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Adhesion G-protein coupled receptor G1 (G-protein coupled receptor 56) (Protein TM7XN1) [Cleaved into: ADGRG1 N-terminal fragment (ADGRG1 NT) (GPR56 N-terminal fragment) (GPR56 NT) (GPR56(N)) (GPR56 extracellular subunit) (GPR56 subunit alpha); ADGRG1 C-terminal fragment (ADGRG1 CT) (GPR56 C-terminal fragment) (GPR56 CT) (GPR56(C)) (GPR56 seven-transmembrane subunit) (GPR56 7TM) (GPR56 subunit beta)]

 AGRG1_HUMAN             Reviewed;         693 AA.
Q9Y653; A6NIT7; A6NJV9; B0M0K4; B4DR54; O95966; Q6ZMP1; Q8NGB3;
Q96HB4;
15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
15-MAR-2004, sequence version 2.
25-OCT-2017, entry version 160.
RecName: Full=Adhesion G-protein coupled receptor G1;
AltName: Full=G-protein coupled receptor 56;
AltName: Full=Protein TM7XN1;
Contains:
RecName: Full=ADGRG1 N-terminal fragment;
Short=ADGRG1 NT;
AltName: Full=GPR56 N-terminal fragment;
Short=GPR56 NT;
Short=GPR56(N);
AltName: Full=GPR56 extracellular subunit;
AltName: Full=GPR56 subunit alpha;
Contains:
RecName: Full=ADGRG1 C-terminal fragment;
Short=ADGRG1 CT;
AltName: Full=GPR56 C-terminal fragment;
Short=GPR56 CT;
Short=GPR56(C);
AltName: Full=GPR56 seven-transmembrane subunit;
Short=GPR56 7TM;
AltName: Full=GPR56 subunit beta;
Flags: Precursor;
Name=ADGRG1 {ECO:0000312|HGNC:HGNC:4512};
Synonyms=GPR56, TM7LN4, TM7XN1; ORFNames=UNQ540/PRO1083;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-281 AND
HIS-306.
PubMed=10049584; DOI=10.1006/geno.1998.5644;
Liu M., Parker R.M.C., Darby K., Eyre H.J., Copeland N.G.,
Crawford J., Gilbert D.J., Sutherland G.R., Jenkins N.A., Herzog H.;
"GPR56, a novel secretin-like human G-protein-coupled receptor gene.";
Genomics 55:296-305(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS ARG-281 AND
HIS-306.
PubMed=10100861; DOI=10.1016/S0014-5793(99)00230-6;
Zendman A.J.W., Cornelissen I.M.H.A., Weidle U.H., Ruiter D.J.,
van Muijen G.N.P.;
"TM7XN1, a novel human EGF-TM7 like protein, detected with mRNA
differential display using human melanoma cell lines with different
metastatic potential.";
FEBS Lett. 446:292-298(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
Kaighin V.A., Martin A.L., Aronstam R.S.;
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND
VARIANTS ARG-281 AND HIS-306.
TISSUE=Prostate;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
"Genome-wide discovery and analysis of human seven transmembrane helix
receptor genes.";
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
HIS-306.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND VARIANT
HIS-306.
TISSUE=Colon carcinoma;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
HIS-306.
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
PROTEIN SEQUENCE OF 26-40.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[13]
INTERACTION WITH CD81; CD9 AND GNA11.
PubMed=15004227; DOI=10.1091/mbc.E03-12-0886;
Little K.D., Hemler M.E., Stipp C.S.;
"Dynamic regulation of a GPCR-tetraspanin-G protein complex on intact
cells: central role of CD81 in facilitating GPR56-Galpha q/11
association.";
Mol. Biol. Cell 15:2375-2387(2004).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[15]
FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH TGM2.
PubMed=16757564; DOI=10.1073/pnas.0602681103;
Xu L., Begum S., Hearn J.D., Hynes R.O.;
"GPR56, an atypical G protein-coupled receptor, binds tissue
transglutaminase, TG2, and inhibits melanoma tumor growth and
metastasis.";
Proc. Natl. Acad. Sci. U.S.A. 103:9023-9028(2006).
[16]
FUNCTION, AND ALTERNATIVE SPLICING (ISOFORMS 3; 4 AND 5).
