ITPR2_HUMAN
ID ITPR2_HUMAN Reviewed; 2701 AA.
AC Q14571; O94773;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Inositol 1,4,5-trisphosphate receptor type 2;
DE AltName: Full=IP3 receptor isoform 2;
DE Short=IP3R 2;
DE Short=InsP3R2;
DE AltName: Full=Type 2 inositol 1,4,5-trisphosphate receptor;
DE Short=Type 2 InsP3 receptor;
GN Name=ITPR2;
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] (ISOFORM LONG).
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] (ISOFORM SHORT).
RC TISSUE=Heart;
RX PubMed=9729462; DOI=10.1042/bj3340559;
RA Futatsugi A., Kuwajima G., Mikoshiba K.;
RT "Muscle-specific mRNA isoform encodes a protein composed mainly of the N-
RT terminal 175 residues of type 2 Ins(1,4,5)P3 receptor.";
RL Biochem. J. 334:559-563(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1160, AND IDENTIFICATION BY
RP 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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1160, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [8]
RP INVOLVEMENT IN ANHD, VARIANT ANHD SER-2498, AND CHARACTERIZATION OF VARIANT
RP ANHD SER-2498.
RX PubMed=25329695; DOI=10.1172/jci70720;
RA Klar J., Hisatsune C., Baig S.M., Tariq M., Johansson A.C., Rasool M.,
RA Malik N.A., Ameur A., Sugiura K., Feuk L., Mikoshiba K., Dahl N.;
RT "Abolished InsP3R2 function inhibits sweat secretion in both humans and
RT mice.";
RL J. Clin. Invest. 124:4773-4780(2014).
RN [9]
RP IDENTIFICATION BY 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 [10]
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. This release is
CC regulated by cAMP both dependently and independently of PKA (By
CC similarity). {ECO:0000250|UniProtKB:Q9Z329}.
CC -!- SUBUNIT: Homotetramer (By similarity). Interacts with CABP1
CC (PubMed:12032348). Interacts with BOK; regulates ITPR2 expression (By
CC similarity). Interacts with BCL2L10 (PubMed:27995898). Interacts with
CC TRPC4 (By similarity). {ECO:0000250|UniProtKB:P29995,
CC ECO:0000269|PubMed:12032348, ECO:0000269|PubMed:27995898}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q14571-1; Sequence=Displayed;
CC Name=Short; Synonyms=TIPR;
CC IsoId=Q14571-2; Sequence=VSP_002699, VSP_002700;
CC -!- TISSUE SPECIFICITY: Isoform Short is found in skeletal muscle and
CC heart.
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: Phosphorylation by cAMP-dependent PKA on Ser-937 increases calcium
CC release. {ECO:0000250}.
CC -!- DISEASE: Anhidrosis, isolated, with normal sweat glands (ANHD)
CC [MIM:106190]: An autosomal recessive disorder characterized by
CC generalized, isolated anhidrosis, severe heat intolerance, and
CC morphologically normal eccrine sweat glands. Body growth, teeth, hair,
CC nails, and skin are normal. {ECO:0000269|PubMed:25329695}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: Calcium appears to inhibit ligand binding to the
CC receptor, most probably by interacting with a distinct calcium-binding
CC protein which then inhibits the receptor.
CC -!- SIMILARITY: Belongs to the InsP3 receptor family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D26350; BAA05384.1; -; mRNA.
DR EMBL; AB012610; BAA33961.1; -; mRNA.
DR EMBL; AC023051; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC023425; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC024093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC024145; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC055720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS41764.1; -. [Q14571-1]
DR RefSeq; NP_002214.2; NM_002223.3. [Q14571-1]
DR SMR; Q14571; -.
DR BioGRID; 109914; 104.
DR IntAct; Q14571; 32.
DR MINT; Q14571; -.
DR STRING; 9606.ENSP00000370744; -.
DR BindingDB; Q14571; -.
DR ChEMBL; CHEMBL2111451; -.
DR DrugBank; DB00201; Caffeine.
DR GlyGen; Q14571; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q14571; -.
