ID ITPR1_MOUSE Reviewed; 2749 AA. AC P11881; P20943; Q99LG5; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 2. DT 26-NOV-2014, entry version 173. DE RecName: Full=Inositol 1,4,5-trisphosphate receptor type 1; DE AltName: Full=IP3 receptor isoform 1; DE Short=IP3R 1; DE Short=InsP3R1; DE AltName: Full=Inositol 1,4,5-trisphosphate-binding protein P400; DE AltName: Full=Protein PCD-6; DE AltName: Full=Purkinje cell protein 1; DE AltName: Full=Type 1 inositol 1,4,5-trisphosphate receptor; DE Short=Type 1 InsP3 receptor; GN Name=Itpr1; Synonyms=Insp3r, Pcd6, Pcp1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR RP LOCATION. RC TISSUE=Purkinje cell; RX PubMed=2554142; DOI=10.1038/342032a0; RA Furuichi T., Yoshikawa S., Miyawaki A., Wada K., Maeda N., RA Mikoshiba K.; RT "Primary structure and functional expression of the inositol 1,4,5- RT trisphosphate-binding protein P400."; RL Nature 342:32-38(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=ICR; TISSUE=Cerebellum; RX PubMed=2762133; DOI=10.1093/nar/17.13.5385; RA Furuichi T., Yoshikawa S., Mikoshiba K.; RT "Nucleotide sequence of cDNA encoding P400 protein in the mouse RT cerebellum."; RL Nucleic Acids Res. 17:5385-5386(1989). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 318-332 AND 1692-1731, AND RP ALTERNATIVE SPLICING. RC STRAIN=ICR; RX PubMed=1648733; DOI=10.1073/pnas.88.14.6244; RA Nakagawa T., Okano H., Furuichi T., Aruga J., Mikoshiba K.; RT "The subtypes of the mouse inositol 1,4,5-trisphosphate receptor are RT expressed in a tissue-specific and developmentally specific manner."; RL Proc. Natl. Acad. Sci. U.S.A. 88:6244-6248(1991). RN [5] RP PROTEIN SEQUENCE OF 862-871, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2098-2749. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2250-2749. RC STRAIN=C57BL/6J; TISSUE=Cerebellum; RX PubMed=3199205; RA Nordquist D.T., Kozak C.A., Orr H.T.; RT "cDNA cloning and characterization of three genes uniquely expressed RT in cerebellum by Purkinje neurons."; RL J. Neurosci. 8:4780-4789(1988). RN [8] RP INTERACTION WITH AHCYL1. RX PubMed=12525476; DOI=10.1074/jbc.M210119200; RA Ando H., Mizutani A., Matsu-ura T., Mikoshiba K.; RT "IRBIT, a novel inositol 1,4,5-trisphosphate (IP3) receptor-binding RT protein, is released from the IP3 receptor upon IP3 binding to the RT receptor."; RL J. Biol. Chem. 278:10602-10612(2003). RN [9] RP INTERACTION WITH ERP44, AND MUTAGENESIS OF CYS-2496; CYS-2504 AND RP CYS-2527. RX PubMed=15652484; DOI=10.1016/j.cell.2004.11.048; RA Higo T., Hattori M., Nakamura T., Natsume T., Michikawa T., RA Mikoshiba K.; RT "Subtype-specific and ER lumenal environment-dependent regulation of RT inositol 1,4,5-trisphosphate receptor type 1 by ERp44."; RL Cell 120:85-98(2005). RN [10] RP INTERACTION WITH AHCYL1. RX PubMed=16527252; DOI=10.1016/j.bbrc.2006.02.119; RA Devogelaere B., Nadif Kasri N., Derua R., Waelkens E., Callewaert G., RA Missiaen L., Parys J.B., De Smedt H.; RT "Binding of IRBIT to the IP3 receptor: determinants and functional RT effects."; RL Biochem. Biophys. Res. Commun. 343:49-56(2006). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1588, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18630941; DOI=10.1021/pr800223m; RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; RT "Specific phosphopeptide enrichment with immobilized titanium ion RT affinity chromatography adsorbent for phosphoproteome analysis."; RL J. Proteome Res. 7:3957-3967(2008). RN [12] RP FUNCTION. RX PubMed=19752026; DOI=10.1083/jcb.200904060; RA Li G., Mongillo M., Chin K.T., Harding H., Ron D., Marks A.R., RA Tabas I.; RT "Role of ERO1-alpha-mediated stimulation of inositol 1,4,5- RT triphosphate receptor activity in endoplasmic reticulum stress-induced RT apoptosis."; RL J. Cell Biol. 186:783-792(2009). RN [13] RP FUNCTION, AND MUTAGENESIS OF TYR-167 AND LYS-168. RX PubMed=20813840; DOI=10.1074/jbc.M110.140129; RA Yamazaki H., Chan J., Ikura M., Michikawa T., Mikoshiba K.; RT "Tyr-167/Trp-168 in type 1/3 inositol 1,4,5-trisphosphate receptor RT mediates functional coupling between ligand binding and channel RT opening."; RL J. Biol. Chem. 285:36081-36091(2010). RN [14] RP INTERACTION WITH TESPA1. RX PubMed=23650607; DOI=10.1016/j.fob.2012.08.005; RA Matsuzaki H., Fujimoto T., Ota T., Ogawa M., Tsunoda T., Doi K., RA Hamabashiri M., Tanaka M., Shirasawa S.; RT "Tespa1 is a novel inositol 1,4,5-trisphosphate receptor binding RT protein in T and B lymphocytes."; RL FEBS Open Bio 2:255-259(2012). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 224-604 IN COMPLEX WITH RP INOSITOL 1,4,5-TRISPHOSPHATE, AND MUTAGENESIS OF THR-267 AND TYR-567. RX PubMed=12442173; DOI=10.1038/nature01268; RA Bosanac I., Alattia J.R., Mal T.K., Chan J., Talarico S., Tong F.K., RA Tong K.I., Yoshikawa F., Furuichi T., Iwai M., Michikawa T., RA Mikoshiba K., Ikura M.; RT "Structure of the inositol 1,4,5-trisphosphate receptor binding core RT in complex with its ligand."; RL Nature 420:696-700(2002). RN [16] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-223. RX PubMed=15664189; DOI=10.1016/j.molcel.2004.11.047; RA Bosanac I., Yamazaki H., Matsu-Ura T., Michikawa T., Mikoshiba K., RA Ikura M.; RT "Crystal structure of the ligand binding suppressor domain of type 1 RT inositol 1,4,5-trisphosphate receptor."; RL Mol. Cell 17:193-203(2005). RN [17] RP INTERACTION WITH MRVI1. RX PubMed=16990611; DOI=10.1182/blood-2005-10-026294; RA Antl M., von Bruehl M.-L., Eiglsperger C., Werner M., Konrad I., RA Kocher T., Wilm M., Hofmann F., Massberg S., Schlossmann J.; RT "IRAG mediates NO/cGMP-dependent inhibition of platelet aggregation RT and thrombus formation."; RL Blood 109:552-559(2007). CC -!- FUNCTION: Intracellular channel that mediates calcium release from CC the endoplasmic reticulum following stimulation by inositol 1,4,5- CC trisphosphate. Plays a role in ER stress-induced apoptosis. CC Cytoplasmic calcium released from the ER triggers apoptosis by the CC activation of CaM kinase II, eventually leading to the activation CC of downstream apoptosis pathways. {ECO:0000269|PubMed:19752026, CC ECO:0000269|PubMed:20813840, ECO:0000269|PubMed:2554142}. CC -!- SUBUNIT: Homotetramer. Interacts with TRPC4. The PPXXF motif binds CC HOM1, HOM2 and HOM3. Interacts with RYR1, RYR2, ITPR1, SHANK1 and CC SHANK3. Part of cGMP kinase signaling complex at least composed of CC ACTA2/alpha-actin, CNN1/calponin H1, PLN/phospholamban, PRKG1 and CC ITPR1 (By similarity). Interacts with ERP44 in a pH-, redox state- CC and calcium-dependent manner which results in the inhibition the CC calcium channel activity. The strength of this interaction CC inversely correlates with calcium concentration. Interacts with CC AHCYL1 and MRVI1. Interacts with CABP1 (By similarity). Interacts CC with TESPA1. {ECO:0000250, ECO:0000269|PubMed:12442173, CC ECO:0000269|PubMed:12525476, ECO:0000269|PubMed:15652484, CC ECO:0000269|PubMed:16527252, ECO:0000269|PubMed:16990611, CC ECO:0000269|PubMed:23650607}. CC -!