PubMed=19572147; DOI=10.1007/s00432-009-0635-z;
Kim J.E., Han J.M., Park C.R., Shin K.J., Ahn C., Seong J.Y.,
Hwang J.I.;
"Splicing variants of the orphan G-protein-coupled receptor GPR56
regulate the activity of transcription factors associated with
tumorigenesis.";
J. Cancer Res. Clin. Oncol. 136:47-53(2010).
[17]
FUNCTION (ADGRG1 N-TERMINAL FRAGMENT AND ADGRG1 C-TERMINAL FRAGMENT),
AND INTERACTION WITH TGM2.
PubMed=21724588; DOI=10.1158/0008-5472.CAN-10-4543;
Yang L., Chen G., Mohanty S., Scott G., Fazal F., Rahman A., Begum S.,
Hynes R.O., Xu L.;
"GPR56 Regulates VEGF production and angiogenesis during melanoma
progression.";
Cancer Res. 71:5558-5568(2011).
[18]
SUBUNIT, SUBCELLULAR LOCATION (ADGRG1 N-TERMINAL FRAGMENT),
GLYCOSYLATION, CHARACTERIZATION OF VARIANTS BFPP TRP-38; CYS-88;
SER-91; SER-346; SER-349; TRP-565 AND ARG-640, AND MUTAGENESIS OF
THR-383.
PubMed=21349848; DOI=10.1074/jbc.M110.183830;
Chiang N.Y., Hsiao C.C., Huang Y.S., Chen H.Y., Hsieh I.J.,
Chang G.W., Lin H.H.;
"Disease-associated GPR56 mutations cause bilateral frontoparietal
polymicrogyria via multiple mechanisms.";
J. Biol. Chem. 286:14215-14225(2011).
[19]
FUNCTION, SUBUNIT, ENZYME REGULATION, AND UBIQUITINATION.
PubMed=21708946; DOI=10.1074/jbc.M111.247973;
Paavola K.J., Stephenson J.R., Ritter S.L., Alter S.P., Hall R.A.;
"The N terminus of the adhesion G protein-coupled receptor GPR56
controls receptor signaling activity.";
J. Biol. Chem. 286:28914-28921(2011).
[20]
PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF HIS-381 AND THR-383.
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).
[21]
LIGAND-BINDING, AND CHARACTERIZATION OF VARIANTS BFPP GLN-38; TRP-38;
CYS-88 AND SER-91.
PubMed=22238662; DOI=10.1371/journal.pone.0029818;
Luo R., Jin Z., Deng Y., Strokes N., Piao X.;
"Disease-associated mutations prevent GPR56-collagen III
interaction.";
PLoS ONE 7:E29818-E29818(2012).
[22]
FUNCTION, AND INVOLVEMENT IN BPPR.
PubMed=24531968; DOI=10.1126/science.1244392;
Bae B.I., Tietjen I., Atabay K.D., Evrony G.D., Johnson M.B.,
Asare E., Wang P.P., Murayama A.Y., Im K., Lisgo S.N., Overman L.,
Sestan N., Chang B.S., Barkovich A.J., Grant P.E., Topcu M.,
Politsky J., Okano H., Piao X., Walsh C.A.;
"Evolutionarily dynamic alternative splicing of GPR56 regulates
regional cerebral cortical patterning.";
Science 343:764-768(2014).
[23]
ENZYME REGULATION.
PubMed=25918380; DOI=10.1073/pnas.1421785112;
Stoveken H.M., Hajduczok A.G., Xu L., Tall G.G.;
"Adhesion G protein-coupled receptors are activated by exposure of a
cryptic tethered agonist.";
Proc. Natl. Acad. Sci. U.S.A. 112:6194-6199(2015).
[24]
ENZYME REGULATION, AND MUTAGENESIS OF THR-383.
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).
[25]
HEPARIN-BINDING DOMAINS, AND MUTAGENESIS OF HIS-28; ARG-29 AND ARG-33.
PubMed=27068534; DOI=10.1242/jcs.174458;
Chiang N.Y., Chang G.W., Huang Y.S., Peng Y.M., Hsiao C.C., Kuo M.L.,
Lin H.H.;
"Heparin interacts with adhesion-GPCR GPR56/ADGRG1, reduces receptor
shedding, and promotes cell adhesion and motility.";
J. Cell Sci. 129:2156-2169(2016).
[26]
VARIANTS BFPP TRP-38; CYS-88; SER-91; SER-346 AND TRP-565.