DR MetOSite; Q14571; -.
DR PhosphoSitePlus; Q14571; -.
DR BioMuta; ITPR2; -.
DR DMDM; 259016258; -.
DR EPD; Q14571; -.
DR jPOST; Q14571; -.
DR MassIVE; Q14571; -.
DR MaxQB; Q14571; -.
DR PaxDb; Q14571; -.
DR PeptideAtlas; Q14571; -.
DR PRIDE; Q14571; -.
DR ProteomicsDB; 60049; -. [Q14571-1]
DR ProteomicsDB; 60050; -. [Q14571-2]
DR Antibodypedia; 24309; 126 antibodies from 30 providers.
DR DNASU; 3709; -.
DR Ensembl; ENST00000242737.5; ENSP00000242737.5; ENSG00000123104.12. [Q14571-2]
DR Ensembl; ENST00000381340.8; ENSP00000370744.3; ENSG00000123104.12. [Q14571-1]
DR GeneID; 3709; -.
DR KEGG; hsa:3709; -.
DR MANE-Select; ENST00000381340.8; ENSP00000370744.3; NM_002223.4; NP_002214.2.
DR UCSC; uc001rhg.4; human. [Q14571-1]
DR CTD; 3709; -.
DR DisGeNET; 3709; -.
DR GeneCards; ITPR2; -.
DR HGNC; HGNC:6181; ITPR2.
DR HPA; ENSG00000123104; Tissue enhanced (liver).
DR MalaCards; ITPR2; -.
DR MIM; 106190; phenotype.
DR MIM; 600144; gene.
DR neXtProt; NX_Q14571; -.
DR OpenTargets; ENSG00000123104; -.
DR Orphanet; 468666; Isolated generalized anhidrosis with normal sweat glands.
DR PharmGKB; PA29979; -.
DR VEuPathDB; HostDB:ENSG00000123104; -.
DR eggNOG; KOG3533; Eukaryota.
DR GeneTree; ENSGT00940000156039; -.
DR HOGENOM; CLU_000206_1_0_1; -.
DR InParanoid; Q14571; -.
DR OMA; NHNSELQ; -.
DR OrthoDB; 94996at2759; -.
DR PhylomeDB; Q14571; -.
DR TreeFam; TF312815; -.
DR PathwayCommons; Q14571; -.
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-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR SignaLink; Q14571; -.
DR SIGNOR; Q14571; -.
DR BioGRID-ORCS; 3709; 19 hits in 1071 CRISPR screens.
DR ChiTaRS; ITPR2; human.
DR GeneWiki; ITPR2; -.
DR GenomeRNAi; 3709; -.
DR Pharos; Q14571; Tbio.
DR PRO; PR:Q14571; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q14571; protein.
DR Bgee; ENSG00000123104; Expressed in calcaneal tendon and 193 other tissues.
DR ExpressionAtlas; Q14571; baseline and differential.
DR Genevisible; Q14571; HS.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
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:0033017; C:sarcoplasmic reticulum membrane; IMP:BHF-UCL.
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:0015085; F:calcium ion transmembrane transporter activity; TAS:ProtInc.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IBA:GO_Central.
DR GO; GO:0005220; F:inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; ISS:BHF-UCL.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0097110; F:scaffold protein binding; IPI:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:ARUK-UCL.
DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR GO; GO:0071361; P:cellular response to ethanol; IEA:Ensembl.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISS:BHF-UCL.
DR GO; GO:0001666; P:response to hypoxia; IDA:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR016024; ARM-type_fold.
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; SSF48371; SSF48371; 1.
DR SUPFAM; SSF82109; SSF82109; 2.
