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Inositol 1,4,5-trisphosphate receptor type 1 (IP3 receptor isoform 1) (IP3R 1) (InsP3R1) (Inositol 1,4,5-trisphosphate-binding protein P400) (Protein PCD-6) (Purkinje cell protein 1) (Type 1 inositol 1,4,5-trisphosphate receptor) (Type 1 InsP3 receptor)

 ITPR1_MOUSE             Reviewed;        2749 AA.
P11881; P20943; Q99LG5;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 2.
22-NOV-2017, entry version 202.
RecName: Full=Inositol 1,4,5-trisphosphate receptor type 1;
AltName: Full=IP3 receptor isoform 1;
Short=IP3R 1;
Short=InsP3R1;
AltName: Full=Inositol 1,4,5-trisphosphate-binding protein P400;
AltName: Full=Protein PCD-6;
AltName: Full=Purkinje cell protein 1;
AltName: Full=Type 1 inositol 1,4,5-trisphosphate receptor;
Short=Type 1 InsP3 receptor;
Name=Itpr1; Synonyms=Insp3r, Pcd6, Pcp1;
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] (ISOFORM 1), FUNCTION, AND SUBCELLULAR
LOCATION.
TISSUE=Purkinje cell;
PubMed=2554142; DOI=10.1038/342032a0;
Furuichi T., Yoshikawa S., Miyawaki A., Wada K., Maeda N.,
Mikoshiba K.;
"Primary structure and functional expression of the inositol 1,4,5-
trisphosphate-binding protein P400.";
Nature 342:32-38(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=ICR; TISSUE=Cerebellum;
PubMed=2762133; DOI=10.1093/nar/17.13.5385;
Furuichi T., Yoshikawa S., Mikoshiba K.;
"Nucleotide sequence of cDNA encoding P400 protein in the mouse
cerebellum.";
Nucleic Acids Res. 17:5385-5386(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 318-332 AND 1692-1731, AND
ALTERNATIVE SPLICING.
STRAIN=ICR;
PubMed=1648733; DOI=10.1073/pnas.88.14.6244;
Nakagawa T., Okano H., Furuichi T., Aruga J., Mikoshiba K.;
"The subtypes of the mouse inositol 1,4,5-trisphosphate receptor are
expressed in a tissue-specific and developmentally specific manner.";
Proc. Natl. Acad. Sci. U.S.A. 88:6244-6248(1991).
[5]
PROTEIN SEQUENCE OF 862-871, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2098-2749.
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 2250-2749.
STRAIN=C57BL/6J; TISSUE=Cerebellum;
PubMed=3199205;
Nordquist D.T., Kozak C.A., Orr H.T.;
"cDNA cloning and characterization of three genes uniquely expressed
in cerebellum by Purkinje neurons.";
J. Neurosci. 8:4780-4789(1988).
[8]
INTERACTION WITH AHCYL1.
PubMed=12525476; DOI=10.1074/jbc.M210119200;
Ando H., Mizutani A., Matsu-ura T., Mikoshiba K.;
"IRBIT, a novel inositol 1,4,5-trisphosphate (IP3) receptor-binding
protein, is released from the IP3 receptor upon IP3 binding to the
receptor.";
J. Biol. Chem. 278:10602-10612(2003).
[9]
INTERACTION WITH ERP44, AND MUTAGENESIS OF CYS-2496; CYS-2504 AND
CYS-2527.
PubMed=15652484; DOI=10.1016/j.cell.2004.11.048;
Higo T., Hattori M., Nakamura T., Natsume T., Michikawa T.,
Mikoshiba K.;
"Subtype-specific and ER lumenal environment-dependent regulation of
inositol 1,4,5-trisphosphate receptor type 1 by ERp44.";
Cell 120:85-98(2005).
[10]
INTERACTION WITH AHCYL1.
PubMed=16527252; DOI=10.1016/j.bbrc.2006.02.119;
Devogelaere B., Nadif Kasri N., Derua R., Waelkens E., Callewaert G.,
Missiaen L., Parys J.B., De Smedt H.;
"Binding of IRBIT to the IP3 receptor: determinants and functional
effects.";
Biochem. Biophys. Res. Commun. 343:49-56(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1588, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
"Mitochondrial phosphoproteome revealed by an improved IMAC method and
MS/MS/MS.";
Mol. Cell. Proteomics 6:669-676(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1588, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18630941; DOI=10.1021/pr800223m;
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
"Specific phosphopeptide enrichment with immobilized titanium ion
affinity chromatography adsorbent for phosphoproteome analysis.";
J. Proteome Res. 7:3957-3967(2008).
[13]
FUNCTION.
