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

 AGRB1_MOUSE             Reviewed;        1582 AA.
Q3UHD1; Q3UH36; Q8CGM0;
11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
11-OCT-2005, sequence version 1.
22-NOV-2017, entry version 105.
RecName: Full=Adhesion G protein-coupled receptor B1 {ECO:0000312|MGI:MGI:1933736};
AltName: Full=Brain-specific angiogenesis inhibitor 1 {ECO:0000303|PubMed:11245925};
Contains:
RecName: Full=Vasculostatin-120 {ECO:0000250|UniProtKB:O14514};
Short=Vstat120 {ECO:0000250|UniProtKB:O14514};
Contains:
RecName: Full=Vasculostatin-40 {ECO:0000250|UniProtKB:O14514};
Short=Vstat-40 {ECO:0000250|UniProtKB:O14514};
Flags: Precursor;
Name=Adgrb1 {ECO:0000312|MGI:MGI:1933736};
Synonyms=Bai1 {ECO:0000303|PubMed:11245925};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH
PHYHIP.
STRAIN=ICR; TISSUE=Brain;
PubMed=11245925; DOI=10.1016/S0169-328X(01)00004-3;
Koh J.T., Lee Z.H., Ahn K.Y., Kim J.-K., Bae C.S., Kim H.-H.,
Kee H.J., Kim K.K.;
"Characterization of mouse brain-specific angiogenesis inhibitor 1
(BAI1) and phytanoyl-CoA alpha-hydroxylase-associated protein 1, a
novel BAI1-binding protein.";
Brain Res. Mol. Brain Res. 87:223-237(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
PROTEIN SEQUENCE OF 1255-1268, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[4]
FUNCTION.
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).
[5]
FUNCTION, INTERACTION WITH ELMO1 AND DOCK1, SUBCELLULAR LOCATION,
TISSUE SPECIFICITY, DOMAIN, AND MUTAGENESIS OF 1487-ARG--ARG-1489.
PubMed=17960134; DOI=10.1038/nature06329;
Park D., Tosello-Trampont A.-C., Elliott M.R., Lu M., Haney L.B.,
Ma Z., Klibanov A.L., Mandell J.W., Ravichandran K.S.;
"BAI1 is an engulfment receptor for apoptotic cells upstream of the
ELMO/Dock180/Rac module.";
Nature 450:430-434(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1467, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
TISSUE SPECIFICITY.
PubMed=20888903; DOI=10.1016/j.bbi.2010.09.021;
Sokolowski J.D., Nobles S.L., Heffron D.S., Park D.,
Ravichandran K.S., Mandell J.W.;
"Brain-specific angiogenesis inhibitor-1 expression in astrocytes and
neurons: implications for its dual function as an apoptotic engulfment
receptor.";
Brain Behav. Immun. 25:915-921(2011).
[8]
FUNCTION, AND DOMAIN.
PubMed=21245295; DOI=10.1073/pnas.1014775108;
Das S., Owen K.A., Ly K.T., Park D., Black S.G., Wilson J.M.,
Sifri C.D., Ravichandran K.S., Ernst P.B., Casanova J.E.;
"Brain angiogenesis inhibitor 1 (BAI1) is a pattern recognition
receptor that mediates macrophage binding and engulfment of Gram-
negative bacteria.";
Proc. Natl. Acad. Sci. U.S.A. 108:2136-2141(2011).
[9]
SUBCELLULAR LOCATION.
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).
[10]
TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23615608; DOI=10.1038/nature12135;
Hochreiter-Hufford A.E., Lee C.S., Kinchen J.M., Sokolowski J.D.,
Arandjelovic S., Call J.A., Klibanov A.L., Yan Z., Mandell J.W.,
Ravichandran K.S.;
"Phosphatidylserine receptor BAI1 and apoptotic cells as new promoters
of myoblast fusion.";
Nature 497:263-267(2013).
[12]
FUNCTION, INTERACTION WITH MDM2, AND DISRUPTION PHENOTYPE.
