ITPR3_HUMAN
ID ITPR3_HUMAN Reviewed; 2671 AA.
AC Q14573; Q14649; Q5TAQ2;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Inositol 1,4,5-trisphosphate receptor type 3;
DE AltName: Full=IP3 receptor isoform 3;
DE Short=IP3R 3;
DE Short=InsP3R3;
DE AltName: Full=Type 3 inositol 1,4,5-trisphosphate receptor;
DE Short=Type 3 InsP3 receptor;
GN Name=ITPR3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-2436.
RX PubMed=8081734;
RA Yamamoto-Hino M., Sugiyama T., Hikiti K., Mattei M.-G., Hasegawa K.,
RA Sekine S., Sakurada K., Miyawaki A., Furuichi T., Hasegawa M.,
RA Mikoshiba K.;
RT "Cloning and characterization of human type 2 and type 3 inositol 1,4,5-
RT trisphosphate receptors.";
RL Recept. Channels 2:9-22(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8288584; DOI=10.1016/s0021-9258(17)42246-0;
RA Maranto A.R.;
RT "Primary structure, ligand binding, and localization of the human type 3
RT inositol 1,4,5-trisphosphate receptor expressed in intestinal epithelium.";
RL J. Biol. Chem. 269:1222-1230(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH CABP1.
RX PubMed=12032348; DOI=10.1073/pnas.102006299;
RA Yang J., McBride S., Mak D.-O.D., Vardi N., Palczewski K., Haeseleer F.,
RA Foskett J.K.;
RT "Identification of a family of calcium sensors as protein ligands of
RT inositol trisphosphate receptor Ca(2+) release channels.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7711-7716(2002).
RN [6]
RP INTERACTION WITH TRPV4.
RX PubMed=18826956; DOI=10.1074/jbc.c800184200;
RA Garcia-Elias A., Lorenzo I.M., Vicente R., Valverde M.A.;
RT "IP3 receptor binds to and sensitizes TRPV4 channel to osmotic stimuli via
RT a calmodulin-binding site.";
RL J. Biol. Chem. 283:31284-31288(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-916; SER-934 AND SER-1832,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP INTERACTION WITH TMBIM4/LFG4.
RX PubMed=19553469; DOI=10.1091/mbc.e09-05-0385;
RA de Mattia F., Gubser C., van Dommelen M.M., Visch H.J., Distelmaier F.,
RA Postigo A., Luyten T., Parys J.B., de Smedt H., Smith G.L., Willems P.H.,
RA van Kuppeveld F.J.;
RT "Human Golgi antiapoptotic protein modulates intracellular calcium
RT fluxes.";
RL Mol. Biol. Cell 20:3638-3645(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1813, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-916 AND SER-2670, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-916; SER-934; SER-1832;
RP SER-1834; SER-2609 AND SER-2670, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP INTERACTION WITH CEMIP.
RX PubMed=23936024; DOI=10.1371/journal.pone.0069473;
RA Tiwari A., Schneider M., Fiorino A., Haider R., Okoniewski M.J.,
RA Roschitzki B., Uzozie A., Menigatti M., Jiricny J., Marra G.;
RT "Early insights into the function of KIAA1199, a markedly overexpressed
RT protein in human colorectal tumors.";
RL PLoS ONE 8:E69473-E69473(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1832, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP INTERACTION WITH TMEM203.
RX PubMed=25996873; DOI=10.1371/journal.pone.0127480;
RA Shambharkar P.B., Bittinger M., Latario B., Xiong Z., Bandyopadhyay S.,
RA Davis V., Lin V., Yang Y., Valdez R., Labow M.A.;
RT "TMEM203 is a novel regulator of intracellular calcium homeostasis and is
RT required for spermatogenesis.";
RL PLoS ONE 10:E0127480-E0127480(2015).
RN [16]
RP INTERACTION WITH BCL2L10.