PubMed=19752026; DOI=10.1083/jcb.200904060;
Li G., Mongillo M., Chin K.T., Harding H., Ron D., Marks A.R.,
Tabas I.;
"Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-
triphosphate receptor activity in endoplasmic reticulum stress-induced
apoptosis.";
J. Cell Biol. 186:783-792(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1588, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
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).
[15]
FUNCTION, AND MUTAGENESIS OF TYR-167 AND LYS-168.
PubMed=20813840; DOI=10.1074/jbc.M110.140129;
Yamazaki H., Chan J., Ikura M., Michikawa T., Mikoshiba K.;
"Tyr-167/Trp-168 in type 1/3 inositol 1,4,5-trisphosphate receptor
mediates functional coupling between ligand binding and channel
opening.";
J. Biol. Chem. 285:36081-36091(2010).
[16]
INTERACTION WITH TESPA1.
PubMed=23650607; DOI=10.1016/j.fob.2012.08.005;
Matsuzaki H., Fujimoto T., Ota T., Ogawa M., Tsunoda T., Doi K.,
Hamabashiri M., Tanaka M., Shirasawa S.;
"Tespa1 is a novel inositol 1,4,5-trisphosphate receptor binding
protein in T and B lymphocytes.";
FEBS Open Bio 2:255-259(2012).
[17]
INTERACTION WITH MRVI1.
PubMed=16990611; DOI=10.1182/blood-2005-10-026294;
Antl M., von Bruehl M.-L., Eiglsperger C., Werner M., Konrad I.,
Kocher T., Wilm M., Hofmann F., Massberg S., Schlossmann J.;
"IRAG mediates NO/cGMP-dependent inhibition of platelet aggregation
and thrombus formation.";
Blood 109:552-559(2007).
[18]
INTERACTION WITH AHCYL1, MUTAGENESIS OF SER-1588 AND SER-1755,
PHOSPHORYLATION, AND FUNCTION.
PubMed=23542070; DOI=10.1053/j.gastro.2013.03.047;
Park S., Shcheynikov N., Hong J.H., Zheng C., Suh S.H., Kawaai K.,
Ando H., Mizutani A., Abe T., Kiyonari H., Seki G., Yule D.,
Mikoshiba K., Muallem S.;
"Irbit mediates synergy between ca(2+) and cAMP signaling pathways
during epithelial transport in mice.";
Gastroenterology 145:232-241(2013).
[19]
INTERACTION WITH BOK.
PubMed=23884412; DOI=10.1074/jbc.M113.496570;
Schulman J.J., Wright F.A., Kaufmann T., Wojcikiewicz R.J.;
"The Bcl-2 protein family member Bok binds to the coupling domain of
inositol 1,4,5-trisphosphate receptors and protects them from
proteolytic cleavage.";
J. Biol. Chem. 288:25340-25349(2013).
[20]
PALMITOYLATION AT CYS-56 AND CYS-849, AND MUTAGENESIS OF CYS-56;
CYS-849 AND CYS-2215.
PubMed=25368151; DOI=10.1073/pnas.1417176111;
Fredericks G.J., Hoffmann F.W., Rose A.H., Osterheld H.J., Hess F.M.,
Mercier F., Hoffmann P.R.;
"Stable expression and function of the inositol 1,4,5-triphosphate
receptor requires palmitoylation by a DHHC6/selenoprotein K complex.";
Proc. Natl. Acad. Sci. U.S.A. 111:16478-16483(2014).
[21]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 224-604 IN COMPLEX WITH
INOSITOL 1,4,5-TRISPHOSPHATE, AND MUTAGENESIS OF THR-267 AND TYR-567.
PubMed=12442173; DOI=10.1038/nature01268;
Bosanac I., Alattia J.R., Mal T.K., Chan J., Talarico S., Tong F.K.,
Tong K.I., Yoshikawa F., Furuichi T., Iwai M., Michikawa T.,
Mikoshiba K., Ikura M.;
"Structure of the inositol 1,4,5-trisphosphate receptor binding core
in complex with its ligand.";
Nature 420:696-700(2002).
[22]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-223.
PubMed=15664189; DOI=10.1016/j.molcel.2004.11.047;
Bosanac I., Yamazaki H., Matsu-Ura T., Michikawa T., Mikoshiba K.,
Ikura M.;
"Crystal structure of the ligand binding suppressor domain of type 1
inositol 1,4,5-trisphosphate receptor.";
Mol. Cell 17:193-203(2005).
-!- FUNCTION: Intracellular channel that mediates calcium release from
the endoplasmic reticulum following stimulation by inositol 1,4,5-
trisphosphate. Involved in the regulation of epithelial secretion
of electrolytes and fluid through the interaction with AHCYL1
(PubMed:23542070). Plays a role in ER stress-induced apoptosis.