PubMed=25751059; DOI=10.1172/JCI74603;
Zhu D., Li C., Swanson A.M., Villalba R.M., Guo J., Zhang Z.,
Matheny S., Murakami T., Stephenson J.R., Daniel S., Fukata M.,
Hall R.A., Olson J.J., Neigh G.N., Smith Y., Rainnie D.G.,
Van Meir E.G.;
"BAI1 regulates spatial learning and synaptic plasticity in the
hippocampus.";
J. Clin. Invest. 125:1497-1508(2015).
[13]
FUNCTION, AND DISRUPTION PHENOTYPE.
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:17960134). Also mediates the
binding and engulfment of Gram-negative bacteria (PubMed:21245295,
PubMed:26838550, PubMed:26838550). Stimulates production of
reactive oxygen species by macrophages in response to Gram-
negative bacteria, resulting in enhanced microbicidal macrophage
activity (By similarity). In the gastric mucosa, required for
recognition and engulfment of apoptotic gastric epithelial cells
(By similarity). Promotes myoblast fusion (PubMed:23615608).
Activates the Rho pathway in a G-protein-dependent manner (By
similarity). Inhibits MDM2-mediated ubiquitination and degradation
of DLG4/PSD95, promoting DLG4 stability and regulating synaptic
plasticity (PubMed:25751059). 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 (By similarity).
{ECO:0000250|UniProtKB:C0HL12, ECO:0000250|UniProtKB:O14514,
ECO:0000269|PubMed:11875720, ECO:0000269|PubMed:17960134,
ECO:0000269|PubMed:21245295, ECO:0000269|PubMed:23615608,
ECO:0000269|PubMed:25751059, ECO:0000269|PubMed:26838550}.
-!- FUNCTION: Vasculostatin-120: Inhibits angiogenesis in a CD36-
dependent manner. {ECO:0000250|UniProtKB:O14514}.
-!- FUNCTION: Vasculostatin-40: Inhibits angiogenesis.
{ECO:0000250|UniProtKB:O14514}.
-!- SUBUNIT: Interacts with ELMO1 and DOCK1 (PubMed:17960134). When
bound to ELMO1 and DOCK1, acts as a module to promote apoptotic
cell engulfment (PubMed:17960134). Interacts with MDM2; the
interaction results in inhibition of MDM2-mediated ubiquitination
and degradation of DLG4/PSD95 (PubMed:25751059). Interacts with
PARD3 and TIAM1; the interaction is required for correct dendritic
localization of PARD3 and TIAM1 and for dendritic spine formation
(By similarity). Interacts with MAGI1, MAGI3 and BAIAP2 (By
similarity). Interacts with PHYHIP (PubMed:11245925). Interacts
with DLG4 (via PDZ domain) (By similarity). Vasculostatin-120:
Interacts with CD36 (By similarity). Vasculostatin-120: Interacts
with ARRB2 (By similarity). {ECO:0000250|UniProtKB:C0HL12,
ECO:0000250|UniProtKB:O14514, ECO:0000269|PubMed:11245925,
ECO:0000269|PubMed:17960134, ECO:0000269|PubMed:25751059}.
-!- INTERACTION:
Q92556-1:ELMO1 (xeno); NbExp=9; IntAct=EBI-911280, EBI-15668002;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17960134,
ECO:0000269|PubMed:20888903}; Multi-pass membrane protein
{ECO:0000255}. Cell projection, phagocytic cup
{ECO:0000269|PubMed:17960134}. Cell junction, focal adhesion
{ECO:0000269|PubMed:20888903}. Cell projection, dendritic spine
{ECO:0000250|UniProtKB:C0HL12}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density
{ECO:0000269|PubMed:23595754, ECO:0000269|PubMed:23782696}.
-!- SUBCELLULAR LOCATION: Vasculostatin-120: Secreted
{ECO:0000250|UniProtKB:O14514}.