PubMed=15044805; DOI=10.1126/science.1092780;
Piao X., Hill R.S., Bodell A., Chang B.S., Basel-Vanagaite L.,
Straussberg R., Dobyns W.B., Qasrawi B., Winter R.M., Innes A.M.,
Voit T., Ross M.E., Michaud J.L., Descarie J.-C., Barkovich A.J.,
Walsh C.A.;
"G protein-coupled receptor-dependent development of human frontal
cortex.";
Science 303:2033-2036(2004).
[27]
VARIANTS BFPP GLN-38; TRP-38; SER-349; TRP-565 AND ARG-640.
PubMed=16240336; DOI=10.1002/ana.20616;
Piao X., Chang B.S., Bodell A., Woods K., Benzeev B., Topcu M.,
Guerrini R., Goldberg-Stern H., Sztriha L., Dobyns W.B.,
Barkovich A.J., Walsh C.A.;
"Genotype-phenotype analysis of human frontoparietal polymicrogyria
syndromes.";
Ann. Neurol. 58:680-687(2005).
[28]
VARIANT BFPP LYS-496, AND CHARACTERIZATION OF VARIANT BFPP LYS-496.
PubMed=21723461; DOI=10.1016/j.pediatrneurol.2011.02.004;
Luo R., Yang H.M., Jin Z., Halley D.J., Chang B.S., MacPherson L.,
Brueton L., Piao X.;
"A novel GPR56 mutation causes bilateral frontoparietal
polymicrogyria.";
Pediatr. Neurol. 45:49-53(2011).
[29]
CHARACTERIZATION OF VARIANT BFPP ARG-640, LIGAND-BINDING, SUBCELLULAR
LOCATION, AND ENZYME REGULATION.
PubMed=24949629; DOI=10.1371/journal.pone.0100043;
Luo R., Jeong S.J., Yang A., Wen M., Saslowsky D.E., Lencer W.I.,
Arac D., Piao X.;
"Mechanism for adhesion G protein-coupled receptor GPR56-mediated RhoA
activation induced by collagen III stimulation.";
PLoS ONE 9:E100043-E100043(2014).
-!- FUNCTION: Receptor involved in cell adhesion and probably in cell-
cell interactions. Mediates cell matrix adhesion in developing
neurons and hematopoietic stem cells. Receptor for collagen
III/COL3A1 in the developing brain and involved in regulation of
cortical development, specifically in maintenance of the pial
basement membrane integrity and in cortical lamination (By
similarity). Binding to the COL3A1 ligand inhibits neuronal
migration and activates the RhoA pathway by coupling to GNA13 and
possibly GNA12 (PubMed:22238662). Plays a role in the maintenance
of hematopoietic stem cells and/or leukemia stem cells in bone
marrow niche (By similarity). Plays a critical role in cancer
progression by inhibiting VEGFA production threreby inhibiting
angiogenesis through a signaling pathway mediated by PRKCA
(PubMed:16757564, PubMed:21724588). Plays an essential role in
testis development (By similarity). {ECO:0000250|UniProtKB:Q8K209,
ECO:0000269|PubMed:16757564, ECO:0000269|PubMed:19572147,
ECO:0000269|PubMed:21708946, ECO:0000269|PubMed:21724588,
ECO:0000269|PubMed:22238662, ECO:0000269|PubMed:24531968}.
-!- FUNCTION: ADGRG1 N-terminal fragment: Plays a critical role in
cancer progression by activating VEGFA production and angiogenesis
through a signaling pathway mediated by PRKCA (PubMed:21724588).
{ECO:0000269|PubMed:21724588}.
-!- ENZYME REGULATION: ADGRG1 NT is proposed to inhibit receptor
signaling; its interactions with extracellular ligands and /or
homophilic ADGRG1NT interactions may relieve the inhibition
(PubMed:21708946, PubMed:24949629, PubMed:25918380). Following
ligand binding to the N-terminal fragment, the N-terminal fragment
is released from the seven-transmembrane C-terminal fragment to
unveil a new N-terminal stalk, which then stimulates G-protein-
dependent signaling activity (PubMed:25918380). The N-terminal
stalk has also been shown to be dispensable for at least some G-
protein-dependent signaling (PubMed:26710850).
{ECO:0000269|PubMed:21708946, ECO:0000269|PubMed:24949629,
ECO:0000269|PubMed:25918380, ECO:0000269|PubMed:26710850}.