RX PubMed=27995898; DOI=10.7554/elife.19896;
RA Bonneau B., Ando H., Kawaai K., Hirose M., Takahashi-Iwanaga H.,
RA Mikoshiba K.;
RT "IRBIT controls apoptosis by interacting with the Bcl-2 homolog, Bcl2l10,
RT and by promoting ER-mitochondria contact.";
RL Elife 5:e19896-e19896(2016).
CC -!- FUNCTION: Receptor for inositol 1,4,5-trisphosphate, a second messenger
CC that mediates the release of intracellular calcium.
CC -!- SUBUNIT: Homotetramer. Interacts with TRPC1, TRPC3 and TRPC4. Interacts
CC with TRPV4 (PubMed:18826956). Interacts with SIGMAR1 (By similarity).
CC Interacts with PML and AKT1 (By similarity). Interacts with IRAG2 (via
CC coiled-coil domain) (By similarity). Interacts with CABP1
CC (PubMed:12032348). Interacts with TMBIM4/LFG4 (PubMed:19553469).
CC Interacts with CEMIP (PubMed:23936024). Interacts with TESPA1 (By
CC similarity). Interacts with TMEM203 (PubMed:25996873). Interacts with
CC BOK; regulates ITPR3 expression (By similarity). Interacts with BCL2L10
CC (PubMed:27995898). {ECO:0000250|UniProtKB:P70227,
CC ECO:0000250|UniProtKB:Q63269, ECO:0000269|PubMed:12032348,
CC ECO:0000269|PubMed:18826956, ECO:0000269|PubMed:19553469,
CC ECO:0000269|PubMed:23936024, ECO:0000269|PubMed:25996873,
CC ECO:0000269|PubMed:27995898}.
CC -!- INTERACTION:
CC Q14573; Q92560: BAP1; NbExp=12; IntAct=EBI-351055, EBI-1791447;
CC Q14573; Q13507: TRPC3; NbExp=5; IntAct=EBI-351055, EBI-520807;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in intestinal crypt and villus epithelial
CC cells.
CC -!- DOMAIN: The receptor contains a calcium channel in its C-terminal
CC extremity. Its large N-terminal cytoplasmic region has the ligand-
CC binding site in the N-terminus and modulatory sites in the middle
CC portion immediately upstream of the channel region.
CC -!- PTM: Phosphorylated on tyrosine residues. Phosphorylated by AKT1 on
CC serine and/or threonine residues (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the InsP3 receptor family. {ECO:0000305}.
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DR EMBL; D26351; BAA05385.1; -; mRNA.
DR EMBL; U01062; AAC50064.1; -; mRNA.
DR EMBL; AL139044; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03744.1; -; Genomic_DNA.
DR CCDS; CCDS4783.1; -.
DR PIR; A49873; A49873.
DR RefSeq; NP_002215.2; NM_002224.3.
DR PDB; 6DQJ; EM; 3.49 A; A/B/C/D=1-2671.
DR PDB; 6DQN; EM; 3.33 A; A/B/C/D=1-2671.
DR PDB; 6DQS; EM; 4.12 A; A/B/C/D=1-2671.
DR PDB; 6DQV; EM; 3.82 A; A/B/C/D=1-2671.
DR PDB; 6DQZ; EM; 6.01 A; A/B/C/D=1-2671.
DR PDB; 6DR0; EM; 4.47 A; A/B/C/D=1-2671.
DR PDB; 6DR2; EM; 4.33 A; A/B/C/D=1-2671.
DR PDB; 6DRA; EM; 3.96 A; A/B/C/D=1-2671.
DR PDB; 6DRC; EM; 3.92 A; A/B/C/D=1-2671.
DR PDB; 6UQK; EM; 3.77 A; A/B/C/D=4-2611.
DR PDB; 7T3P; EM; 3.20 A; A/B/C/D=1-2611.
DR PDB; 7T3Q; EM; 3.30 A; A/B/C/D=1-2611.
DR PDB; 7T3R; EM; 3.40 A; A/B/C/D=1-2611.
DR PDB; 7T3T; EM; 3.80 A; A/B/C/D=1-2611.
DR PDB; 7T3U; EM; 3.70 A; A/B/C/D=1-2611.