- INTERACTION: CC Q9D1Q6:Erp44; NbExp=5; IntAct=EBI-541478, EBI-541567; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:2554142}; Multi-pass membrane protein CC {ECO:0000269|PubMed:2554142}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=8; CC Comment=There is a combination of two alternatively spliced CC domains at site SI and site SII (A, B and C). Experimental CC confirmation may be lacking for some isoforms.; CC Name=1; Synonyms=SISIIABC; CC IsoId=P11881-1; Sequence=Displayed; CC Name=2; Synonyms=SI-SIIABC; CC IsoId=P11881-2; Sequence=VSP_002691; CC Name=3; Synonyms=SISIIAC; CC IsoId=P11881-3; Sequence=VSP_002693; CC Name=4; Synonyms=SI-SIIAC; CC IsoId=P11881-4; Sequence=VSP_002691, VSP_002693; CC Name=5; Synonyms=SISIIA; CC IsoId=P11881-5; Sequence=VSP_002693, VSP_002694; CC Name=6; Synonyms=SI-SIIA; CC IsoId=P11881-6; Sequence=VSP_002691, VSP_002693, VSP_002694; CC Name=7; Synonyms=SISII; CC IsoId=P11881-7; Sequence=VSP_002692, VSP_002693, VSP_002694; CC Name=8; Synonyms=SI-SII; CC IsoId=P11881-8; Sequence=VSP_002691, VSP_002692, VSP_002693, CC VSP_002694; 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 by cAMP kinase. Phosphorylation prevents the CC ligand-induced opening of the calcium channels. CC {ECO:0000269|PubMed:18630941}. CC -!- PTM: Phosphorylated on tyrosine residues. {ECO:0000250}. CC -!- PTM: Ubiquitination at multiple lysines targets ITPR1 for CC proteasomal degradation. Approximately 40% of the ITPR1-associated CC ubiquitin is monoubiquitin, and polyubiquitins are both 'Lys-48'- CC and 'Lys-63'-linked (By similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: Calcium appears to inhibit ligand binding to the CC receptor, most probably by interacting with a distinct calcium- CC binding protein which then inhibits the receptor. CC -!- SIMILARITY: Belongs to the InsP3 receptor family. {ECO:0000305}. CC -!- SIMILARITY: Contains 5 MIR domains. {ECO:0000255|PROSITE- CC ProRule:PRU00131}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA88319.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=AAH03271.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={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; X15373; CAA33433.1; -; mRNA. DR EMBL; AC120411; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC153986; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC156506; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M75986; AAA39316.1; -; Genomic_DNA. DR EMBL; M75987; AAA39317.1; -; Genomic_DNA. DR EMBL; BC003271; AAH03271.1; ALT_INIT; mRNA. DR EMBL; M21530; AAA88319.1; ALT_INIT; mRNA. DR CCDS; CCDS51869.1; -. [P11881-1] DR PIR; S04844; ACMSIT. DR RefSeq; NP_034715.3; NM_010585.5. [P11881-1] DR RefSeq; XP_006505693.1; XM_006505630.1. [P11881-2] DR RefSeq; XP_006505699.1; XM_006505636.1. [P11881-7] DR RefSeq; XP_006505700.1; XM_006505637.1. [P11881-8] DR UniGene; Mm.227912; -. DR PDB; 1N4K; X-ray; 2.20 A; A=224-604. DR PDB; 1XZZ; X-ray; 1.80 A; A=2-223. DR PDBsum; 1N4K; -. DR PDBsum; 1XZZ; -. DR