Cytoplasmic calcium released from the ER triggers apoptosis by the
activation of CaM kinase II, eventually leading to the activation
of downstream apoptosis pathways. {ECO:0000269|PubMed:19752026,
ECO:0000269|PubMed:20813840, ECO:0000269|PubMed:23542070,
ECO:0000269|PubMed:2554142}.
-!- SUBUNIT: Homotetramer. Interacts with TRPC4. The PPXXF motif binds
HOM1, HOM2 and HOM3. Interacts with RYR1, RYR2, ITPR1, SHANK1 and
SHANK3. Part of cGMP kinase signaling complex at least composed of
ACTA2/alpha-actin, CNN1/calponin H1, PLN/phospholamban, PRKG1 and
ITPR1 (By similarity). Interacts with ERP44 in a pH-, redox
state- and calcium-dependent manner which results in the
inhibition the calcium channel activity. The strength of this
interaction inversely correlates with calcium concentration.
Interacts with MRVI1. Interacts with CABP1 (By similarity).
Interacts with TESPA1. Interacts (when not phosphorylated) with
AHCYL1 (when phosphorylated); the interaction suppresses inositol
1,4,5-trisphosphate binding to ITPR1 (PubMed:23542070). Interacts
with AHCYL2 (with lower affinity than with AHCYL1) (By
similarity). Interacts with BOK (via BH4 domain); protects ITPR1
from proteolysis by CASP3 during apoptosis (PubMed:23884412).
{ECO:0000250|UniProtKB:Q14643, ECO:0000269|PubMed:12442173,
ECO:0000269|PubMed:12525476, ECO:0000269|PubMed:15652484,
ECO:0000269|PubMed:16527252, ECO:0000269|PubMed:16990611,
ECO:0000269|PubMed:23542070, ECO:0000269|PubMed:23650607,
ECO:0000269|PubMed:23884412}.
-!- INTERACTION:
Q8VDN2:Atp1a1; NbExp=3; IntAct=EBI-541478, EBI-444536;
Q6PIE5:Atp1a2; NbExp=3; IntAct=EBI-541478, EBI-6665421;
P10415:BCL2 (xeno); NbExp=3; IntAct=EBI-541478, EBI-77694;
Q9D1Q6:Erp44; NbExp=5; IntAct=EBI-541478, EBI-541567;
O35157:Slc8a1; NbExp=4; IntAct=EBI-541478, EBI-8351080;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000305|PubMed:25368151}; Multi-pass membrane protein
{ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane
{ECO:0000250|UniProtKB:Q9TU34}; Multi-pass membrane protein
{ECO:0000255}. Cytoplasm, perinuclear region
{ECO:0000250|UniProtKB:Q14643}. Note=Endoplasmic reticulum and
secretory granules (By similarity).
{ECO:0000250|UniProtKB:Q9TU34}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Comment=There is a combination of two alternatively spliced
domains at site SI and site SII (A, B and C). Experimental
confirmation may be lacking for some isoforms.;
Name=1; Synonyms=SISIIABC;
IsoId=P11881-1; Sequence=Displayed;
Name=2; Synonyms=SI-SIIABC;
IsoId=P11881-2; Sequence=VSP_002691;
Name=3; Synonyms=SISIIAC;
IsoId=P11881-3; Sequence=VSP_002693;
Name=4; Synonyms=SI-SIIAC;
IsoId=P11881-4; Sequence=VSP_002691, VSP_002693;
Name=5; Synonyms=SISIIA;
IsoId=P11881-5; Sequence=VSP_002693, VSP_002694;
Name=6; Synonyms=SI-SIIA;
IsoId=P11881-6; Sequence=VSP_002691, VSP_002693, VSP_002694;
Name=7; Synonyms=SISII;
IsoId=P11881-7; Sequence=VSP_002692, VSP_002693, VSP_002694;
Name=8; Synonyms=SI-SII;
IsoId=P11881-8; Sequence=VSP_002691, VSP_002692, VSP_002693,
VSP_002694;
-!- DOMAIN: The receptor contains a calcium channel in its C-terminal
extremity. Its large N-terminal cytoplasmic region has the ligand-
binding site in the N-terminus and modulatory sites in the middle
portion immediately upstream of the channel region.
-!- PTM: Phosphorylated by cAMP kinase (PKA). Phosphorylation prevents
the ligand-induced opening of the calcium channels.
Phosphorylation by PKA increases the interaction with inositol
1,4,5-trisphosphate and decreases the interaction with AHCYL1.
{ECO:0000305|PubMed:23542070}.
-!- PTM: Phosphorylated on tyrosine residues.
{ECO:0000250|UniProtKB:Q14643}.