-!- SUBCELLULAR LOCATION: Vasculostatin-40: Secreted
{ECO:0000250|UniProtKB:O14514}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q3UHD1-1; Sequence=Displayed;
Name=2;
IsoId=Q3UHD1-2; Sequence=Not described;
Note=Observed very weakly in the kidney, skeletal muscle, skin,
stomach, thymus and brain from embryonic day 18. By neonatal day
1, the expression is targeted only to the brain.;
-!- TISSUE SPECIFICITY: In brain, widespread expression in all
neuropil-rich zones including spinal cord gray matter, cerebellar
molecular layer, cerebral cortex, thalamic nuclei and basal
ganglia with no expression in white matter (at protein level)
(PubMed:20888903). In the cerebellar molecular layer, highly
expressed in interneuron processes whereas Purkinje cells and
their dendrites show weaker expression (at protein level)
(PubMed:20888903). In the olfactory bulb, highly expressed in
glomeruli (at protein level) (PubMed:20888903). In the retina,
highly concentrated in the outer and inner plexiform layers (at
protein level) (PubMed:20888903). Expressed in brain
(PubMed:11245925). Enriched in hippocampus and cortex
(PubMed:23595754). Also detected in other tissues including bone
marrow and spleen (PubMed:17960134). {ECO:0000269|PubMed:11245925,
ECO:0000269|PubMed:17960134, ECO:0000269|PubMed:20888903,
ECO:0000269|PubMed:23595754}.
-!- DOMAIN: The TSP type-1 repeats in the extracellular domain mediate
binding to phosphatidylserine (PubMed:17960134). They are also
required for bacterial recognition and binding to bacterial outer
membrane lipopolysaccharide (PubMed:21245295).
{ECO:0000269|PubMed:17960134, ECO:0000269|PubMed:21245295}.
-!- PTM: Proteolytically cleaved to produce vasculostatin-40 and
vasculostatin-120. 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. {ECO:0000250|UniProtKB:O14514}.
-!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:O14514}.
-!- DISRUPTION PHENOTYPE: Viable and fertile with normal brain anatomy
but mutants display severe deficits in hippocampus-dependent
spatial learning and memory that are accompanied by enhanced long-
term potentiation, impaired long-term depression, a thinning of
the postsynaptic density at hippocampal synapses, reduced protein
levels of Dlg4 and increased Dlg4 polyubiquitination
(PubMed:25751059). Smaller myofibers than wild-type animals and
impaired muscle regeneration after injury (PubMed:23615608).
Impaired bacterial clearance following E.coli infection
(PubMed:26838550). RNAi-mediated knockdown in embryos results in
greatly reduced dendritic spine density and small but significant
increases in spine length and decreases in spine diameter
(PubMed:23595754). {ECO:0000269|PubMed:23595754,
ECO:0000269|PubMed:23615608, ECO:0000269|PubMed:25751059,
ECO:0000269|PubMed:26838550}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
LN-TM7 subfamily. {ECO:0000305}.
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EMBL; AY168408; AAN86966.1; -; mRNA.
EMBL; AK147494; BAE27949.1; -; mRNA.
EMBL; AK147456; BAE27923.1; -; mRNA.
EMBL; AK147459; BAE27926.1; -; mRNA.
EMBL; AK147607; BAE28021.1; -; mRNA.
CCDS; CCDS70635.1; -. [Q3UHD1-1]
RefSeq; NP_778156.2; NM_174991.3. [Q3UHD1-1]
UniGene; Mm.43133; -.
ProteinModelPortal; Q3UHD1; -.
SMR; Q3UHD1; -.
BioGrid; 223612; 3.
DIP; DIP-37711N; -.
IntAct; Q3UHD1; 4.
STRING; 10090.ENSMUSP00000046097; -.
iPTMnet; Q3UHD1; -.
PhosphoSitePlus; Q3UHD1; -.
PaxDb; Q3UHD1; -.
PeptideAtlas; Q3UHD1; -.
PRIDE; Q3UHD1; -.
Ensembl; ENSMUST00000042035; ENSMUSP00000046097; ENSMUSG00000034730. [Q3UHD1-1]
GeneID; 107831; -.
KEGG; mmu:107831; -.