-!- SUBUNIT: Heterodimer of 2 chains generated by proteolytic
processing; the large extracellular N-terminal fragment (ADGRG1
NT) and the membrane-bound C-terminal fragment (ADGRG1-CT)
predominantly remain associated and non-covalently linked. ADGRG1
NT self-associates in a trans-trans manner; the homophilic
interaction enhances receptor signaling. ADGRG1-CT interacts with
ARRB2; the interaction is impaired by ADGRG1 NT. Interacts with
TGM2; TGM2 probably is not a ADGRG1 ligand and the interaction is
reported controversial (PubMed:16757564, PubMed:21349848). Part of
a GPCR-tetraspanin complex at least consisting of ADGRG1, CD81,
eventually CD9, and GNA11 in which CD81 is enhancing the
association of ADGRG1 with GNA11. Interacts with heparin; leading
to the reduction of ADGRG1 shedding (PubMed:27068534).
{ECO:0000269|PubMed:15004227, ECO:0000269|PubMed:16757564,
ECO:0000269|PubMed:21349848, ECO:0000269|PubMed:21708946,
ECO:0000269|PubMed:21724588, ECO:0000269|PubMed:27068534}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21349848,
ECO:0000269|PubMed:24949629}; Multi-pass membrane protein
{ECO:0000255}.
-!- SUBCELLULAR LOCATION: ADGRG1 N-terminal fragment: Secreted
{ECO:0000269|PubMed:21349848}.
-!- SUBCELLULAR LOCATION: ADGRG1 C-terminal fragment: Membrane raft
{ECO:0000269|PubMed:24949629}. Note=Interaction with its ligand
COL3A1 leads to the release of ADGRG1 NT from the membrane and
triggers the association of ADGRG1 CT with lipid rafts.
{ECO:0000269|PubMed:24949629}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q9Y653-1; Sequence=Displayed;
Name=2; Synonyms=S1;
IsoId=Q9Y653-2; Sequence=VSP_035068;
Name=3; Synonyms=S2;
IsoId=Q9Y653-3; Sequence=VSP_047555, VSP_035068;
Name=4; Synonyms=S3;
IsoId=Q9Y653-4; Sequence=VSP_047556;
Name=5; Synonyms=S4;
IsoId=Q9Y653-5; Sequence=VSP_047554;
Note=Has no predictable signal peptide.;
-!- TISSUE SPECIFICITY: Widely distributed with highest levels found
in thyroid gland, brain and heart. Expressed in a great number of
tumor cells. Expression is down-regulated in different tumors from
highly metastatic cells. {ECO:0000269|PubMed:16757564}.
-!- PTM: Autoproteolytically cleaved into 2 fragments; the large
extracellular N-terminal fragment (ADGRG1 NT) and the membrane-
bound C-terminal fragment (ADGRG1 CT) predominantly remain
associated and non-covalently linked. Shedding to yield the
secreted ADGRG1 N-terminal fragment seems to involve
metalloprotease(s) (PubMed:22333914).
{ECO:0000269|PubMed:22333914}.
-!- PTM: N-glycosylated. Contains sialic acid residues.
{ECO:0000269|PubMed:21349848}.
-!- PTM: Ubiquitinated. Undergoes polyubiquitination upon activation.
{ECO:0000269|PubMed:21708946}.
-!- DISEASE: Polymicrogyria, bilateral frontoparietal (BFPP)
[MIM:606854]: A malformation of the cortex in which the brain
surface is irregular and characterized by an excessive number of
small gyri with abnormal lamination, most severe in the
frontoparietal regions. BFPP clinical manifestations include
developmental and psychomotor delay, cerebellar and pyramidal
signs, truncal ataxia, seizures, hyperreflexia. Polymicrogyria is
a heterogeneous disorder, considered to be the result of
postmigratory abnormal cortical organization.
{ECO:0000269|PubMed:15044805, ECO:0000269|PubMed:16240336,
ECO:0000269|PubMed:21349848, ECO:0000269|PubMed:21723461,
ECO:0000269|PubMed:22238662, ECO:0000269|PubMed:24949629}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Polymicrogyria, bilateral perisylvian, autosomal
recessive (BPPR) [MIM:615752]: A form of polymicrogyria, a
malformation of the cortex in which the brain surface is irregular
and characterized by an excessive number of small gyri with
abnormal lamination. BPPR is characterized by strikingly
restricted polymicrogyria limited to the cortex surrounding the
Sylvian fissure. Affected individuals have intellectual and
language difficulty and seizures, but no motor disability.
Polymicrogyria is a heterogeneous disorder, considered to be the
result of post-migratory abnormal cortical organization.