-!- PTM: Ubiquitination at multiple lysines targets ITPR1 for
proteasomal degradation. Approximately 40% of the ITPR1-associated
ubiquitin is monoubiquitin, and polyubiquitins are both 'Lys-
48'- and 'Lys-63'-linked (By similarity).
{ECO:0000250|UniProtKB:P29994}.
-!- PTM: Palmitoylated by ZDHHC6 in immune cells, leading to regulate
ITPR1 stability and function (PubMed:25368151).
{ECO:0000269|PubMed:25368151}.
-!- MISCELLANEOUS: Calcium appears to inhibit ligand binding to the
receptor, most probably by interacting with a distinct calcium-
binding protein which then inhibits the receptor.
-!- SIMILARITY: Belongs to the InsP3 receptor family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA88319.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH03271.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; X15373; CAA33433.1; -; mRNA.
EMBL; AC120411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC153986; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC156506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M75986; AAA39316.1; -; Genomic_DNA.
EMBL; M75987; AAA39317.1; -; Genomic_DNA.
EMBL; BC003271; AAH03271.1; ALT_INIT; mRNA.
EMBL; M21530; AAA88319.1; ALT_INIT; mRNA.
CCDS; CCDS51869.1; -. [P11881-1]
PIR; S04844; ACMSIT.
RefSeq; NP_034715.3; NM_010585.5. [P11881-1]
RefSeq; XP_006505693.1; XM_006505630.1. [P11881-2]
RefSeq; XP_006505699.1; XM_006505636.1. [P11881-7]
RefSeq; XP_006505700.1; XM_006505637.1. [P11881-8]
RefSeq; XP_017176897.1; XM_017321408.1. [P11881-3]
RefSeq; XP_017176899.1; XM_017321410.1. [P11881-4]
UniGene; Mm.227912; -.
PDB; 1N4K; X-ray; 2.20 A; A=224-604.
PDB; 1XZZ; X-ray; 1.80 A; A=2-223.
PDB; 5GUG; X-ray; 7.40 A; A/B=1-2217.
PDB; 5X9Z; X-ray; 7.31 A; A/B=1-2217.
PDB; 5XA0; X-ray; 5.81 A; A/B=1-1581.
PDB; 5XA1; X-ray; 6.20 A; A/B=1-1581.
PDBsum; 1N4K; -.
PDBsum; 1XZZ; -.
PDBsum; 5GUG; -.
PDBsum; 5X9Z; -.
PDBsum; 5XA0; -.
PDBsum; 5XA1; -.
ProteinModelPortal; P11881; -.
SMR; P11881; -.
BioGrid; 200847; 17.
CORUM; P11881; -.
DIP; DIP-32243N; -.
IntAct; P11881; 20.
MINT; MINT-4099099; -.
STRING; 10090.ENSMUSP00000032192; -.
iPTMnet; P11881; -.
PhosphoSitePlus; P11881; -.
MaxQB; P11881; -.
PaxDb; P11881; -.
PeptideAtlas; P11881; -.
PRIDE; P11881; -.
Ensembl; ENSMUST00000032192; ENSMUSP00000032192; ENSMUSG00000030102. [P11881-1]
Ensembl; ENSMUST00000203615; ENSMUSP00000144880; ENSMUSG00000030102. [P11881-3]
GeneID; 16438; -.
KEGG; mmu:16438; -.
UCSC; uc033itt.1; mouse. [P11881-1]
CTD; 3708; -.
MGI; MGI:96623; Itpr1.
eggNOG; KOG3533; Eukaryota.
eggNOG; ENOG410XR97; LUCA.
GeneTree; ENSGT00760000119152; -.
HOGENOM; HOG000007660; -.
HOVERGEN; HBG052158; -.
InParanoid; P11881; -.
KO; K04958; -.
OMA; DPDDHYQ; -.
OrthoDB; EOG091G00T2; -.
PhylomeDB; P11881; -.
TreeFam; TF312815; -.
Reactome; R-MMU-114508; Effects of PIP2 hydrolysis.
Reactome; R-MMU-139853; Elevation of cytosolic Ca2+ levels.
Reactome; R-MMU-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
Reactome; R-MMU-418457; cGMP effects.
Reactome; R-MMU-5578775; Ion homeostasis.
Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
ChiTaRS; Itpr1; mouse.
EvolutionaryTrace; P11881; -.
PRO; PR:P11881; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000030102; -.
CleanEx; MM_ITPR1; -.
ExpressionAtlas; P11881; baseline and differential.
Genevisible; P11881; MM.
GO; GO:0005955; C:calcineurin complex; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; TAS:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005635; C:nuclear envelope; IDA:MGI.
GO; GO:0005637; C:nuclear inner membrane; IDA:MGI.
GO; GO:0005730; C:nucleolus; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0031088; C:platelet dense granule membrane; ISO:MGI.
