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   13-FEB-2019, entry version 171.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Tatsumi K., Yoshida S., Ono M., Kuwano M., Nakamura Y., Tokino T.;
RT   "A novel brain-specific p53-target gene, BAI1, containing
RT   thrombospondin 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.,
RA   Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA   Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA   Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA   Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA   DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA   Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA   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.,
RA   O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA   Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA   Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA   Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA   Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA   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.,
RA   Tokino T.;
RT   "Cloning and characterization of BAI-associated protein 1: a PDZ
RT   domain-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.,
RA   Tokino T., 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;
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
RT   MAGI3, 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.,
RA   Motoi F., Horii A., Tani K., Asano S., Nakamura Y., Matsuno S.;
RT   "Overexpression of the p53-inducible brain-specific angiogenesis
RT   inhibitor 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
RT   brain and glioblastoma independently of p53 expression.";
RL   Am. J. Pathol. 162:19-27(2003).
RN   [10]
RP   FUNCTION (VASCULOSTATIN-120), SUBCELLULAR LOCATION
RP   (VASCULOSTATIN-120), PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF
RP   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
RT   1, 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
RT   regulates 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.,
RA   Sudhof T.C., Brunger A.T.;
RT   "A novel evolutionarily conserved domain of cell-adhesion GPCRs
RT   mediates autoproteolysis.";
RL   EMBO J. 31:1364-1378(2012).
RN   [13]
RP   FUNCTION (VASCULOSTATIN-40), SUBCELLULAR LOCATION (VASCULOSTATIN-40
RP   AND 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
RT   40 kDa 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
RP   BY 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
RT   during infection with Helicobacter pylori and mediates the recognition
RT   and 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
RT   protein-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
RT   microbicidal activity against Gram-negative bacteria.";
RL   Sci. Signal. 9:RA14-RA14(2016).
CC   -!- FUNCTION: Phosphatidylserine receptor which enhances the
CC       engulfment of apoptotic cells (PubMed:24509909). Also mediates the
CC       binding and engulfment of Gram-negative bacteria
CC       (PubMed:26838550). Stimulates production of reactive oxygen
CC       species by macrophages in response to Gram-negative bacteria,
CC       resulting in enhanced microbicidal macrophage activity
CC       (PubMed:26838550). In the gastric mucosa, required for recognition
CC       and engulfment of apoptotic gastric epithelial cells
CC       (PubMed:24509909). Promotes myoblast fusion (By similarity).
CC       Activates the Rho pathway in a G-protein-dependent manner
CC       (PubMed:23782696). Inhibits MDM2-mediated ubiquitination and
CC       degradation of DLG4/PSD95, promoting DLG4 stability and regulating
CC       synaptic plasticity (By similarity). 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
CC       and may play a significant role as a mediator of the p53/TP53
CC       signal in suppression of glioblastoma (PubMed:11875720).
CC       {ECO:0000250|UniProtKB:C0HL12, ECO:0000250|UniProtKB:Q3UHD1,
CC       ECO:0000269|PubMed:11875720, ECO:0000269|PubMed:23782696,
CC       ECO:0000269|PubMed:24509909, 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
CC       to ELMO1 and DOCK1, acts as a module to promote apoptotic cell
CC       engulfment (By similarity). Interacts with MDM2; the interaction
CC       results in inhibition of MDM2-mediated ubiquitination and
CC       degradation of DLG4/PSD95 (By similarity). Interacts with PARD3
CC       and TIAM1; the interaction is required for correct dendritic.
CC       localization of PARD3 and TIAM1 and for dendritic spine formation
CC       (PubMed:23595754). Interacts with MAGI1 (PubMed:9647739).
CC       Interacts with MAGI3 (PubMed:10748157). Interacts with BAIAP2
CC       (PubMed:10343108). Interacts with PHYHIP (By similarity).
CC       Interacts with DLG4 (via PDZ domain) (PubMed:23782696).
CC       Vasculostatin-120: Interacts with CD36 (PubMed:19176395).
CC       Vasculostatin-120: Interacts with ARRB2 (PubMed:23782696).