UCSC; uc007wco.1; mouse. [Q3UHD1-1]
CTD; 575; -.
MGI; MGI:1933736; Adgrb1.
eggNOG; ENOG410IEA0; Eukaryota.
eggNOG; ENOG4111FBM; LUCA.
GeneTree; ENSGT00900000140832; -.
HOGENOM; HOG000230916; -.
HOVERGEN; HBG004813; -.
InParanoid; Q3UHD1; -.
KO; K04596; -.
OMA; SWRGCRT; -.
OrthoDB; EOG091G00C7; -.
PhylomeDB; Q3UHD1; -.
TreeFam; TF331634; -.
PRO; PR:Q3UHD1; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000034730; -.
CleanEx; MM_BAI1; -.
ExpressionAtlas; Q3UHD1; baseline and differential.
Genevisible; Q3UHD1; MM.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0001891; C:phagocytic cup; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0004930; F:G-protein coupled receptor activity; ISS:UniProtKB.
GO; GO:0001530; F:lipopolysaccharide binding; IDA:UniProtKB.
GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB.
GO; GO:0004872; F:receptor activity; IDA:UniProtKB.
GO; GO:0043277; P:apoptotic cell clearance; ISO:MGI.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
GO; GO:0043652; P:engulfment of apoptotic cell; IDA:UniProtKB.
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; ISS:UniProtKB.
GO; GO:0010596; P:negative regulation of endothelial cell migration; ISS:UniProtKB.
GO; GO:0042177; P:negative regulation of protein catabolic process; IMP:UniProtKB.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:UniProtKB.
GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
GO; GO:0006911; P:phagocytosis, engulfment; IMP:UniProtKB.
GO; GO:0006910; P:phagocytosis, recognition; IMP:UniProtKB.
GO; GO:1901741; P:positive regulation of myoblast fusion; IMP:UniProtKB.
GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; ISS:UniProtKB.
GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
GO; GO:0048167; P:regulation of synaptic plasticity; IMP:UniProtKB.
Gene3D; 2.20.100.10; -; 5.
InterPro; IPR032471; GAIN_dom_N.
InterPro; IPR017981; GPCR_2-like.
InterPro; IPR008077; GPCR_2_brain_angio_inhib.
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;
Alternative splicing; Cell junction; Cell membrane; Cell projection;
Complete proteome; Direct protein sequencing; 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 33 {ECO:0000255}.
CHAIN 34 1582 Adhesion G protein-coupled receptor B1.
/FTId=PRO_0000245046.
CHAIN 34 926 Vasculostatin-120.
{ECO:0000250|UniProtKB:O14514}.
/FTId=PRO_0000441807.
CHAIN 34 327 Vasculostatin-40.
{ECO:0000250|UniProtKB:O14514}.
/FTId=PRO_0000441806.
TOPO_DOM 34 948 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 1582 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:0000250|UniProtKB:O14514}.
REGION 1363 1582 Involved in interaction with MAGI1.
{ECO:0000250|UniProtKB:O14514}.
REGION 1579 1582 Indispensable for interaction with MAGI1.
{ECO:0000250|UniProtKB:O14514}.
COMPBIAS 1382 1449 Pro-rich.
SITE 926 927 Cleavage. {ECO:0000250|UniProtKB:O14514}.
MOD_RES 609 609 Phosphothreonine.
{ECO:0000250|UniProtKB:O14514}.
MOD_RES 1467 1467 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
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 1487 1489 RKR->AAA: Reduced binding to ELMO1 and
failure to promote engulfment of
apoptotic thymocytes.
{ECO:0000269|PubMed:17960134}.
CONFLICT 264 264 W -> L (in Ref. 1; AAN86966).
{ECO:0000305}.
CONFLICT 275 286 RDCGGGLQTRTR -> AGLRGRPANSNP (in Ref. 1;
AAN86966). {ECO:0000305}.
CONFLICT 300 300 E -> K (in Ref. 1; AAN86966).
{ECO:0000305}.
CONFLICT 821 821 D -> G (in Ref. 2; BAE28021).
