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Adhesion G protein-coupled receptor B1 (Brain-specific angiogenesis inhibitor 1) [Cleaved into: Vasculostatin-40 (Vstat40); Vasculostatin-120 (Vstat120)]

 AGRB1_HUMAN             Reviewed;        1584 AA.
O14514;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
31-OCT-2012, sequence version 2.
18-JUL-2018, entry version 166.
RecName: Full=Adhesion G protein-coupled receptor B1 {ECO:0000312|HGNC:HGNC:943};
AltName: Full=Brain-specific angiogenesis inhibitor 1 {ECO:0000303|PubMed:9393972};
Contains:
RecName: Full=Vasculostatin-40 {ECO:0000303|PubMed:22330140};
Short=Vstat40 {ECO:0000303|PubMed:22330140};
Contains:
RecName: Full=Vasculostatin-120 {ECO:0000303|PubMed:15782143};
Short=Vstat120 {ECO:0000303|PubMed:19176395};
Flags: Precursor;
Name=ADGRB1 {ECO:0000312|HGNC:HGNC:943};
Synonyms=BAI1 {ECO:0000303|PubMed:9393972};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fetal brain;
PubMed=9393972; DOI=10.1038/sj.onc.1201542;
Nishimori H., Shiratsuchi T., Urano T., Kimura Y., Kiyono K.,
Tatsumi K., Yoshida S., Ono M., Kuwano M., Nakamura Y., Tokino T.;
"A novel brain-specific p53-target gene, BAI1, containing
thrombospondin type 1 repeats inhibits experimental angiogenesis.";
Oncogene 15:2145-2150(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[3]
INTERACTION WITH MAGI1.
PubMed=9647739; DOI=10.1006/bbrc.1998.8603;
Shiratsuchi T., Futamura M., Oda K., Nishimori H., Nakamura Y.,
Tokino T.;
"Cloning and characterization of BAI-associated protein 1: a PDZ
domain-containing protein that interacts with BAI1.";
Biochem. Biophys. Res. Commun. 247:597-604(1998).
[4]
INTERACTION WITH BAIAP3.
PubMed=9790924; DOI=10.1006/bbrc.1998.9408;
Shiratsuchi T., Oda K., Nishimori H., Suzuki M., Takahashi E.,
Tokino T., Nakamura Y.;
"Cloning and characterization of BAP3 (BAI-associated protein 3), a C2
domain-containing protein that interacts with BAI1.";
Biochem. Biophys. Res. Commun. 251:158-165(1998).
[5]
INTERACTION WITH BAIAP2.
PubMed=10343108;
Oda K., Shiratsuchi T., Nishimori H., Inazawa J., Yoshikawa H.,
Taketani Y., Nakamura Y., Tokino T.;
"Identification of BAIAP2 (BAI-associated protein 2), a novel human
homologue of hamster IRSp53, whose SH3 domain interacts with the
cytoplasmic domain of BAI1.";
Cytogenet. Cell Genet. 84:75-82(1999).
[6]
INTERACTION WITH MAGI3.
PubMed=10748157; DOI=10.1074/jbc.M909741199;
Wu Y., Dowbenko D., Spencer S., Laura R., Lee J., Gu Q., Lasky L.A.;
"Interaction of the tumor suppressor PTEN/MMAC with a PDZ domain of
MAGI3, a novel membrane-associated guanylate kinase.";
J. Biol. Chem. 275:21477-21485(2000).
[7]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=11875720; DOI=10.1038/sj.bjc.6600067;
Duda D.G., Sunamura M., Lozonschi L., Yokoyama T., Yatsuoka T.,
Motoi F., Horii A., Tani K., Asano S., Nakamura Y., Matsuno S.;
"Overexpression of the p53-inducible brain-specific angiogenesis
inhibitor 1 suppresses efficiently tumour angiogenesis.";
Br. J. Cancer 86:490-496(2002).