ProteinModelPortal; P11881; -. DR SMR; P11881; 7-580. DR BioGrid; 200847; 17. DR DIP; DIP-32243N; -. DR IntAct; P11881; 11. DR MINT; MINT-4099099; -. DR PhosphoSite; P11881; -. DR MaxQB; P11881; -. DR PaxDb; P11881; -. DR PRIDE; P11881; -. DR Ensembl; ENSMUST00000032192; ENSMUSP00000032192; ENSMUSG00000030102. [P11881-1] DR GeneID; 16438; -. DR KEGG; mmu:16438; -. DR UCSC; uc009ddh.3; mouse. [P11881-1] DR CTD; 3708; -. DR MGI; MGI:96623; Itpr1. DR eggNOG; NOG280601; -. DR GeneTree; ENSGT00760000119152; -. DR HOGENOM; HOG000007660; -. DR HOVERGEN; HBG052158; -. DR InParanoid; P11881; -. DR KO; K04958; -. DR OMA; KAFTTFR; -. DR OrthoDB; EOG76HQ0M; -. DR PhylomeDB; P11881; -. DR TreeFam; TF312815; -. DR Reactome; REACT_188194; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers. DR Reactome; REACT_188202; FCERI mediated Ca+2 mobilization. DR Reactome; REACT_188269; DAG and IP3 signaling. DR Reactome; REACT_210240; Role of phospholipids in phagocytosis. DR Reactome; REACT_219232; Effects of PIP2 hydrolysis. DR Reactome; REACT_221970; Ca2+ pathway. DR Reactome; REACT_227667; Elevation of cytosolic Ca2+ levels. DR Reactome; REACT_229620; cGMP effects. DR Reactome; REACT_245086; VEGFR2 mediated cell proliferation. DR Reactome; REACT_248547; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion. DR Reactome; REACT_253342; PLC beta mediated events. DR Reactome; REACT_263148; Regulation of insulin secretion. DR ChiTaRS; Itpr1; mouse. DR EvolutionaryTrace; P11881; -. DR NextBio; 289681; -. DR PRO; PR:P11881; -. DR Bgee; P11881; -. DR CleanEx; MM_ITPR1; -. DR ExpressionAtlas; P11881; baseline and differential. DR Genevestigator; P11881; -. DR GO; GO:0005955; C:calcineurin complex; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005783; C:endoplasmic reticulum; TAS:MGI. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005635; C:nuclear envelope; IDA:MGI. DR GO; GO:0005637; C:nuclear inner membrane; IDA:MGI. DR GO; GO:0005730; C:nucleolus; IDA:MGI. DR GO; GO:0031088; C:platelet dense granule membrane; IEA:Ensembl. DR GO; GO:0031094; C:platelet dense tubular network; IEA:Ensembl. DR GO; GO:0014069; C:postsynaptic density; IDA:MGI. DR GO; GO:0043234; C:protein complex; IPI:MGI. DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:MGI. DR GO; GO:0005220; F:inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; IDA:UniProtKB. DR GO; GO:0005218; F:intracellular ligand-gated calcium channel activity; IDA:UniProtKB. DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB. DR GO; GO:0006816; P:calcium ion transport; IDA:MGI. DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IGI:MGI. DR GO; GO:0048016; P:inositol phosphate-mediated signaling; IDA:GOC. DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:UniProtKB. DR GO; GO:0009791; P:post-embryonic development; IMP:MGI. DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:UniProtKB. DR GO; GO:0001666; P:response to hypoxia; IDA:BHF-UCL. DR GO; GO:0050882; P:voluntary musculoskeletal movement; IMP:MGI. DR Gene3D; 1.25.10.30; -; 2. DR InterPro; IPR014821; Ins145_P3_rcpt. DR InterPro; IPR000493; InsP3_rcpt-bd. DR InterPro; IPR005821; Ion_trans_dom. DR InterPro; IPR016093; MIR_motif. DR InterPro; IPR013662; RIH_assoc-dom. DR InterPro; IPR000699; RIH_dom. DR InterPro; IPR015925; Ryanodine_recept-rel. DR PANTHER; PTHR13715; PTHR13715; 1. 