; 1.25.40.610; -; 1.
DR   Gene3D; 2.60.220.50; -; 1.
DR   Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 5.
DR   InterPro; IPR043838; AGRB_N.
DR   InterPro; IPR032471; GAIN_dom_N.
DR   InterPro; IPR046338; GAIN_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
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   PANTHER; PTHR12011:SF39; ADHESION G PROTEIN-COUPLED RECEPTOR B1; 1.
DR   PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
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   PRINTS; PR01705; TSP1REPEAT.
DR   SMART; SM00303; GPS; 1.
DR   SMART; SM00008; HormR; 1.
DR   SMART; SM00209; TSP1; 5.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 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.
DR   Genevisible; O14514; HS.
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
//