{ECO:0000305}.
SEQUENCE 1582 AA; 173297 MW; 6D1AA6D46E2E223B CRC64;
MRGQAAAPGP IWILAPLLLL LLLLGRWARA ASGADIGPGT EQCTTLVQGK FFGYFSAAAV
FPANASRCSW TLRNPDPRRY TLYMKVAKAP APCSGPGRVR TYQFDSFLES TRTYLGVESF
DEVLRLCDSS APLAFLQASK QFLQMQRQQP PQDGDLGPQG EFPSSSDDFS VEYLVVGNRN
PSHAACQMLC RWLDACLAGS RSSHPCGIMQ TPCACLGGDV GDPASSPLVP RGDVCLRDGV
AGGPENCLTS LTQDRGGHGS AGGWKLWSLW GECTRDCGGG LQTRTRTCLP TLGVEGGGCE
GVLEEGRLCN RKACGPTGRS SSRSQSLRST DARRREEFGD ELQQFGFPSP QTGDPAAEEW
SPWSVCSSTC GEGWQTRTRF CVSSSYSTQC SGPLREQRLC NNSAVCPVHG AWDEWSPWSL
CSSTCGRGFR DRTRTCRPPQ FGGNPCEGPE KQTKFCNIAL CPGRAVDGNW NEWSSWSTCS
ASCSQGRQQR TRECNGPSYG GAECQGHWVE TRDCFLQQCP VDGKWQAWAS WGSCSVTCGG
GSQRRERVCS GPFFGGAACQ GPQDEYRQCG AQRCPEPHEI CDEDNFGAVV WKETPAGEVA
AVRCPRNATG LILRRCELDE EGIAFWEPPT YIRCVSIDYR NIQMMTREHL AKAQRGLPGE
GVSEVIQTLL EISQDGTSYS GDLLSTIDVL RNMTEIFRRA YYSPTPGDVQ NFVQIISNLL
AEENRDKWEE AQLMGPNAKE LFRLVEDFVD VIGFRMKDLR DAYQVTDNLV LSIHKLPASG
ATDISFPMKG WRATGDWAKV PEDRVTVSKS VFSTGLAEAD DSSVFVVGTV LYRNLGSFLA
LQRNTTVLNS KVISVTVKPP PRSLLTPLEI EFAHMYNGTT NQTCILWDET DGPSSSAPPQ
LGPWSWRGCR TVPLDALRTR CLCDRLSTFA ILAQLSADAT MDKVTVPSVT LIVGCGVSSL
TLLMLVIIYV SVWRYIRSER SVILINFCLS IISSNALILI GQTQTRNKVV CTLVAAFLHF
FFLSSFCWVL TEAWQSYMAV TGRLRSRLVR KRFLCLGWGL PALVVAISVG FTKAKGYSTM
NYCWLSLEGG LLYAFVGPAA AVVLVNMVIG ILVFNKLVSK DGITDKKLKE RAGASLWSSC
VVLPLLALTW MSAVLAVTDR RSALFQILFA VFDSLEGFVI VMVHCILRRE VQDAVKCRVV
DRQEEGNGDS GGSFQNGHAQ LMTDFEKDVD LACRSVLNKD IAACRTATIT GTFKRPSLPE
EEKMKLAKGP PPTFNSLPAN VSKLHLHGSP RYPGGPLPDF PNHSLTLKKD KAPKSSFIGD
GDIFKKLDSE LSRAQEKALD TSYVILPTAT ATLRPKPKEE PKYSINIDQM PQTRLIHLSM
APDASFPTRS PPAREPPGGA PPEVPPVQPP PPPPPPPPPP QQPIPPPPTL EPAPPSLGDT
GEPAAHPGPS SGAGAKNENV ATLSVSSLER RKSRYAELDF EKIMHTRKRH QDMFQDLNRK
LQHAAEKEKE VPGADSKPEK QQTPNKRAWE SLRKPHGTPA WVKKELEPLP PSPLELRSVE
WEKAGATIPL VGQDIIDLQT EV


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