DR PDBsum; 6DQJ; -.
DR PDBsum; 6DQN; -.
DR PDBsum; 6DQS; -.
DR PDBsum; 6DQV; -.
DR PDBsum; 6DQZ; -.
DR PDBsum; 6DR0; -.
DR PDBsum; 6DR2; -.
DR PDBsum; 6DRA; -.
DR PDBsum; 6DRC; -.
DR PDBsum; 6UQK; -.
DR PDBsum; 7T3P; -.
DR PDBsum; 7T3Q; -.
DR PDBsum; 7T3R; -.
DR PDBsum; 7T3T; -.
DR PDBsum; 7T3U; -.
DR AlphaFoldDB; Q14573; -.
DR SMR; Q14573; -.
DR BioGRID; 109915; 203.
DR CORUM; Q14573; -.
DR IntAct; Q14573; 57.
DR MINT; Q14573; -.
DR STRING; 9606.ENSP00000363435; -.
DR BindingDB; Q14573; -.
DR ChEMBL; CHEMBL3904; -.
DR DrugBank; DB00201; Caffeine.
DR GlyGen; Q14573; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q14573; -.
DR PhosphoSitePlus; Q14573; -.
DR SwissPalm; Q14573; -.
DR BioMuta; ITPR3; -.
DR DMDM; 209572633; -.
DR EPD; Q14573; -.
DR jPOST; Q14573; -.
DR MassIVE; Q14573; -.
DR MaxQB; Q14573; -.
DR PaxDb; Q14573; -.
DR PeptideAtlas; Q14573; -.
DR PRIDE; Q14573; -.
DR ProteomicsDB; 60051; -.
DR Antibodypedia; 1294; 159 antibodies from 27 providers.
DR DNASU; 3710; -.
DR Ensembl; ENST00000374316.9; ENSP00000363435.4; ENSG00000096433.11.
DR Ensembl; ENST00000605930.3; ENSP00000475177.1; ENSG00000096433.11.
DR GeneID; 3710; -.
DR KEGG; hsa:3710; -.
DR MANE-Select; ENST00000605930.3; ENSP00000475177.1; NM_002224.4; NP_002215.2.
DR UCSC; uc063nyh.1; human.
DR CTD; 3710; -.
DR DisGeNET; 3710; -.
DR GeneCards; ITPR3; -.
DR HGNC; HGNC:6182; ITPR3.
DR HPA; ENSG00000096433; Low tissue specificity.
DR MalaCards; ITPR3; -.
DR MIM; 147267; gene.
DR neXtProt; NX_Q14573; -.
DR OpenTargets; ENSG00000096433; -.
DR PharmGKB; PA29980; -.
DR VEuPathDB; HostDB:ENSG00000096433; -.
DR eggNOG; KOG3533; Eukaryota.
DR GeneTree; ENSGT00940000157078; -.
DR HOGENOM; CLU_000206_1_0_1; -.
DR InParanoid; Q14573; -.
DR OMA; WLMWTDK; -.
DR OrthoDB; 94996at2759; -.
DR PhylomeDB; Q14573; -.
DR TreeFam; TF312815; -.
DR PathwayCommons; Q14573; -.
DR Reactome; R-HSA-112043; PLC beta mediated events.
DR Reactome; R-HSA-114508; Effects of PIP2 hydrolysis.
DR Reactome; R-HSA-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-HSA-1489509; DAG and IP3 signaling.
DR Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-HSA-4086398; Ca2+ pathway.
DR Reactome; R-HSA-422356; Regulation of insulin secretion.
DR Reactome; R-HSA-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-HSA-5578775; Ion homeostasis.
DR Reactome; R-HSA-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR Reactome; R-HSA-9664323; FCGR3A-mediated IL10 synthesis.
DR Reactome; R-HSA-9717207; Sensory perception of sweet, bitter, and umami (glutamate) taste.
DR Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR SignaLink; Q14573; -.
DR BioGRID-ORCS; 3710; 8 hits in 1081 CRISPR screens.
DR ChiTaRS; ITPR3; human.