{ECO:0000269|PubMed:24531968}. Note=The disease is caused by
mutations affecting the gene represented in this entry. Homozygous
deletion of 1 of 2 tandem 15-bp repeats located 144 bp upstream of
the ADGRG1 non-coding exon 1m transcription start site, results in
impaired perisylvian ADGRG1 expression and disruption of
perisylvian gyri (PubMed:24531968). {ECO:0000269|PubMed:24531968}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
LN-TM7 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF106858; AAD30545.1; -; mRNA.
EMBL; AJ011001; CAB37294.1; -; mRNA.
EMBL; EU432119; ABY87918.1; -; mRNA.
EMBL; AY358400; AAQ88766.1; -; mRNA.
EMBL; AK131550; BAD18684.1; -; mRNA.
EMBL; AK299110; BAG61166.1; -; mRNA.
EMBL; AB065909; BAC06124.1; -; Genomic_DNA.
EMBL; BT007311; AAP35975.1; -; mRNA.
EMBL; CR936747; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC018552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471092; EAW82939.1; -; Genomic_DNA.
EMBL; CH471092; EAW82940.1; -; Genomic_DNA.
EMBL; BC008770; AAH08770.1; -; mRNA.
CCDS; CCDS32460.1; -. [Q9Y653-1]
CCDS; CCDS32461.1; -. [Q9Y653-2]
CCDS; CCDS73893.1; -. [Q9Y653-3]
RefSeq; NP_001139242.1; NM_001145770.2. [Q9Y653-2]
RefSeq; NP_001139243.1; NM_001145771.2. [Q9Y653-1]
RefSeq; NP_001139244.1; NM_001145772.2. [Q9Y653-2]
RefSeq; NP_001139245.1; NM_001145773.2. [Q9Y653-3]
RefSeq; NP_001139246.1; NM_001145774.2. [Q9Y653-2]
RefSeq; NP_001277071.1; NM_001290142.1. [Q9Y653-4]
RefSeq; NP_001277072.1; NM_001290143.1. [Q9Y653-5]
RefSeq; NP_005673.3; NM_005682.6. [Q9Y653-1]
RefSeq; NP_958932.1; NM_201524.3. [Q9Y653-2]
RefSeq; NP_958933.1; NM_201525.3. [Q9Y653-2]
RefSeq; XP_005256303.1; XM_005256246.2. [Q9Y653-1]
RefSeq; XP_005256304.1; XM_005256247.2. [Q9Y653-1]
RefSeq; XP_005256305.1; XM_005256248.2. [Q9Y653-1]
RefSeq; XP_005256306.1; XM_005256249.3. [Q9Y653-1]
RefSeq; XP_005256308.1; XM_005256251.4. [Q9Y653-1]
RefSeq; XP_005256309.1; XM_005256252.2. [Q9Y653-1]
RefSeq; XP_005256311.1; XM_005256254.2. [Q9Y653-1]
RefSeq; XP_005256312.1; XM_005256255.2. [Q9Y653-2]
RefSeq; XP_006721405.1; XM_006721342.2. [Q9Y653-1]
RefSeq; XP_006721406.1; XM_006721343.3. [Q9Y653-1]
RefSeq; XP_006721407.1; XM_006721344.2. [Q9Y653-1]
RefSeq; XP_006721408.1; XM_006721345.3. [Q9Y653-1]
RefSeq; XP_006721409.1; XM_006721346.2. [Q9Y653-1]
RefSeq; XP_006721410.1; XM_006721347.2. [Q9Y653-3]
RefSeq; XP_011521765.1; XM_011523463.2. [Q9Y653-1]
RefSeq; XP_011521766.1; XM_011523464.2. [Q9Y653-1]
RefSeq; XP_011521767.1; XM_011523465.2. [Q9Y653-1]
RefSeq; XP_011521768.1; XM_011523466.2. [Q9Y653-1]
RefSeq; XP_011521769.1; XM_011523467.2. [Q9Y653-1]
RefSeq; XP_011521770.1; XM_011523468.2. [Q9Y653-1]
RefSeq; XP_016879381.1; XM_017023892.1. [Q9Y653-2]
UniGene; Hs.513633; -.
ProteinModelPortal; Q9Y653; -.
SMR; Q9Y653; -.
BioGrid; 114704; 3.
CORUM; Q9Y653; -.
IntAct; Q9Y653; 3.
STRING; 9606.ENSP00000369018; -.
MEROPS; P02.008; -.
iPTMnet; Q9Y653; -.