GO; GO:0031094; C:platelet dense tubular network; ISO:MGI.
GO; GO:0014069; C:postsynaptic density; IDA:MGI.
GO; GO:0043234; C:protein complex; IPI:MGI.
GO; GO:0016529; C:sarcoplasmic reticulum; IDA:MGI.
GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0019855; F:calcium channel inhibitor activity; ISO:MGI.
GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
GO; GO:0015278; F:calcium-release channel activity; IDA:UniProtKB.
GO; GO:0005220; F:inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; IDA:UniProtKB.
GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
GO; GO:0006816; P:calcium ion transport; IDA:MGI.
GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IGI:MGI.
GO; GO:0042045; P:epithelial fluid transport; IDA:UniProtKB.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:UniProtKB.
GO; GO:0050849; P:negative regulation of calcium-mediated signaling; ISO:MGI.
GO; GO:0009791; P:post-embryonic development; IMP:MGI.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:UniProtKB.
GO; GO:0001666; P:response to hypoxia; IDA:BHF-UCL.
GO; GO:0050882; P:voluntary musculoskeletal movement; IMP:MGI.
Gene3D; 1.25.10.30; -; 2.
InterPro; IPR014821; Ins145_P3_rcpt.
InterPro; IPR000493; InsP3_rcpt-bd.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR035910; IP3R_RIH_dom_sf.
InterPro; IPR036300; MIR_dom_sf.
InterPro; IPR016093; MIR_motif.
InterPro; IPR013662; RIH_assoc-dom.
InterPro; IPR000699; RIH_dom.
InterPro; IPR015925; Ryanodine_recept-rel.
PANTHER; PTHR13715; PTHR13715; 1.
Pfam; PF08709; Ins145_P3_rec; 1.
Pfam; PF00520; Ion_trans; 1.
Pfam; PF02815; MIR; 1.
Pfam; PF08454; RIH_assoc; 1.
Pfam; PF01365; RYDR_ITPR; 2.
PRINTS; PR00779; INSP3RECEPTR.
SMART; SM00472; MIR; 4.
SUPFAM; SSF100909; SSF100909; 2.
SUPFAM; SSF82109; SSF82109; 2.
PROSITE; PS50919; MIR; 5.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Calcium;
Calcium channel; Calcium transport; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Direct protein sequencing; Endoplasmic reticulum;
Ion channel; Ion transport; Isopeptide bond; Ligand-gated ion channel;
Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport; Ubl conjugation.
CHAIN 1 2749 Inositol 1,4,5-trisphosphate receptor
type 1.
/FTId=PRO_0000153921.
TOPO_DOM 1 2273 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2274 2294 Helical. {ECO:0000255}.
TOPO_DOM 2295 2305 Lumenal. {ECO:0000255}.
TRANSMEM 2306 2326 Helical. {ECO:0000255}.
TOPO_DOM 2327 2352 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2353 2373 Helical. {ECO:0000255}.
TOPO_DOM 2374 2396 Lumenal. {ECO:0000255}.
TRANSMEM 2397 2417 Helical. {ECO:0000255}.
TOPO_DOM 2418 2439 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2440 2460 Helical. {ECO:0000255}.
TOPO_DOM 2461 2569 Lumenal. {ECO:0000255}.
TRANSMEM 2570 2590 Helical. {ECO:0000255}.
TOPO_DOM 2591 2749 Cytoplasmic. {ECO:0000255}.
DOMAIN 112 166 MIR 1. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
DOMAIN 173 223 MIR 2. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
DOMAIN 231 287 MIR 3. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
DOMAIN 294 373 MIR 4. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
DOMAIN 379 435 MIR 5. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
REGION 265 269 Inositol 1,4,5-trisphosphate binding.
REGION 508 511 Inositol 1,4,5-trisphosphate binding.
REGION 567 569 Inositol 1,4,5-trisphosphate binding.
REGION 2463 2528 Interaction with ERP44.
{ECO:0000269|PubMed:15652484}.
MOD_RES 482 482 Phosphotyrosine. {ECO:0000255}.
MOD_RES 1588 1588 Phosphoserine.
{ECO:0000244|PubMed:17208939,
ECO:0000244|PubMed:18630941,
ECO:0000244|PubMed:21183079}.
MOD_RES 1755 1755 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:Q14643,
ECO:0000255}.
MOD_RES 2655 2655 Phosphotyrosine. {ECO:0000255}.
LIPID 56 56 S-palmitoyl cysteine.
{ECO:0000269|PubMed:25368151}.
LIPID 849 849 S-palmitoyl cysteine.
{ECO:0000269|PubMed:25368151}.
CROSSLNK 916 916 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P29994}.
CROSSLNK 962 962 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P29994}.
CROSSLNK 1571 1571 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P29994}.