[8]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=12074842; DOI=10.1016/S0168-0102(02)00018-4;
Mori K., Kanemura Y., Fujikawa H., Nakano A., Ikemoto H., Ozaki I.,
Matsumoto T., Tamura K., Yokota M., Arita N.;
"Brain-specific angiogenesis inhibitor 1 (BAI1) is expressed in human
cerebral neuronal cells.";
Neurosci. Res. 43:69-74(2002).
[9]
TISSUE SPECIFICITY.
PubMed=12507886; DOI=10.1016/S0002-9440(10)63794-7;
Kaur B., Brat D.J., Calkins C.C., Van Meir E.G.;
"Brain angiogenesis inhibitor 1 is differentially expressed in normal
brain and glioblastoma independently of p53 expression.";
Am. J. Pathol. 162:19-27(2003).
[10]
FUNCTION (VASCULOSTATIN-120), SUBCELLULAR LOCATION
(VASCULOSTATIN-120), PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF
SER-927.
PubMed=15782143; DOI=10.1038/sj.onc.1208317;
Kaur B., Brat D.J., Devi N.S., Van Meir E.G.;
"Vasculostatin, a proteolytic fragment of brain angiogenesis inhibitor
1, is an antiangiogenic and antitumorigenic factor.";
Oncogene 24:3632-3642(2005).
[11]
FUNCTION (VASCULOSTATIN-120), AND INTERACTION WITH CD36
(VASCULOSTATIN-120).
PubMed=19176395; DOI=10.1158/0008-5472.CAN-08-1166;
Kaur B., Cork S.M., Sandberg E.M., Devi N.S., Zhang Z., Klenotic P.A.,
Febbraio M., Shim H., Mao H., Tucker-Burden C., Silverstein R.L.,
Brat D.J., Olson J.J., Van Meir E.G.;
"Vasculostatin inhibits intracranial glioma growth and negatively
regulates in vivo angiogenesis through a CD36-dependent mechanism.";
Cancer Res. 69:1212-1220(2009).
[12]
PROTEOLYTIC PROCESSING.
PubMed=22333914; DOI=10.1038/emboj.2012.26;
Arac D., Boucard A.A., Bolliger M.F., Nguyen J., Soltis S.M.,
Sudhof T.C., Brunger A.T.;
"A novel evolutionarily conserved domain of cell-adhesion GPCRs
mediates autoproteolysis.";
EMBO J. 31:1364-1378(2012).
[13]
FUNCTION (VASCULOSTATIN-40), SUBCELLULAR LOCATION (VASCULOSTATIN-40
AND VASCULOSTATIN-120), PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF
323-ARG--GLN-325; 326-SER--ARG-328 AND SER-927.
PubMed=22330140; DOI=10.1038/onc.2012.1;
Cork S.M., Kaur B., Devi N.S., Cooper L., Saltz J.H., Sandberg E.M.,
Kaluz S., Van Meir E.G.;
"A proprotein convertase/MMP-14 proteolytic cascade releases a novel
40 kDa vasculostatin from tumor suppressor BAI1.";
Oncogene 31:5144-5152(2012).
[14]
FUNCTION, INTERACTION WITH ARRB2 AND DLG4, AND UBIQUITINATION.
PubMed=23782696; DOI=10.1074/jbc.M113.489757;
Stephenson J.R., Paavola K.J., Schaefer S.A., Kaur B., Van Meir E.G.,
Hall R.A.;
"Brain-specific angiogenesis inhibitor-1 signaling, regulation, and
enrichment in the postsynaptic density.";
J. Biol. Chem. 288:22248-22256(2013).
[15]
INTERACTION WITH PARD3 AND TIAM1.