PhosphoSitePlus; Q9Y653; -.
BioMuta; GPR56; -.
DMDM; 45476992; -.
EPD; Q9Y653; -.
PaxDb; Q9Y653; -.
PeptideAtlas; Q9Y653; -.
PRIDE; Q9Y653; -.
DNASU; 9289; -.
Ensembl; ENST00000388813; ENSP00000373465; ENSG00000205336. [Q9Y653-2]
Ensembl; ENST00000456916; ENSP00000398034; ENSG00000205336. [Q9Y653-3]
Ensembl; ENST00000540164; ENSP00000444911; ENSG00000205336. [Q9Y653-2]
Ensembl; ENST00000562558; ENSP00000456620; ENSG00000205336. [Q9Y653-2]
Ensembl; ENST00000562631; ENSP00000455351; ENSG00000205336. [Q9Y653-2]
Ensembl; ENST00000567835; ENSP00000456794; ENSG00000205336. [Q9Y653-1]
Ensembl; ENST00000568908; ENSP00000457456; ENSG00000205336. [Q9Y653-2]
Ensembl; ENST00000568909; ENSP00000455215; ENSG00000205336. [Q9Y653-1]
GeneID; 9289; -.
KEGG; hsa:9289; -.
UCSC; uc002emb.3; human. [Q9Y653-1]
CTD; 9289; -.
DisGeNET; 9289; -.
EuPathDB; HostDB:ENSG00000205336.11; -.
GeneCards; ADGRG1; -.
GeneReviews; GPR56; -.
HGNC; HGNC:4512; ADGRG1.
HPA; HPA046065; -.
MalaCards; ADGRG1; -.
MIM; 604110; gene.
MIM; 606854; phenotype.
MIM; 615752; phenotype.
neXtProt; NX_Q9Y653; -.
OpenTargets; ENSG00000205336; -.
Orphanet; 101070; Bilateral frontoparietal polymicrogyria.
Orphanet; 98889; Bilateral perisylvian polymicrogyria.
PharmGKB; PA28901; -.
eggNOG; KOG4193; Eukaryota.
eggNOG; ENOG410XSD2; LUCA.
GeneTree; ENSGT00900000140853; -.
HOGENOM; HOG000015136; -.
HOVERGEN; HBG051814; -.
InParanoid; Q9Y653; -.
KO; K08450; -.
OMA; SMCWIRD; -.
OrthoDB; EOG091G02U6; -.
PhylomeDB; Q9Y653; -.
TreeFam; TF321769; -.
SIGNOR; Q9Y653; -.
ChiTaRS; GPR56; human.
GenomeRNAi; 9289; -.
PRO; PR:Q9Y653; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000205336; -.
CleanEx; HS_GPR56; -.
ExpressionAtlas; Q9Y653; baseline and differential.
Genevisible; Q9Y653; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0097451; C:glial limiting end-foot; 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:0005622; C:intracellular; IEA:GOC.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005518; F:collagen binding; ISS:UniProtKB.
GO; GO:0050840; F:extracellular matrix binding; ISS:UniProtKB.
GO; GO:0004930; F:G-protein coupled receptor activity; ISS:UniProtKB.
GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
GO; GO:0001525; P:angiogenesis; IDA:UniProtKB.
GO; GO:0007420; P:brain development; IMP:GDB.
GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
GO; GO:0016477; P:cell migration; IDA:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0021801; P:cerebral cortex radial glia guided migration; ISS:UniProtKB.
GO; GO:0021796; P:cerebral cortex regionalization; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc.
GO; GO:0021819; P:layer formation in cerebral cortex; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:2001223; P:negative regulation of neuron migration; ISS:UniProtKB.
GO; GO:0045785; P:positive regulation of cell adhesion; IDA:UniProtKB.
GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IEA:Ensembl.
GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISS:UniProtKB.
GO; GO:0070528; P:protein kinase C signaling; IDA:UniProtKB.
GO; GO:0007266; P:Rho protein signal transduction; IDA:UniProtKB.
GO; GO:0072520; P:seminiferous tubule development; IEA:Ensembl.
GO; GO:0010573; P:vascular endothelial growth factor production; IDA:UniProtKB.
InterPro; IPR017981; GPCR_2-like.
InterPro; IPR000832; GPCR_2_secretin-like.
InterPro; IPR003910; GPR1/GPR3/GPR5.
InterPro; IPR000203; GPS.
Pfam; PF00002; 7tm_2; 1.