DR GeneWiki; ITPR3; -.
DR GenomeRNAi; 3710; -.
DR Pharos; Q14573; Tchem.
DR PRO; PR:Q14573; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q14573; protein.
DR Bgee; ENSG00000096433; Expressed in cartilage tissue and 183 other tissues.
DR Genevisible; Q14573; HS.
DR GO; GO:0045177; C:apical part of cell; ISS:BHF-UCL.
DR GO; GO:0005903; C:brush border; ISS:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:BHF-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0043209; C:myelin sheath; ISS:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; ISS:BHF-UCL.
DR GO; GO:0005640; C:nuclear outer membrane; ISS:BHF-UCL.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0031095; C:platelet dense tubular network membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0030667; C:secretory granule membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0015278; F:calcium-release channel activity; ISS:UniProtKB.
DR GO; GO:0043533; F:inositol 1,3,4,5 tetrakisphosphate binding; ISS:BHF-UCL.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IDA:BHF-UCL.
DR GO; GO:0005220; F:inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; IDA:BHF-UCL.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; ISS:BHF-UCL.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
DR GO; GO:0007613; P:memory; IEA:Ensembl.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:BHF-UCL.
DR GO; GO:0051592; P:response to calcium ion; IDA:BHF-UCL.
DR GO; GO:0050913; P:sensory perception of bitter taste; IEA:Ensembl.
DR GO; GO:0050916; P:sensory perception of sweet taste; IEA:Ensembl.
DR GO; GO:0050909; P:sensory perception of taste; TAS:Reactome.
DR GO; GO:0050917; P:sensory perception of umami taste; IEA:Ensembl.
DR InterPro; IPR014821; Ins145_P3_rcpt.
DR InterPro; IPR000493; InsP3_rcpt.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR036300; MIR_dom_sf.
DR InterPro; IPR016093; MIR_motif.
DR InterPro; IPR013662; RIH_assoc-dom.
DR InterPro; IPR000699; RIH_dom.
DR InterPro; IPR035910; RyR/IP3R_RIH_dom_sf.
DR Pfam; PF08709; Ins145_P3_rec; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF02815; MIR; 1.
DR Pfam; PF08454; RIH_assoc; 1.
DR Pfam; PF01365; RYDR_ITPR; 2.
DR PRINTS; PR00779; INSP3RECEPTR.
DR SMART; SM00472; MIR; 4.
DR SUPFAM; SSF100909; SSF100909; 2.
DR SUPFAM; SSF82109; SSF82109; 2.
DR PROSITE; PS50919; MIR; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Calcium channel; Calcium transport;
KW Endoplasmic reticulum; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..2671
FT /note="Inositol 1,4,5-trisphosphate receptor type 3"
FT /id="PRO_0000153928"
FT TOPO_DOM 1..2202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2203..2223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2224..2235
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2236..2256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2257..2264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2265..2285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2286..2325