CROSSLNK 1771 1771 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P29994}.
CROSSLNK 1884 1884 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P29994}.
CROSSLNK 1885 1885 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P29994}.
CROSSLNK 1886 1886 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P29994}.
CROSSLNK 1901 1901 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P29994}.
CROSSLNK 1924 1924 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P29994}.
CROSSLNK 2118 2118 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P29994}.
CROSSLNK 2257 2257 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P29994}.
VAR_SEQ 318 332 Missing (in isoform 2, isoform 4, isoform
6 and isoform 8). {ECO:0000305}.
/FTId=VSP_002691.
VAR_SEQ 1692 1714 Missing (in isoform 7 and isoform 8).
{ECO:0000305}.
/FTId=VSP_002692.
VAR_SEQ 1715 1715 Missing (in isoform 3, isoform 4, isoform
5, isoform 6, isoform 7 and isoform 8).
{ECO:0000305}.
/FTId=VSP_002693.
VAR_SEQ 1716 1731 Missing (in isoform 5, isoform 6, isoform
7 and isoform 8). {ECO:0000305}.
/FTId=VSP_002694.
MUTAGEN 56 56 C->A: Strongly reduced palmitoylation;
when associated with A-849 and A-2215.
{ECO:0000269|PubMed:25368151}.
MUTAGEN 167 167 Y->A: Nearly abolishes calcium flux.
{ECO:0000269|PubMed:20813840}.
MUTAGEN 168 168 K->A: Reduces calcium flux by about 50%.
{ECO:0000269|PubMed:20813840}.
MUTAGEN 169 169 L->A: Reduces calcium flux by about 50%.
MUTAGEN 267 267 T->A: Abolishes inositol 1,4,5-
triphosphate binding.
{ECO:0000269|PubMed:12442173}.
MUTAGEN 567 567 Y->A,F: Abolishes inositol 1,4,5-
triphosphate binding.
{ECO:0000269|PubMed:12442173}.
MUTAGEN 849 849 C->A: Strongly reduced palmitoylation;
when associated with A-56 and A-2215.
{ECO:0000269|PubMed:25368151}.
MUTAGEN 1588 1588 S->A: Increases interaction with AHCYL1;
when associated with A-1755.
MUTAGEN 1588 1588 S->E: Decreases interaction with AHCYL1;
when associated with A-1755.
MUTAGEN 1755 1755 S->A: Increases interaction with AHCYL1;
when associated with A-1588.
MUTAGEN 1755 1755 S->E: Decreases interaction with AHCYL1;
when associated with A-1588.
MUTAGEN 2215 2215 C->A: Strongly reduced palmitoylation;
when associated with A-56 and A-849.
{ECO:0000269|PubMed:25368151}.
MUTAGEN 2496 2496 C->S: No effect on channel activity.
Significant decrease of interaction with
ERP44. Complete loss of channel
inhibition by ERP44.
{ECO:0000269|PubMed:15652484}.
MUTAGEN 2504 2504 C->S: No effect on channel activity.
Significant decrease of interaction with
ERP44. Complete loss of channel
inhibition by ERP44.
{ECO:0000269|PubMed:15652484}.
MUTAGEN 2527 2527 C->S: Complete loss of channel activity.
Significant decrease of interaction with
ERP44. {ECO:0000269|PubMed:15652484}.
CONFLICT 1264 1264 N -> K (in Ref. 1; CAA33433).
{ECO:0000305}.
CONFLICT 2675 2675 P -> L (in Ref. 1; CAA33433).
{ECO:0000305}.
STRAND 14 23 {ECO:0000244|PDB:1XZZ}.
STRAND 25 30 {ECO:0000244|PDB:1XZZ}.
STRAND 36 39 {ECO:0000244|PDB:1XZZ}.
HELIX 41 43 {ECO:0000244|PDB:1XZZ}.
STRAND 46 48 {ECO:0000244|PDB:1XZZ}.
HELIX 53 56 {ECO:0000244|PDB:1XZZ}.
STRAND 58 61 {ECO:0000244|PDB:1XZZ}.
HELIX 67 74 {ECO:0000244|PDB:1XZZ}.
HELIX 86 109 {ECO:0000244|PDB:1XZZ}.
TURN 110 112 {ECO:0000244|PDB:1XZZ}.
STRAND 120 125 {ECO:0000244|PDB:1XZZ}.
TURN 126 129 {ECO:0000244|PDB:1XZZ}.
STRAND 130 139 {ECO:0000244|PDB:1XZZ}.
STRAND 141 143 {ECO:0000244|PDB:1XZZ}.
STRAND 146 154 {ECO:0000244|PDB:1XZZ}.
HELIX 157 159 {ECO:0000244|PDB:1XZZ}.