PubMed=23595754; DOI=10.1523/JNEUROSCI.3978-12.2013;
Duman J.G., Tzeng C.P., Tu Y.K., Munjal T., Schwechter B., Ho T.S.,
Tolias K.F.;
"The adhesion-GPCR BAI1 regulates synaptogenesis by controlling the
recruitment of the Par3/Tiam1 polarity complex to synaptic sites.";
J. Neurosci. 33:6964-6978(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-609, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=24509909; DOI=10.1096/fj.13-243238;
Das S., Sarkar A., Ryan K.A., Fox S., Berger A.H., Juncadella I.J.,
Bimczok D., Smythies L.E., Harris P.R., Ravichandran K.S., Crowe S.E.,
Smith P.D., Ernst P.B.;
"Brain angiogenesis inhibitor 1 is expressed by gastric phagocytes
during infection with Helicobacter pylori and mediates the recognition
and engulfment of human apoptotic gastric epithelial cells.";
FASEB J. 28:2214-2224(2014).
[18]
ROLE OF N-TERMINAL STALK IN ACTIVITY.
PubMed=26710850; DOI=10.1074/jbc.M115.689349;
Kishore A., Purcell R.H., Nassiri-Toosi Z., Hall R.A.;
"Stalk-dependent and stalk-independent signaling by the adhesion G
protein-coupled receptors GPR56 (ADGRG1) and BAI1 (ADGRB1).";
J. Biol. Chem. 291:3385-3394(2016).
[19]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=26838550; DOI=10.1126/scisignal.aac6250;
Billings E.A., Lee C.S., Owen K.A., D'Souza R.S., Ravichandran K.S.,
Casanova J.E.;
"The adhesion GPCR BAI1 mediates macrophage ROS production and
microbicidal activity against Gram-negative bacteria.";
Sci. Signal. 9:RA14-RA14(2016).
-!- FUNCTION: Phosphatidylserine receptor which enhances the
engulfment of apoptotic cells (PubMed:24509909). Also mediates the
binding and engulfment of Gram-negative bacteria
(PubMed:26838550). Stimulates production of reactive oxygen
species by macrophages in response to Gram-negative bacteria,
resulting in enhanced microbicidal macrophage activity
(PubMed:26838550). In the gastric mucosa, required for recognition
and engulfment of apoptotic gastric epithelial cells
(PubMed:24509909). Promotes myoblast fusion (By similarity).
Activates the Rho pathway in a G-protein-dependent manner
(PubMed:23782696). Inhibits MDM2-mediated ubiquitination and
degradation of DLG4/PSD95, promoting DLG4 stability and regulating
synaptic plasticity (By similarity). Required for the formation of
dendritic spines by ensuring the correct localization of PARD3 and
TIAM1 (By similarity). Potent inhibitor of angiogenesis in brain
and may play a significant role as a mediator of the p53/TP53
signal in suppression of glioblastoma (PubMed:11875720).
{ECO:0000250|UniProtKB:C0HL12, ECO:0000250|UniProtKB:Q3UHD1,
ECO:0000269|PubMed:11875720, ECO:0000269|PubMed:23782696,
ECO:0000269|PubMed:24509909, ECO:0000269|PubMed:26838550}.
-!- FUNCTION: Vasculostatin-120: Inhibits angiogenesis in a CD36-
dependent manner. {ECO:0000269|PubMed:15782143,
ECO:0000269|PubMed:19176395}.
-!- FUNCTION: Vasculostatin-40: Inhibits angiogenesis.
{ECO:0000269|PubMed:22330140}.
-!- SUBUNIT: Interacts with ELMO1 and DOCK (By similarity). When bound
to ELMO1 and DOCK1, acts as a module to promote apoptotic cell
engulfment (By similarity). Interacts with MDM2; the interaction
results in inhibition of MDM2-mediated ubiquitination and
degradation of DLG4/PSD95 (By similarity). Interacts with PARD3
and TIAM1; the interaction is required for correct dendritic.
localization of PARD3 and TIAM1 and for dendritic spine formation
(PubMed:23595754). Interacts with MAGI1 (PubMed:9647739).
Interacts with MAGI3 (PubMed:10748157). Interacts with BAIAP2
(PubMed:10343108). Interacts with PHYHIP (By similarity).