CC       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       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}. Cell junction, synapse,
CC       postsynaptic cell membrane, 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
CC       phagocytes and monocyte-derived macrophages in the gastric mucosa
CC       (at protein level) (PubMed:24509909). Expressed in normal
CC       pancreatic tissue but not in pancreatic tumor tissue
CC       (PubMed:11875720). Reduced or no expression is observed in some
CC       glioblastomas (PubMed:12507886). {ECO:0000269|PubMed:11875720,
CC       ECO:0000269|PubMed:12074842, ECO:0000269|PubMed:12507886,
CC       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
CC       bacterial recognition and binding to bacterial outer membrane
CC       lipopolysaccharide. {ECO:0000250|UniProtKB:Q3UHD1}.
CC   -!- PTM: Proteolytically cleaved to produce vasculostatin-40 and
CC       vasculostatin-120 (PubMed:15782143, PubMed:22333914,
CC       PubMed:22330140). Vasculostatin-40 is the major form and is
CC       produced through proteolytic cleavage by MMP14 between residues
CC       321 and 329 with cleavage likely to be between Ser-326 and Leu-327
CC       (PubMed:22330140). {ECO:0000269|PubMed:15782143,
CC       ECO:0000269|PubMed:22330140, ECO:0000269|PubMed:22333914}.
CC   -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:23782696}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       LN-TM7 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   UniGene; Hs.194654; -.
DR   ProteinModelPortal; O14514; -.
DR   SMR; O14514; -.
DR   BioGrid; 107051; 20.
DR   DIP; DIP-40884N; -.
DR   IntAct; O14514; 8.
DR   MINT; O14514; -.
DR   STRING; 9606.ENSP00000313046; -.
DR   iPTMnet; O14514; -.
DR   PhosphoSitePlus; O14514; -.
DR   BioMuta; ADGRB1; -.
DR   EPD; O14514; -.
DR   jPOST; O14514; -.
DR   PaxDb; O14514; -.
DR   PeptideAtlas; O14514; -.
DR   PRIDE; O14514; -.
DR   ProteomicsDB; 48061; -.
DR   DNASU; 575; -.
DR   Ensembl; ENST00000323289; ENSP00000313046; ENSG00000181790.
DR   Ensembl; ENST00000517894; ENSP00000430945; ENSG00000181790.
DR   GeneID; 575; -.
DR   KEGG; hsa:575; -.
DR   UCSC; uc003ywm.4; human.
DR   CTD; 575; -.
DR   DisGeNET; 575; -.
DR   EuPathDB; HostDB:ENSG00000181790.10; -.
DR   GeneCards; ADGRB1; -.
DR   H-InvDB; HIX0025534; -.
DR   HGNC; HGNC:943; ADGRB1.
DR   MIM; 602682; gene.
DR   neXtProt; NX_O14514; -.
DR   OpenTargets; ENSG00000181790; -.
DR   PharmGKB; PA25247; -.
DR   eggNOG; ENOG410IEA0; Eukaryota.
DR   eggNOG; ENOG4111FBM; LUCA.
DR   GeneTree; ENSGT00940000157432; -.
DR   HOGENOM; HOG000230916; -.
DR   HOVERGEN; HBG004813; -.
DR   InParanoid; O14514; -.
DR   KO; K04596; -.
DR   OMA; RLIHLNM; -.
DR   OrthoDB; 27621at2759; -.
DR   PhylomeDB; O14514; -.
DR   TreeFam; TF331634; -.
DR   SignaLink; O14514; -.
DR   ChiTaRS; ADGRB1; human.
DR   GeneWiki; Brain-specific_angiogenesis_inhibitor_1; -.
DR   GenomeRNAi; 575; -.
DR   PRO; PR:O14514; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   Bgee; ENSG00000181790; Expressed in 129 organ(s), highest expression level in anterior cingulate cortex.
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:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
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; 4.10.1240.10; -; 1.
DR   InterPro; IPR032471; GAIN_dom_N.