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2326..2346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2347..2368
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2369..2389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2390..2496
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2497..2517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2518..2671
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 113..173
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 174..224
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 232..288
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 295..372
FT /note="MIR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 378..434
FT /note="MIR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT REGION 322..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1809..1848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1831..1845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 266..270
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT /evidence="ECO:0000250"
FT BINDING 507..510
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT /evidence="ECO:0000250"
FT BINDING 567..569
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT /evidence="ECO:0000250"
FT MOD_RES 916
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 934
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1813
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1832
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1834
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2609
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2670
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 374
FT /note="L -> W (in dbSNP:rs2229646)"
FT /id="VAR_049604"
FT VARIANT 667
FT /note="R -> Q (in dbSNP:rs11963294)"
FT /id="VAR_046978"
FT VARIANT 742
FT /note="D -> E (in dbSNP:rs2229633)"
FT /id="VAR_046979"
FT VARIANT 1029
FT /note="G -> V (in dbSNP:rs2296333)"
FT /id="VAR_046980"
FT VARIANT 1552
FT /note="L -> V (in dbSNP:rs9461899)"
FT /id="VAR_046981"
FT VARIANT 1850
FT /note="R -> Q (in dbSNP:rs12528378)"
FT /id="VAR_046982"
FT VARIANT 2398
FT /note="E -> Q (in dbSNP:rs2229641)"
FT /id="VAR_046983"
FT VARIANT 2436
FT /note="L -> V (in dbSNP:rs2229642)"
FT /evidence="ECO:0000269|PubMed:8081734"
FT /id="VAR_046984"
FT CONFLICT 524
FT /note="A -> V (in Ref. 2; AAC50064)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="H -> Y (in Ref. 2; AAC50064)"
FT /evidence="ECO:0000305"
FT CONFLICT 989
FT /note="Y -> H (in Ref. 1; BAA05385)"
FT /evidence="ECO:0000305"
FT CONFLICT 1143
FT /note="A -> T (in Ref. 2; AAC50064)"
FT /evidence="ECO:0000305"
FT CONFLICT 1391
FT /note="L -> V (in Ref. 2; AAC50064)"
FT /evidence="ECO:0000305"
FT CONFLICT 1496..1497
FT /note="TI -> PV (in Ref. 2; AAC50064)"
FT /evidence="ECO:0000305"
FT CONFLICT 1674
FT /note="L -> V (in Ref. 2; AAC50064)"
FT /evidence="ECO:0000305"
FT CONFLICT 2187..2188
FT /note="KL -> NV (in Ref. 1; BAA05385 and 2; AAC50064)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2671 AA; 304106 MW; 04D1957A53320EEE CRC64;