Interacts with DLG4 (via PDZ domain) (PubMed:23782696).
Vasculostatin-120: Interacts with CD36 (PubMed:19176395).
Vasculostatin-120: Interacts with ARRB2 (PubMed:23782696).
Interacts with BAIAP3; this interaction is direct
(PubMed:9790924). {ECO:0000250|UniProtKB:Q3UHD1,
ECO:0000269|PubMed:10343108, ECO:0000269|PubMed:10748157,
ECO:0000269|PubMed:19176395, ECO:0000269|PubMed:23595754,
ECO:0000269|PubMed:23782696, ECO:0000269|PubMed:9647739,
ECO:0000269|PubMed:9790924}.
-!- INTERACTION:
Q92556-1:ELMO1; NbExp=2; IntAct=EBI-1995178, EBI-15668002;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12074842,
ECO:0000269|PubMed:26838550}; Multi-pass membrane protein
{ECO:0000255}. Cell projection, phagocytic cup
{ECO:0000250|UniProtKB:Q3UHD1}. Cell junction, focal adhesion
{ECO:0000250|UniProtKB:Q3UHD1}. Cell projection, dendritic spine
{ECO:0000250|UniProtKB:C0HL12}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density
{ECO:0000250|UniProtKB:Q3UHD1}.
-!- SUBCELLULAR LOCATION: Vasculostatin-120: Secreted
{ECO:0000269|PubMed:15782143, ECO:0000269|PubMed:22330140}.
-!- SUBCELLULAR LOCATION: Vasculostatin-40: Secreted
{ECO:0000269|PubMed:22330140}.
-!- TISSUE SPECIFICITY: Expressed in brain (at protein level)
(PubMed:12074842, PubMed:12507886). Expressed on mononuclear
phagocytes and monocyte-derived macrophages in the gastric mucosa
(at protein level) (PubMed:24509909). Expressed in normal
pancreatic tissue but not in pancreatic tumor tissue
(PubMed:11875720). Reduced or no expression is observed in some
glioblastomas (PubMed:12507886). {ECO:0000269|PubMed:11875720,
ECO:0000269|PubMed:12074842, ECO:0000269|PubMed:12507886,
ECO:0000269|PubMed:24509909}.
-!- INDUCTION: By p53/TP53.
-!- DOMAIN: The TSP type-1 repeats in the extracellular domain mediate
binding to phosphatidylserine. They are also required for
bacterial recognition and binding to bacterial outer membrane
lipopolysaccharide. {ECO:0000250|UniProtKB:Q3UHD1}.
-!- PTM: Proteolytically cleaved to produce vasculostatin-40 and
vasculostatin-120 (PubMed:15782143, PubMed:22333914,
PubMed:22330140). Vasculostatin-40 is the major form and is
produced through proteolytic cleavage by MMP14 between residues
321 and 329 with cleavage likely to be between Ser-326 and Leu-327
(PubMed:22330140). {ECO:0000269|PubMed:15782143,
ECO:0000269|PubMed:22330140, ECO:0000269|PubMed:22333914}.
-!- PTM: Ubiquitinated. {ECO:0000269|PubMed:23782696}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
LN-TM7 subfamily. {ECO:0000305}.
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EMBL; AB005297; BAA23647.1; -; mRNA.
EMBL; AC139676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS64985.1; -.
PIR; T00026; T00026.
RefSeq; NP_001693.2; NM_001702.2.
RefSeq; XP_011515501.1; XM_011517199.2.
UniGene; Hs.194654; -.
ProteinModelPortal; O14514; -.
SMR; O14514; -.
BioGrid; 107051; 20.
DIP; DIP-40884N; -.
IntAct; O14514; 5.
MINT; O14514; -.
STRING; 9606.ENSP00000313046; -.
iPTMnet; O14514; -.
PhosphoSitePlus; O14514; -.
BioMuta; BAI1; -.
EPD; O14514; -.