STRAND 161 167 {ECO:0000244|PDB:1XZZ}.
STRAND 181 189 {ECO:0000244|PDB:1XZZ}.
STRAND 193 199 {ECO:0000244|PDB:1XZZ}.
STRAND 201 205 {ECO:0000244|PDB:1XZZ}.
STRAND 207 213 {ECO:0000244|PDB:1XZZ}.
STRAND 217 223 {ECO:0000244|PDB:1XZZ}.
STRAND 239 244 {ECO:0000244|PDB:1N4K}.
TURN 245 248 {ECO:0000244|PDB:1N4K}.
STRAND 249 255 {ECO:0000244|PDB:1N4K}.
STRAND 257 265 {ECO:0000244|PDB:1N4K}.
STRAND 269 271 {ECO:0000244|PDB:1N4K}.
HELIX 272 274 {ECO:0000244|PDB:1N4K}.
HELIX 278 280 {ECO:0000244|PDB:1N4K}.
STRAND 282 286 {ECO:0000244|PDB:1N4K}.
STRAND 303 307 {ECO:0000244|PDB:1N4K}.
TURN 308 310 {ECO:0000244|PDB:1N4K}.
STRAND 313 318 {ECO:0000244|PDB:1N4K}.
STRAND 353 359 {ECO:0000244|PDB:1N4K}.
HELIX 364 366 {ECO:0000244|PDB:1N4K}.
STRAND 368 371 {ECO:0000244|PDB:1N4K}.
STRAND 388 392 {ECO:0000244|PDB:1N4K}.
TURN 393 396 {ECO:0000244|PDB:1N4K}.
STRAND 397 406 {ECO:0000244|PDB:1N4K}.
STRAND 409 412 {ECO:0000244|PDB:1N4K}.
STRAND 415 423 {ECO:0000244|PDB:1N4K}.
STRAND 430 434 {ECO:0000244|PDB:1N4K}.
HELIX 437 461 {ECO:0000244|PDB:1N4K}.
HELIX 467 484 {ECO:0000244|PDB:1N4K}.
TURN 485 487 {ECO:0000244|PDB:1N4K}.
HELIX 495 499 {ECO:0000244|PDB:1N4K}.
HELIX 504 512 {ECO:0000244|PDB:1N4K}.
HELIX 515 524 {ECO:0000244|PDB:1N4K}.
HELIX 525 527 {ECO:0000244|PDB:1N4K}.
HELIX 547 564 {ECO:0000244|PDB:1N4K}.
HELIX 568 585 {ECO:0000244|PDB:1N4K}.
HELIX 589 599 {ECO:0000244|PDB:1N4K}.
SEQUENCE 2749 AA; 313167 MW; FC4CF3ABB85EB82B CRC64;
MSDKMSSFLH IGDICSLYAE GSTNGFISTL GLVDDRCVVQ PEAGDLNNPP KKFRDCLFKL
CPMNRYSAQK QFWKAAKPGA NSTTDAVLLN KLHHAADLEK KQNETENRKL LGTVIQYGNV
IQLLHLKSNK YLTVNKRLPA LLEKNAMRVT LDEAGNEGSW FYIQPFYKLR SIGDSVVIGD
KVVLNPVNAG QPLHASSHQL VDNPGCNEVN SVNCNTSWKI VLFMKWSDNK DDILKGGDVV
RLFHAEQEKF LTCDEHRKKQ HVFLRTTGRQ SATSATSSKA LWEVEVVQHD PCRGGAGYWN
SLFRFKHLAT GHYLAAEVDP DFEEECLEFQ PSVDPDQDAS RSRLRNAQEK MVYSLVSVPE
GNDISSIFEL DPTTLRGGDS LVPRNSYVRL RHLCTNTWVH STNIPIDKEE EKPVMLKIGT
SPLKEDKEAF AIVPVSPAEV RDLDFANDAS KVLGSIAGKL EKGTITQNER RSVTKLLEDL
VYFVTGGTNS GQDVLEVVFS KPNRERQKLM REQNILKQIF KLLQAPFTDC GDGPMLRLEE
LGDQRHAPFR HICRLCYRVL RHSQQDYRKN QEYIAKQFGF MQKQIGYDVL AEDTITALLH
NNRKLLEKHI TAAEIDTFVS LVRKNREPRF LDYLSDLCVS MNKSIPVTQE LICKAVLNPT
NADILIETKL VLSRFEFEGV STGENALEAG EDEEEVWLFW RDSNKEIRSK SVRELAQDAK