MSEMSSFLHI GDIVSLYAEG SVNGFISTLG LVDDRCVVEP AAGDLDNPPK KFRDCLFKVC
PMNRYSAQKQ YWKAKQTKQD KEKIADVVLL QKLQHAAQME QKQNDTENKK VHGDVVKYGS
VIQLLHMKSN KYLTVNKRLP ALLEKNAMRV TLDATGNEGS WLFIQPFWKL RSNGDNVVVG
DKVILNPVNA GQPLHASNYE LSDNAGCKEV NSVNCNTSWK INLFMQFRDH LEEVLKGGDV
VRLFHAEQEK FLTCDEYKGK LQVFLRTTLR QSATSATSSN ALWEVEVVHH DPCRGGAGHW
NGLYRFKHLA TGNYLAAEEN PSYKGDASDP KAAGMGAQGR TGRRNAGEKI KYCLVAVPHG
NDIASLFELD PTTLQKTDSF VPRNSYVRLR HLCTNTWIQS TNVPIDIEEE RPIRLMLGTC
PTKEDKEAFA IVSVPVSEIR DLDFANDASS MLASAVEKLN EGFISQNDRR FVIQLLEDLV
FFVSDVPNNG QNVLDIMVTK PNRERQKLMR EQNILKQVFG ILKAPFREKG GEGPLVRLEE
LSDQKNAPYQ HMFRLCYRVL RHSQEDYRKN QEHIAKQFGM MQSQIGYDIL AEDTITALLH
NNRKLLEKHI TKTEVETFVS LVRKNREPRF LDYLSDLCVS NHIAIPVTQE LICKCVLDPK
NSDILIRTEL RPVKEMAQSH EYLSIEYSEE EVWLTWTDKN NEHHEKSVRQ LAQEARAGNA
HDENVLSYYR YQLKLFARMC LDRQYLAIDE ISQQLGVDLI FLCMADEMLP FDLRASFCHL
MLHVHVDRDP QELVTPVKFA RLWTEIPTAI TIKDYDSNLN ASRDDKKNKF ANTMEFVEDY
LNNVVSEAVP FANEEKNKLT FEVVSLAHNL IYFGFYSFSE LLRLTRTLLG IIDCVQGPPA
MLQAYEDPGG KNVRRSIQGV GHMMSTMVLS RKQSVFSAPS LSAGASAAEP LDRSKFEENE
DIVVMETKLK ILEILQFILN VRLDYRISYL LSVFKKEFVE VFPMQDSGAD GTAPAFDSTT
ANMNLDRIGE QAEAMFGVGK TSSMLEVDDE GGRMFLRVLI HLTMHDYAPL VSGALQLLFK
HFSQRQEAMH TFKQVQLLIS AQDVENYKVI KSELDRLRTM VEKSELWVDK KGSGKGEEVE
AGAAKDKKER PTDEEGFLHP PGEKSSENYQ IVKGILERLN KMCGVGEQMR KKQQRLLKNM
DAHKVMLDLL QIPYDKGDAK MMEILRYTHQ FLQKFCAGNP GNQALLHKHL HLFLTPGLLE
AETMQHIFLN NYQLCSEISE PVLQHFVHLL ATHGRHVQYL DFLHTVIKAE GKYVKKCQDM
IMTELTNAGD DVVVFYNDKA SLAHLLDMMK AARDGVEDHS PLMYHISLVD LLAACAEGKN
VYTEIKCTSL LPLEDVVSVV THEDCITEVK MAYVNFVNHC YVDTEVEMKE IYTSNHIWTL
FENFTLDMAR VCSKREKRVA DPTLEKYVLS VVLDTINAFF SSPFSENSTS LQTHQTIVVQ
LLQSTTRLLE CPWLQQQHKG SVEACIRTLA MVAKGRAILL PMDLDAHISS MLSSGASCAA
AAQRNASSYK ATTRAFPRVT PTANQWDYKN IIEKLQDIIT ALEERLKPLV QAELSVLVDV
LHWPELLFLE GSEAYQRCES GGFLSKLIQH TKDLMESEEK LCIKVLRTLQ QMLLKKTKYG
DRGNQLRKML LQNYLQNRKS TSRGDLPDPI GTGLDPDWSA IAATQCRLDK EGATKLVCDL
ITSTKNEKIF QESIGLAIHL LDGGNTEIQK SFHNLMMSDK KSERFFKVLH DRMKRAQQET
KSTVAVNMND LGSQPHEDRE PVDPTTKGRV ASFSIPGSSS RYSLGPSLRR GHEVSERVQS
SEMGTSVLIM QPILRFLQLL CENHNRDLQN FLRCQNNKTN YNLVCETLQF LDIMCGSTTG
GLGLLGLYIN EDNVGLVIQT LETLTEYCQG PCHENQTCIV THESNGIDII TALILNDISP
LCKYRMDLVL QLKDNASKLL LALMESRHDS ENAERILISL RPQELVDVIK KAYLQEEERE
NSEVSPREVG HNIYILALQL SRHNKQLQHL LKPVKRIQEE EAEGISSMLS LNNKQLSQML
KSSAPAQEEE EDPLAYYENH TSQIEIVRQD RSMEQIVFPV PGICQFLTEE TKHRLFTTTE
QDEQGSKVSD FFDQSSFLHN EMEWQRKLRS MPLIYWFSRR MTLWGSISFN LAVFINIIIA
FFYPYMEGAS TGVLDSPLIS LLFWILICFS IAALFTKRYS IRPLIVALIL RSIYYLGIGP
TLNILGALNL TNKIVFVVSF VGNRGTFIRG YKAMVMDMEF LYHVGYILTS VLGLFAHELF
YSILLFDLIY REETLFNVIK SVTRNGRSIL LTALLALILV YLFSIVGFLF LKDDFILEVD
RLPNNHSTAS PLGMPHGAAA FVDTCSGDKM DCVSGLSVPE VLEEDRELDS TERACDTLLM
CIVTVMNHGL RNGGGVGDIL RKPSKDESLF PARVVYDLLF FFIVIIIVLN LIFGVIIDTF
ADLRSEKQKK EEILKTTCFI CGLERDKFDN KTVSFEEHIK LEHNMWNYLY FIVLVRVKNK
TDYTGPESYV AQMIKNKNLD WFPRMRAMSL VSNEGEGEQN EIRILQDKLN STMKLVSHLT
AQLNELKEQM TEQRKRRQRL GFVDVQNCIS R