PaxDb; O14514; -.
PeptideAtlas; O14514; -.
PRIDE; O14514; -.
ProteomicsDB; 48061; -.
DNASU; 575; -.
Ensembl; ENST00000323289; ENSP00000313046; ENSG00000181790.
Ensembl; ENST00000517894; ENSP00000430945; ENSG00000181790.
GeneID; 575; -.
KEGG; hsa:575; -.
UCSC; uc003ywm.4; human.
CTD; 575; -.
DisGeNET; 575; -.
EuPathDB; HostDB:ENSG00000181790.10; -.
GeneCards; ADGRB1; -.
H-InvDB; HIX0025534; -.
HGNC; HGNC:943; ADGRB1.
MIM; 602682; gene.
neXtProt; NX_O14514; -.
OpenTargets; ENSG00000181790; -.
PharmGKB; PA25247; -.
eggNOG; ENOG410IEA0; Eukaryota.
eggNOG; ENOG4111FBM; LUCA.
GeneTree; ENSGT00920000148969; -.
HOGENOM; HOG000230916; -.
HOVERGEN; HBG004813; -.
InParanoid; O14514; -.
KO; K04596; -.
OMA; SWRGCRT; -.
OrthoDB; EOG091G00C7; -.
PhylomeDB; O14514; -.
TreeFam; TF331634; -.
SignaLink; O14514; -.
ChiTaRS; ADGRB1; human.
GeneWiki; Brain-specific_angiogenesis_inhibitor_1; -.
GenomeRNAi; 575; -.
PRO; PR:O14514; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000181790; -.
CleanEx; HS_BAI1; -.
ExpressionAtlas; O14514; baseline and differential.
Genevisible; O14514; HS.
GO; GO:0005911; C:cell-cell junction; TAS:ProtInc.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; TAS:GDB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0001891; C:phagocytic cup; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0004930; F:G-protein coupled receptor activity; IDA:UniProtKB.
GO; GO:0001530; F:lipopolysaccharide binding; ISS:UniProtKB.
GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
GO; GO:0001786; F:phosphatidylserine binding; ISS:UniProtKB.
GO; GO:0043277; P:apoptotic cell clearance; IMP:UniProtKB.
GO; GO:0007409; P:axonogenesis; TAS:ProtInc.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:UniProtKB.
GO; GO:0043652; P:engulfment of apoptotic cell; IMP:UniProtKB.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:GDB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
GO; GO:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
GO; GO:0010596; P:negative regulation of endothelial cell migration; IDA:UniProtKB.
GO; GO:0042177; P:negative regulation of protein catabolic process; ISS:UniProtKB.
GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
GO; GO:0007422; P:peripheral nervous system development; TAS:ProtInc.
GO; GO:0006910; P:phagocytosis, recognition; ISS:UniProtKB.
GO; GO:1901741; P:positive regulation of myoblast fusion; ISS:UniProtKB.
GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IMP:UniProtKB.
GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
Gene3D; 2.20.100.10; -; 5.
Gene3D; 4.10.1240.10; -; 1.
InterPro; IPR032471; GAIN_dom_N.
InterPro; IPR017981; GPCR_2-like.
InterPro; IPR008077; GPCR_2_brain_angio_inhib.
InterPro; IPR036445; GPCR_2_extracell_dom_sf.
InterPro; IPR001879; GPCR_2_extracellular_dom.
InterPro; IPR000832; GPCR_2_secretin-like.
InterPro; IPR000203; GPS.
InterPro; IPR000884; TSP1_rpt.
InterPro; IPR036383; TSP1_rpt_sf.
Pfam; PF00002; 7tm_2; 1.
Pfam; PF16489; GAIN; 1.
Pfam; PF01825; GPS; 1.
Pfam; PF02793; HRM; 1.
Pfam; PF00090; TSP_1; 5.
PRINTS; PR01694; BAIPRECURSOR.
PRINTS; PR00249; GPCRSECRETIN.