DR PROSITE; PS50919; MIR; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW Disease variant; 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..2701
FT /note="Inositol 1,4,5-trisphosphate receptor type 2"
FT /id="PRO_0000153924"
FT TOPO_DOM 1..2227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2228..2248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2249..2260
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2261..2281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2282..2307
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2308..2328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2329..2351
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2352..2372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2373..2394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2395..2415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2416..2521
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2522..2542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2543..2701
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 112..166
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 173..223
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 231..287
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 294..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 1140..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 265..269
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 937
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q9Z329"
FT MOD_RES 1160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1709
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z329"
FT MOD_RES 2607
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 2633
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z329"
FT MOD_RES 2636
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z329"
FT VAR_SEQ 176..181
FT /note="IVVGDK -> DASFWI (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:9729462"
FT /id="VSP_002699"
FT VAR_SEQ 182..2701
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:9729462"
FT /id="VSP_002700"
FT VARIANT 453
FT /note="A -> V (in dbSNP:rs2230384)"
FT /id="VAR_055963"
FT VARIANT 1143
FT /note="E -> D (in dbSNP:rs2230373)"
FT /id="VAR_055964"
FT VARIANT 1898
FT /note="A -> V (in dbSNP:rs2230382)"
FT /id="VAR_055965"
FT VARIANT 2498
FT /note="G -> S (in ANHD; loss of function mutation;
FT dbSNP:rs786204832)"
FT /evidence="ECO:0000269|PubMed:25329695"
FT /id="VAR_073688"
FT CONFLICT 597
FT /note="A -> P (in Ref. 1; BAA05384)"
FT /evidence="ECO:0000305"
FT CONFLICT 1070
FT /note="P -> A (in Ref. 1; BAA05384)"
FT /evidence="ECO:0000305"
FT CONFLICT 1178
FT /note="N -> K (in Ref. 1; BAA05384)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2701 AA; 308064 MW; 373BA20228A159BC CRC64;
MTEKMSSFLY IGDIVSLYAE GSVNGFISTL GLVDDRCVVH PEAGDLANPP KKFRDCLFKV