Pfam; PF01825; GPS; 1.
PRINTS; PR00249; GPCRSECRETIN.
PRINTS; PR01422; GPR56ORPHANR.
SMART; SM00303; GPS; 1.
PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PROSITE; PS50221; GPS; 1.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell membrane; Complete proteome;
Developmental protein; Differentiation; Direct protein sequencing;
Disease mutation; G-protein coupled receptor; Glycoprotein;
Heparin-binding; Membrane; Neurogenesis; Polymorphism; Receptor;
Reference proteome; Secreted; Signal; Transducer; Transmembrane;
Transmembrane helix; Ubl conjugation.
SIGNAL 1 25 {ECO:0000269|PubMed:15340161}.
CHAIN 26 693 Adhesion G-protein coupled receptor G1.
/FTId=PRO_0000012880.
CHAIN 26 ?382 ADGRG1 N-terminal fragment.
{ECO:0000305|PubMed:22333914}.
/FTId=PRO_0000423086.
CHAIN ?383 693 ADGRG1 C-terminal fragment.
{ECO:0000305|PubMed:22333914}.
/FTId=PRO_0000423087.
TOPO_DOM 26 402 Extracellular. {ECO:0000255}.
TRANSMEM 403 423 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 424 448 Cytoplasmic. {ECO:0000255}.
TRANSMEM 449 469 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 470 476 Extracellular. {ECO:0000255}.
TRANSMEM 477 497 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 498 518 Cytoplasmic. {ECO:0000255}.
TRANSMEM 519 539 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 540 576 Extracellular. {ECO:0000255}.
TRANSMEM 577 597 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 598 609 Cytoplasmic. {ECO:0000255}.
TRANSMEM 610 630 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 631 636 Extracellular. {ECO:0000255}.
TRANSMEM 637 657 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 658 693 Cytoplasmic. {ECO:0000255}.
DOMAIN 343 394 GPS. {ECO:0000255|PROSITE-
ProRule:PRU00098}.
REGION 26 33 Heparin-binding.
{ECO:0000269|PubMed:27068534}.
REGION 190 200 Heparin-binding.
{ECO:0000269|PubMed:27068534}.
SITE 382 383 Cleavage; by autolysis.
{ECO:0000305|PubMed:22333914}.
CARBOHYD 39 39 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 148 148 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 171 171 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 234 234 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 303 303 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 324 324 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 341 341 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 175 Missing (in isoform 5).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_047554.
VAR_SEQ 21 21 Q -> QASASS (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047555.
VAR_SEQ 38 207 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047556.
VAR_SEQ 429 434 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:10100861,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_035068.
VARIANT 38 38 R -> Q (in BFPP; abolishes interaction
with COL3A1; dbSNP:rs764367185).
{ECO:0000269|PubMed:16240336,
ECO:0000269|PubMed:22238662}.
/FTId=VAR_069581.
VARIANT 38 38 R -> W (in BFPP; abolishes interaction
with COL3A1; reduces cell surface
localization; dbSNP:rs121908462).
{ECO:0000269|PubMed:15044805,
ECO:0000269|PubMed:16240336,
ECO:0000269|PubMed:21349848,
ECO:0000269|PubMed:22238662}.
/FTId=VAR_026242.
VARIANT 88 88 Y -> C (in BFPP; abolishes interaction
with COL3A1; reduces cell surface
localization; dbSNP:rs121908466).
{ECO:0000269|PubMed:15044805,
ECO:0000269|PubMed:21349848,
ECO:0000269|PubMed:22238662}.
/FTId=VAR_026243.
VARIANT 91 91 C -> S (in BFPP; abolishes interaction
with COL3A1; reduces cell surface
localization; dbSNP:rs121908465).
{ECO:0000269|PubMed:15044805,
ECO:0000269|PubMed:21349848,
ECO:0000269|PubMed:22238662}.
/FTId=VAR_026244.
VARIANT 281 281 S -> R (in dbSNP:rs1801257).
{ECO:0000269|PubMed:10049584,
ECO:0000269|PubMed:10100861,
ECO:0000269|PubMed:14702039}.
/FTId=VAR_017910.
VARIANT 306 306 Q -> H (in dbSNP:rs1801255).
{ECO:0000269|PubMed:10049584,
ECO:0000269|PubMed:10100861,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005,
ECO:0000269|Ref.7}.
/FTId=VAR_017911.