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; Alternative splicing; Apoptosis; Calcium; KW Calcium channel; Calcium transport; Complete proteome; KW Direct protein sequencing; Endoplasmic reticulum; Ion channel; KW Ion transport; Isopeptide bond; Ligand-gated ion channel; Membrane; KW Phosphoprotein; Receptor; Reference proteome; Repeat; Transmembrane; KW Transmembrane helix; Transport; Ubl conjugation. FT CHAIN 1 2749 Inositol 1,4,5-trisphosphate receptor FT type 1. FT /FTId=PRO_0000153921. FT TOPO_DOM 1 2273 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 2274 2294 Helical. {ECO:0000255}. FT TOPO_DOM 2295 2305 Lumenal. {ECO:0000255}. FT TRANSMEM 2306 2326 Helical. {ECO:0000255}. FT TOPO_DOM 2327 2352 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 2353 2373 Helical. {ECO:0000255}. FT TOPO_DOM 2374 2396 Lumenal. {ECO:0000255}. FT TRANSMEM 2397 2417 Helical. {ECO:0000255}. FT TOPO_DOM 2418 2439 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 2440 2460 Helical. {ECO:0000255}. FT TOPO_DOM 2461 2569 Lumenal. {ECO:0000255}. FT TRANSMEM 2570 2590 Helical. {ECO:0000255}. FT TOPO_DOM 2591 2749 Cytoplasmic. {ECO:0000255}. FT DOMAIN 112 166 MIR 1. {ECO:0000255|PROSITE- FT ProRule:PRU00131}. FT DOMAIN 173 223 MIR 2. {ECO:0000255|PROSITE- FT ProRule:PRU00131}. FT DOMAIN 231 287 MIR 3. {ECO:0000255|PROSITE- FT ProRule:PRU00131}. FT DOMAIN 294 373 MIR 4. {ECO:0000255|PROSITE- FT ProRule:PRU00131}. FT DOMAIN 379 435 MIR 5. {ECO:0000255|PROSITE- FT ProRule:PRU00131}. FT REGION 265 269 Inositol 1,4,5-trisphosphate binding. FT REGION 508 511 Inositol 1,4,5-trisphosphate binding. FT REGION 567 569 Inositol 1,4,5-trisphosphate binding. FT REGION 2463 2528 Interaction with ERP44. FT MOD_RES 482 482 Phosphotyrosine. {ECO:0000255}. FT MOD_RES 1588 1588 Phosphoserine. FT {ECO:0000269|PubMed:18630941}. FT MOD_RES 1755 1755 Phosphoserine; by PKA. {ECO:0000255}. FT MOD_RES 2655 2655 Phosphotyrosine. {ECO:0000255}. FT CROSSLNK 916 916 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000250}. FT CROSSLNK 962 962 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000250}. FT CROSSLNK 1571 1571 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000250}. FT CROSSLNK 1771 1771 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000250}. FT CROSSLNK 1884 1884 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000250}. FT CROSSLNK 1885 1885 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000250}. FT CROSSLNK 1886 1886 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000250}. FT CROSSLNK 1901 1901 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000250}. FT CROSSLNK 1924 1924 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000250}. FT CROSSLNK 2118 2118 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000250}. FT CROSSLNK 2257 2257 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000250}. FT VAR_SEQ 318 332 Missing (in isoform 2, isoform 4, isoform FT 6 and isoform 8). {ECO:0000305}. FT /FTId=VSP_002691. FT VAR_SEQ 1692 1714 Missing (in isoform 7 and isoform 8). FT {ECO:0000305}. FT /FTId=VSP_002692. FT VAR_SEQ 1715 1715 Missing (in isoform 3, isoform 4, isoform FT 5, isoform 6, isoform 7 and isoform 8). FT {ECO:0000305}. FT /FTId=VSP_002693. FT VAR_SEQ 1716 1731 Missing (in isoform 5, isoform 6, isoform FT 7 and isoform 8). {ECO:0000305}. FT /FTId=VSP_002694. FT