CPMNRYSAQK QYWKAKQAKQ GNHTEAALLK KLQHAAELEQ KQNESENKKL LGEIVKYSNV
IQLLHIKSNK YLTVNKRLPA LLEKNAMRVS LDAAGNEGSW FYIHPFWKLR SEGDNIVVGD
KVVLMPVNAG QPLHASNIEL LDNPGCKEVN AVNCNTSWKI TLFMKYSSYR EDVLKGGDVV
RLFHAEQEKF LTCDEYEKKQ HIFLRTTLRQ SATSATSSKA LWEIEVVHHD PCRGGAGQWN
SLFRFKHLAT GNYLAAELNP DYRDAQNEGK NVRDGVPPTS KKKRQAGEKI MYTLVSVPHG
NDIASLFELD ATTLQRADCL VPRNSYVRLR HLCTNTWVTS TSIPIDTDEE RPVMLKIGTC
QTKEDKEAFA IVSVPLSEVR DLDFANDANK VLATTVKKLE NGTITQNERR FVTKLLEDLI
FFVADVPNNG QEVLDVVITK PNRERQKLMR EQNILAQVFG ILKAPFKEKA GEGSMLRLED
LGDQRYAPYK YMLRLCYRVL RHSQQDYRKN QEYIAKNFCV MQSQIGYDIL AEDTITALLH
NNRKLLEKHI TAKEIETFVS LLRRNREPRF LDYLSDLCVS NTTAIPVTQE LICKFMLSPG
NADILIQTKV VSMQADNPME SSILSDDIDD EEVWLYWIDS NKEPHGKAIR HLAQEAKEGT
KADLEVLTYY RYQLNLFARM CLDRQYLAIN QISTQLSVDL ILRCVSDESL PFDLRASFCR
LMLHMHVDRD PQESVVPVRY ARLWTEIPTK ITIHEYDSIT DSSRNDMKRK FALTMEFVEE
YLKEVVNQPF PFGDKEKNKL TFEVVHLARN LIYFGFYSFS ELLRLTRTLL AILDIVQAPM
SSYFERLSKF QDGGNNVMRT IHGVGEMMTQ MVLSRGSIFP MSVPDVPPSI HPSKQGSPTE
HEDVTVMDTK LKIIEILQFI LSVRLDYRIS YMLSIYKKEF GEDNDNAETS ASGSPDTLLP
SAIVPDIDEI AAQAETMFAG RKEKNPVQLD DEGGRTFLRV LIHLIMHDYP PLLSGALQLL
FKHFSQRAEV LQAFKQVQLL VSNQDVDNYK QIKADLDQLR LTVEKSELWV EKSSNYENGE
IGESQVKGGE EPIEESNILS PVQDGTKKPQ IDSNKSNNYR IVKEILIRLS KLCVQNKKCR
NQHQRLLKNM GAHSVVLDLL QIPYEKNDEK MNEVMNLAHT FLQNFCRGNP QNQVLLHKHL
NLFLTPGLLE AETMRHIFMN NYHLCNEISE RVVQHFVHCI ETHGRHVEYL RFLQTIVKAD
GKYVKKCQDM VMTELINGGE DVLIFYNDRA SFPILLHMMC SERDRGDESG PLAYHITLVE
LLAACTEGKN VYTEIKCNSL LPLDDIVRVV THDDCIPEVK IAYVNFVNHC YVDTEVEMKE
IYTSNHIWKL FENFLVDMAR VCNTTTDRKH ADIFLEKCVT ESIMNIVSGF FNSPFSDNST
SLQTHQPVFI QLLQSAFRIY NCTWPNPAQK ASVESCIRTL AEVAKNRGIA IPVDLDSQVN
TLFMKSHSNM VQRAAMGWRL SARSGPRFKE ALGGPAWDYR NIIEKLQDVV ASLEHQFSPM
MQAEFSVLVD VLYSPELLFP EGSDARIRCG AFMSKLINHT KKLMEKEEKL CIKILQTLRE
MLEKKDSFVE EGNTLRKILL NRYFKGDYSI GVNGHLSGAY SKTAQVGGSF SGQDSDKMGI
SMSDIQCLLD KEGASELVID VIVNTKNDRI FSEGIFLGIA LLEGGNTQTQ YSFYQQLHEQ
KKSEKFFKVL YDRMKAAQKE IRSTVTVNTI DLGNKKRDDD NELMTSGPRM RVRDSTLHLK
EGMKGQLTEA SSATSKAYCV YRREMDPEID IMCTGPEAGN TEEKSAEEVT MSPAIAIMQP
ILRFLQLLCE NHNRELQNFL RNQNNKTNYN LVCETLQFLD CICGSTTGGL GLLGLYINEK
NVALVNQNLE SLTEYCQGPC HENQTCIATH ESNGIDIIIA LILNDINPLG KYRMDLVLQL
KNNASKLLLA IMESRHDSEN AERILFNMRP RELVDVMKNA YNQGLECDHG DDEGGDDGVS
PKDVGHNIYI LAHQLARHNK LLQQMLKPGS DPDEGDEALK YYANHTAQIE IVRHDRTMEQ
IVFPVPNICE YLTRESKCRV FNTTERDEQG SKVNDFFQQT EDLYNEMKWQ KKIRNNPALF
WFSRHISLWG SISFNLAVFI NLAVALFYPF GDDGDEGTLS PLFSVLLWIA VAICTSMLFF
FSKPVGIRPF LVSIMLRSIY TIGLGPTLIL LGAANLCNKI VFLVSFVGNR GTFTRGYRAV
ILDMAFLYHV AYVLVCMLGL FVHEFFYSFL LFDLVYREET LLNVIKSVTR NGRSIILTAV
LALILVYLFS IIGFLFLKDD FTMEVDRLKN RTPVTGSHQV PTMTLTTMME ACAKENCSPT
IPASNTADEE YEDGIERTCD TLLMCIVTVL NQGLRNGGGV GDVLRRPSKD EPLFAARVVY
DLLFYFIVII IVLNLIFGVI IDTFADLRSE KQKKEEILKT TCFICGLERD KFDNKTVSFE
EHIKSEHNMW HYLYFIVLVK VKDPTEYTGP ESYVAQMIVE KNLDWFPRMR AMSLVSNEGD
SEQNEIRSLQ EKLESTMSLV KQLSGQLAEL KEQMTEQRKN KQRLGFLGSN TPHVNHHMPP
H