VARIANT 346 346 C -> S (in BFPP; abolishes
autoproteolytic cleavage; reduces cell
surface localization; dbSNP:rs121908463).
{ECO:0000269|PubMed:15044805,
ECO:0000269|PubMed:21349848}.
/FTId=VAR_026245.
VARIANT 349 349 W -> S (in BFPP; abolishes
autoproteolytic cleavage; reduces cell
surface localization).
{ECO:0000269|PubMed:16240336,
ECO:0000269|PubMed:21349848}.
/FTId=VAR_069582.
VARIANT 493 493 M -> T (in dbSNP:rs17379472).
/FTId=VAR_049457.
VARIANT 496 496 E -> K (in BFPP; reduces cell surface
localization; dbSNP:rs556518689).
{ECO:0000269|PubMed:21723461}.
/FTId=VAR_069583.
VARIANT 527 527 P -> L (in dbSNP:rs16958679).
/FTId=VAR_049458.
VARIANT 565 565 R -> W (in BFPP; reduces cell surface
localization; dbSNP:rs121908464).
{ECO:0000269|PubMed:15044805,
ECO:0000269|PubMed:16240336,
ECO:0000269|PubMed:21349848}.
/FTId=VAR_026246.
VARIANT 640 640 L -> R (in BFPP; unclear effects on cell
surface localization; blocks downstream
RhoA activation).
{ECO:0000269|PubMed:16240336,
ECO:0000269|PubMed:21349848,
ECO:0000269|PubMed:24949629}.
/FTId=VAR_069584.
MUTAGEN 28 28 H->A: Abolishes heparin-binding; when
associated with A-29 and A-33.
{ECO:0000269|PubMed:27068534}.
MUTAGEN 29 29 R->A: Abolishes heparin-binding; when
associated with A-28 and A-33.
{ECO:0000269|PubMed:27068534}.
MUTAGEN 33 33 R->A: Reduces heparin-binding. Abolishes
heparin-binding; when associated with A-
28 and A-29.
{ECO:0000269|PubMed:27068534}.
MUTAGEN 381 381 H->S: Abolishes cleavage.
{ECO:0000269|PubMed:22333914}.
MUTAGEN 383 383 T->G: Abolishes cleavage but does not
affect cell membrane localization or
signaling activity.
{ECO:0000269|PubMed:21349848,
ECO:0000269|PubMed:22333914,
ECO:0000269|PubMed:26710850}.
CONFLICT 329 329 V -> A (in Ref. 8). {ECO:0000305}.
CONFLICT 561 561 M -> R (in Ref. 5; BAD18684).
{ECO:0000305}.
CONFLICT 678 678 S -> C (in Ref. 1; AAD30545).
{ECO:0000305}.
SEQUENCE 693 AA; 77738 MW; 801C8E62666A5155 CRC64;
MTPQSLLQTT LFLLSLLFLV QGAHGRGHRE DFRFCSQRNQ THRSSLHYKP TPDLRISIEN
SEEALTVHAP FPAAHPASRS FPDPRGLYHF CLYWNRHAGR LHLLYGKRDF LLSDKASSLL
CFQHQEESLA QGPPLLATSV TSWWSPQNIS LPSAASFTFS FHSPPHTAAH NASVDMCELK
RDLQLLSQFL KHPQKASRRP SAAPASQQLQ SLESKLTSVR FMGDMVSFEE DRINATVWKL
QPTAGLQDLH IHSRQEEEQS EIMEYSVLLP RTLFQRTKGR SGEAEKRLLL VDFSSQALFQ
DKNSSQVLGE KVLGIVVQNT KVANLTEPVV LTFQHQLQPK NVTLQCVFWV EDPTLSSPGH
WSSAGCETVR RETQTSCFCN HLTYFAVLMV SSVEVDAVHK HYLSLLSYVG CVVSALACLV
TIAAYLCSRV PLPCRRKPRD YTIKVHMNLL LAVFLLDTSF LLSEPVALTG SEAGCRASAI
FLHFSLLTCL SWMGLEGYNL YRLVVEVFGT YVPGYLLKLS AMGWGFPIFL VTLVALVDVD
NYGPIILAVH RTPEGVIYPS MCWIRDSLVS YITNLGLFSL VFLFNMAMLA TMVVQILRLR
PHTQKWSHVL TLLGLSLVLG LPWALIFFSF ASGTFQLVVL YLFSIITSFQ GFLIFIWYWS
MRLQARGGPS PLKSNSDSAR LPISSGSTSS SRI


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