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; 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; Complete proteome;
KW   Disulfide bond; G-protein coupled receptor; Glycoprotein; Immunity;
KW   Innate immunity; Membrane; Myogenesis; Neurogenesis; Phagocytosis;
KW   Phosphoprotein; Postsynaptic cell membrane; Receptor;
KW   Reference proteome; Repeat; Secreted; Signal; Synapse; Transducer;
KW   Transmembrane; Transmembrane helix; Ubl conjugation.
FT   SIGNAL        1     30       {ECO:0000255}.
FT   CHAIN        31   1584       Adhesion G protein-coupled receptor B1.
FT                                /FTId=PRO_0000012863.
FT   CHAIN        31    926       Vasculostatin-120.
FT                                {ECO:0000269|PubMed:15782143}.
FT                                /FTId=PRO_0000441805.
FT   CHAIN        31   ?327       Vasculostatin-40.
FT                                {ECO:0000305|PubMed:22330140}.
FT                                /FTId=PRO_0000441804.
FT   TOPO_DOM     31    948       Extracellular. {ECO:0000255}.
FT   TRANSMEM    949    969       Helical; Name=1. {ECO:0000255}.
FT   TOPO_DOM    970    980       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    981   1001       Helical; Name=2. {ECO:0000255}.
FT   TOPO_DOM   1002   1008       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1009   1029       Helical; Name=3. {ECO:0000255}.
FT   TOPO_DOM   1030   1052       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1053   1073       Helical; Name=4. {ECO:0000255}.
FT   TOPO_DOM   1074   1093       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1094   1114       Helical; Name=5. {ECO:0000255}.
FT   TOPO_DOM   1115   1136       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1137   1157       Helical; Name=6. {ECO:0000255}.
FT   TOPO_DOM   1158   1166       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1167   1187       Helical; Name=7. {ECO:0000255}.
FT   TOPO_DOM   1188   1584       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      261    315       TSP type-1 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      354    407       TSP type-1 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      409    462       TSP type-1 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      467    520       TSP type-1 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      522    575       TSP type-1 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      881    938       GPS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00098}.
FT   REGION      927    943       N-terminal stalk following vasculostatin-
FT                                120 cleavage which is not required for
FT                                signaling activity.
FT                                {ECO:0000269|PubMed:26710850}.
FT   REGION     1365   1584       Involved in interaction with MAGI1.
FT                                {ECO:0000269|PubMed:9647739}.
FT   REGION     1581   1584       Indispensable for interaction with MAGI1.
FT                                {ECO:0000269|PubMed:9647739}.
FT   COMPBIAS   1411   1422       Poly-Pro.
FT   COMPBIAS   1425   1430       Poly-Pro.
FT   SITE        926    927       Cleavage. {ECO:0000269|PubMed:15782143}.
FT   MOD_RES     609    609       Phosphothreonine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1469   1469       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q3UHD1}.
FT   CARBOHYD     64     64       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    401    401       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    607    607       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    692    692       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    844    844       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    877    877       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    881    881       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    273    309       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    277    314       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    288    299       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    366    400       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    370    406       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    381    390       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    421    456       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    425    461       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    436    446       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    479    514       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    483    519       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    494    504       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    534    569       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    538    574       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    549    559       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    581    616       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    604    634       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    884    921       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    909    923       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   MUTAGEN     323    325       RSQ->AAA: Abolishes processing of
FT                                vasculostatin-40.
FT                                {ECO:0000269|PubMed:22330140}.
FT   MUTAGEN     326    328       SLR->AAA: Does not affect processing of
FT                                vasculostatin-40.
FT                                {ECO:0000269|PubMed:22330140}.
FT   MUTAGEN     927    927       S->A: Abolishes cleavage and production
FT                                of vasculostatin-120.
FT                                {ECO:0000269|PubMed:15782143}.
FT   MUTAGEN     927    927       S->D: Increased levels of vasculostatin-
FT                                120 and decreased levels of
FT                                vasculostatin-40.
FT                                {ECO:0000269|PubMed:22330140}.
FT   CONFLICT   1010   1010       V -> M (in Ref. 1; BAA23647).
FT                                {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
//