EGQKEDRDIL SYYRYQLNLF ARMCLDRQYL AINEISGQLD VDLILRCMSD ENLPYDLRAS
FCRLMLHMHV DRDPQEQVTP VKYARLWSEI PSEIAIDDYD SSGTSKDEIK ERFAQTMEFV
EEYLRDVVCQ RFPFSDKEKN KLTFEVVNLA RNLIYFGFYN FSDLLRLTKI LLAILDCVHV
TTIFPISKMT KGEENKGSNV MRSIHGVGEL MTQVVLRGGG FLPMTPMAAA PEGNVKQAEP
EKEDIMVMDT KLKIIEILQF ILNVRLDYRI SCLLCIFKRE FDESNSQSSE TSSGNSSQEG
PSNVPGALDF EHIEEQAEGI FGGSEENTPL DLDDHGGRTF LRVLLHLTMH DYPPLVSGAL
QLLFRHFSQR QEVLQAFKQV QLLVTSQDVD NYKQIKQDLD QLRSIVEKSE LWVYKGQGPD
EPMDGASGEN EHKKTEEGTS KPLKHESTSS YNYRVVKEIL IRLSKLCVQE SASVRKSRKQ
QQRLLRNMGA HAVVLELLQI PYEKAEDTKM QEIMRLAHEF LQNFCAGNQQ NQALLHKHIN
LFLNPGILEA VTMQHIFMNN FQLCSEINER VVQHFVHCIE THGRNVQYIK FLQTIVKAEG
KFIKKCQDMV MAELVNSGED VLVFYNDRAS FQTLIQMMRS ERDRMDENSP LMYHIHLVEL
LAVCTEGKNV YTEIKCNSLL PLDDIVRVVT HEDCIPEVKI AYINFLNHCY VDTEVEMKEI
YTSNHMWKLF ENFLVDICRA CNNTSDRKHA DSILEKYVTE IVMSIVTTFF SSPFSDQSTT
LQTRQPVFVQ LLQGVFRVYH CNWLMPSQKA SVESCIRVLS DVAKSRAIAI PVDLDSQVNN
LFLKSHNIVQ KTALNWRLSA RNAARRDSVL AASRDYRNII ERLQDIVSAL EDRLRPLVQA
ELSVLVDVLH RPELLFPENT DARRKCESGG FICKLIKHTK QLLEENEEKL CIKVLQTLRE
MMTKDRGYGE KQISIDESEN AELPQAPEAE NSTEQELEPS PPLRQLEDHK RGEALRQILV
NRYYGNIRPS GRRESLTSFG NGPLSPGGPS KPGGGGGGPG SSSTSRGEMS LAEVQCHLDK
EGASNLVIDL IMNASSDRVF HESILLAIAL LEGGNTTIQH SFFCRLTEDK KSEKFFKVFY
DRMKVAQQEI KATVTVNTSD LGNKKKDDEV DRDAPSRKKA KEPTTQITEE VRDQLLEASA
ATRKAFTTFR READPDDHYQ SGEGTQATTD KAKDDLEMSA VITIMQPILR FLQLLCENHN
RDLQNFLRCQ NNKTNYNLVC ETLQFLDCIC GSTTGGLGLL GLYINEKNVA LINQTLESLT
EYCQGPCHEN QNCIATHESN GIDIITALIL NDINPLGKKR MDLVLELKNN ASKLLLAIME
SRHDSENAER ILYNMRPKEL VEVIKKAYMQ GEVEFEDGEN GEDGAASPRN VGHNIYILAH
QLARHNKELQ TMLKPGGQVD GDEALEFYAK HTAQIEIVRL DRTMEQIVFP VPSICEFLTK
ESKLRIYYTT ERDEQGSKIN DFFLRSEDLF NEMNWQKKLR AQPVLYWCAR NMSFWSSISF
NLAVLMNLLV AFFYPFKGVR GGTLEPHWSG LLWTAMLISL AIVIALPKPH GIRALIASTI
LRLIFSVGLQ PTLFLLGAFN VCNKIIFLMS FVGNCGTFTR GYRAMVLDVE FLYHLLYLLI
CAMGLFVHEF FYSLLLFDLV YREETLLNVI KSVTRNGRSI ILTAVLALIL VYLFSIVGYL
FFKDDFILEV DRLPNETAVP ETGESLANDF LYSDVCRVET GENCTSPAPK EELLPAEETE
QDKEHTCETL LMCIVTVLSH GLRSGGGVGD VLRKPSKEEP LFAARVIYDL LFFFMVIIIV
LNLIFGVIID TFADLRSEKQ KKEEILKTTC FICGLERDKF DNKTVTFEEH IKEEHNMWHY
LCFIVLVKVK DSTEYTGPES YVAEMIRERN LDWFPRMRAM SLVSSDSEGE QNELRNLQEK
LESTMKLVTN LSGQLSELKD QMTEQRKQKQ RIGLLGHPPH MNVNPQQPA


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