MUTAGEN 167 167 Y->A: Nearly abolishes calcium flux. FT {ECO:0000269|PubMed:20813840}. FT MUTAGEN 168 168 K->A: Reduces calcium flux by about 50%. FT {ECO:0000269|PubMed:20813840}. FT MUTAGEN 169 169 L->A: Reduces calcium flux by about 50%. FT MUTAGEN 267 267 T->A: Abolishes inositol 1,4,5- FT triphosphate binding. FT {ECO:0000269|PubMed:12442173}. FT MUTAGEN 567 567 Y->A,F: Abolishes inositol 1,4,5- FT triphosphate binding. FT {ECO:0000269|PubMed:12442173}. FT MUTAGEN 2496 2496 C->S: No effect on channel activity. FT Significant decrease of interaction with FT ERP44. Complete loss of channel FT inhibition by ERP44. FT {ECO:0000269|PubMed:15652484}. FT MUTAGEN 2504 2504 C->S: No effect on channel activity. FT Significant decrease of interaction with FT ERP44. Complete loss of channel FT inhibition by ERP44. FT {ECO:0000269|PubMed:15652484}. FT MUTAGEN 2527 2527 C->S: Complete loss of channel activity. FT Significant decrease of interaction with FT ERP44. {ECO:0000269|PubMed:15652484}. FT CONFLICT 1264 1264 N -> K (in Ref. 1; CAA33433). FT {ECO:0000305}. FT CONFLICT 2675 2675 P -> L (in Ref. 1; CAA33433). FT {ECO:0000305}. FT STRAND 14 23 {ECO:0000244|PDB:1XZZ}. FT STRAND 25 30 {ECO:0000244|PDB:1XZZ}. FT STRAND 36 39 {ECO:0000244|PDB:1XZZ}. FT HELIX 41 43 {ECO:0000244|PDB:1XZZ}. FT STRAND 46 48 {ECO:0000244|PDB:1XZZ}. FT HELIX 53 56 {ECO:0000244|PDB:1XZZ}. FT STRAND 58 61 {ECO:0000244|PDB:1XZZ}. FT HELIX 67 74 {ECO:0000244|PDB:1XZZ}. FT HELIX 86 109 {ECO:0000244|PDB:1XZZ}. FT TURN 110 112 {ECO:0000244|PDB:1XZZ}. FT STRAND 120 125 {ECO:0000244|PDB:1XZZ}. FT TURN 126 129 {ECO:0000244|PDB:1XZZ}. FT STRAND 130 139 {ECO:0000244|PDB:1XZZ}. FT STRAND 141 143 {ECO:0000244|PDB:1XZZ}. FT STRAND 146 154 {ECO:0000244|PDB:1XZZ}. FT HELIX 157 159 {ECO:0000244|PDB:1XZZ}. FT STRAND 161 167 {ECO:0000244|PDB:1XZZ}. FT STRAND 181 189 {ECO:0000244|PDB:1XZZ}. FT STRAND 193 199 {ECO:0000244|PDB:1XZZ}. FT STRAND 201 205 {ECO:0000244|PDB:1XZZ}. FT STRAND 207 213 {ECO:0000244|PDB:1XZZ}. FT STRAND 217 223 {ECO:0000244|PDB:1XZZ}. FT STRAND 239 244 {ECO:0000244|PDB:1N4K}. FT TURN 245 248 {ECO:0000244|PDB:1N4K}. FT STRAND 249 255 {ECO:0000244|PDB:1N4K}. FT STRAND 257 265 {ECO:0000244|PDB:1N4K}. FT STRAND 269 271 {ECO:0000244|PDB:1N4K}. FT HELIX 272 274 {ECO:0000244|PDB:1N4K}. FT HELIX 278 280 {ECO:0000244|PDB:1N4K}. FT STRAND 282 286 {ECO:0000244|PDB:1N4K}. FT STRAND 303 307 {ECO:0000244|PDB:1N4K}. FT TURN 308 310 {ECO:0000244|PDB:1N4K}. FT STRAND 313 318 {ECO:0000244|PDB:1N4K}. FT STRAND 353 359 {ECO:0000244|PDB:1N4K}. FT HELIX 364 366 {ECO:0000244|PDB:1N4K}. FT STRAND 368 371 {ECO:0000244|PDB:1N4K}. FT STRAND 388 392 {ECO:0000244|PDB:1N4K}. FT TURN 393 396 {ECO:0000244|PDB:1N4K}. FT STRAND 397 406 {ECO:0000244|PDB:1N4K}. FT STRAND 409 412 {ECO:0000244|PDB:1N4K}. FT STRAND 415 423 {ECO:0000244|PDB:1N4K}. FT STRAND 430 434 {ECO:0000244|PDB:1N4K}. FT HELIX 437 461 {ECO:0000244|PDB:1N4K}. FT HELIX 467 484 {ECO:0000244|PDB:1N4K}. FT TURN 485 487 {ECO:0000244|PDB:1N4K}. FT HELIX 495 499 {ECO:0000244|PDB:1N4K}. FT HELIX 504 512 {ECO:0000244|PDB:1N4K}. FT HELIX 515 524 {ECO:0000244|PDB:1N4K}. FT HELIX 525 527 {ECO:0000244|PDB:1N4K}. FT HELIX 547 564 {ECO:0000244|PDB:1N4K}. FT HELIX 568 585 {ECO:0000244|PDB:1N4K}. FT HELIX 589 599 {ECO:0000244|PDB:1N4K}. SQ 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 //