SMART; SM00303; GPS; 1.
SMART; SM00008; HormR; 1.
SMART; SM00209; TSP1; 5.
SUPFAM; SSF82895; SSF82895; 5.
PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PROSITE; PS50221; GPS; 1.
PROSITE; PS50092; TSP1; 5.
1: Evidence at protein level;
Cell junction; Cell membrane; Cell projection; Complete proteome;
Disulfide bond; G-protein coupled receptor; Glycoprotein; Immunity;
Innate immunity; Membrane; Myogenesis; Neurogenesis; Phagocytosis;
Phosphoprotein; Postsynaptic cell membrane; Receptor;
Reference proteome; Repeat; Secreted; Signal; Synapse; Transducer;
Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 1584 Adhesion G protein-coupled receptor B1.
/FTId=PRO_0000012863.
CHAIN 31 926 Vasculostatin-120.
{ECO:0000269|PubMed:15782143}.
/FTId=PRO_0000441805.
CHAIN 31 ?327 Vasculostatin-40.
{ECO:0000305|PubMed:22330140}.
/FTId=PRO_0000441804.
TOPO_DOM 31 948 Extracellular. {ECO:0000255}.
TRANSMEM 949 969 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 970 980 Cytoplasmic. {ECO:0000255}.
TRANSMEM 981 1001 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 1002 1008 Extracellular. {ECO:0000255}.
TRANSMEM 1009 1029 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 1030 1052 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1053 1073 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 1074 1093 Extracellular. {ECO:0000255}.
TRANSMEM 1094 1114 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 1115 1136 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1137 1157 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 1158 1166 Extracellular. {ECO:0000255}.
TRANSMEM 1167 1187 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 1188 1584 Cytoplasmic. {ECO:0000255}.
DOMAIN 261 315 TSP type-1 1. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 354 407 TSP type-1 2. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 409 462 TSP type-1 3. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 467 520 TSP type-1 4. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 522 575 TSP type-1 5. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 881 938 GPS. {ECO:0000255|PROSITE-
ProRule:PRU00098}.
REGION 927 943 N-terminal stalk following vasculostatin-
120 cleavage which is not required for
signaling activity.
{ECO:0000269|PubMed:26710850}.
REGION 1365 1584 Involved in interaction with MAGI1.
{ECO:0000269|PubMed:9647739}.
REGION 1581 1584 Indispensable for interaction with MAGI1.
{ECO:0000269|PubMed:9647739}.
COMPBIAS 1411 1422 Poly-Pro.
COMPBIAS 1425 1430 Poly-Pro.
SITE 926 927 Cleavage. {ECO:0000269|PubMed:15782143}.
MOD_RES 609 609 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1469 1469 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UHD1}.
CARBOHYD 64 64 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 401 401 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 607 607 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 692 692 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 844 844 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 877 877 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 881 881 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 273 309 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 277 314 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 288 299 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 366 400 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 370 406 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 381 390 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 421 456 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 425 461 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 436 446 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 479 514 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 483 519 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 494 504 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 534 569 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 538 574 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 549 559 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 581 616 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 604 634 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 884 921 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 909 923 {ECO:0000255|PROSITE-ProRule:PRU00210}.
MUTAGEN 323 325 RSQ->AAA: Abolishes processing of
vasculostatin-40.
{ECO:0000269|PubMed:22330140}.
MUTAGEN 326 328 SLR->AAA: Does not affect processing of
vasculostatin-40.
{ECO:0000269|PubMed:22330140}.
MUTAGEN 927 927 S->A: Abolishes cleavage and production
of vasculostatin-120.
{ECO:0000269|PubMed:15782143}.
MUTAGEN 927 927 S->D: Increased levels of vasculostatin-
120 and decreased levels of
vasculostatin-40.
{ECO:0000269|PubMed:22330140}.
CONFLICT 1010 1010 V -> M (in Ref. 1; BAA23647).
{ECO:0000305}.
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


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