ITPR3_MOUSE
ID ITPR3_MOUSE Reviewed; 2670 AA.
AC P70227; Q5DWM4; Q8CED5; Q91Z08;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 3.
DT 03-AUG-2022, entry version 180.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-507 AND ARG-510.
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=15632133; DOI=10.1074/jbc.m413824200;
RA Iwai M., Tateishi Y., Hattori M., Mizutani A., Nakamura T., Futatsugi A.,
RA Inoue T., Furuichi T., Michikawa T., Mikoshiba K.;
RT "Molecular cloning of mouse type 2 and type 3 inositol 1,4,5-trisphosphate
RT receptors and identification of a novel type 2 receptor splice variant.";
RL J. Biol. Chem. 280:10305-10317(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1857-2670.
RC STRAIN=C57BL/6J; TISSUE=Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2181-2670.
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2406-2609.
RC TISSUE=Placenta;
RX PubMed=1374893; DOI=10.1073/pnas.89.10.4265;
RA Ross C.A., Danoff S.K., Schell M.J., Snyder S.H., Ullrich A.;
RT "Three additional inositol 1,4,5-trisphosphate receptors: molecular cloning
RT and differential localization in brain and peripheral tissues.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:4265-4269(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2433-2629.
RC STRAIN=C3H/HeJ; TISSUE=Embryo;
RX PubMed=9065779; DOI=10.1042/bj3220575;
RA De Smedt H., Missiaen L., Parys J.B., Henning R.H., Sienaert I.,
RA Vanlingen S., Gijsens A., Himpens B., Casteels R.;
RT "Isoform diversity of the inositol trisphosphate receptor in cell types of
RT mouse origin.";
RL Biochem. J. 322:575-583(1997).
RN [6]
RP INTERACTION WITH SIGMAR1.
RX PubMed=11149946; DOI=10.1073/pnas.98.2.491;
RA Hayashi T., Su T.-P.;
RT "Regulating ankyrin dynamics: roles of sigma-1 receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:491-496(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-916, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-916; SER-934; SER-1832 AND
RP SER-2669, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH IRAG2.
RX PubMed=20071408; DOI=10.1093/chemse/bjp097;
RA Shindo Y., Kim M.R., Miura H., Yuuki T., Kanda T., Hino A., Kusakabe Y.;
RT "Lrmp/Jaw1 is expressed in sweet, bitter, and umami receptor-expressing
RT cells.";
RL Chem. Senses 35:171-177(2010).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF TRP-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 mediates
RT functional coupling between ligand binding and channel opening.";
RL J. Biol. Chem. 285:36081-36091(2010).
RN [11]
RP FUNCTION, INTERACTION WITH PML AND AKT1, PHOSPHORYLATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=21030605; DOI=10.1126/science.1189157;
RA Giorgi C., Ito K., Lin H.K., Santangelo C., Wieckowski M.R.,
RA Lebiedzinska M., Bononi A., Bonora M., Duszynski J., Bernardi R.,
RA Rizzuto R., Tacchetti C., Pinton P., Pandolfi P.P.;
RT "PML regulates apoptosis at endoplasmic reticulum by modulating calcium
RT release.";
RL Science 330:1247-1251(2010).
RN [12]
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 protein in
RT T and B lymphocytes.";
RL FEBS Open Bio 2:255-259(2012).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-224.
RX PubMed=20843799; DOI=10.1074/jbc.m110.140160;
RA Chan J., Yamazaki H., Ishiyama N., Seo M.D., Mal T.K., Michikawa T.,
RA Mikoshiba K., Ikura M.;
RT "Structural studies of inositol 1,4,5-trisphosphate receptor: coupling
RT ligand binding to channel gating.";
RL J. Biol. Chem. 285:36092-36099(2010).
CC -!- FUNCTION: Receptor for inositol 1,4,5-trisphosphate, a second messenger
CC that mediates the release of intracellular calcium.
CC {ECO:0000269|PubMed:20813840, ECO:0000269|PubMed:21030605}.
CC -!- SUBUNIT: Homotetramer. Interacts with TRPC1, TRPC3, TRPC4. Interacts
CC with TRPV4 (By similarity). Interacts with SIGMAR1 (PubMed:11149946).
CC Interacts with AKT1 and PML (PubMed:21030605). Interacts with IRAG2
CC (via coiled-coil domain) (PubMed:20071408). Interacts with CABP1 (By
CC similarity). Interacts with TMBIM4/LFG4 (By similarity). Interacts with
CC CEMIP (By similarity). Interacts with TESPA1 (PubMed:23650607).
CC Interacts with TMEM203 (By similarity). Interacts with BOK; regulates
CC ITPR3 expression (By similarity). Interacts with BCL2L10 (By
CC similarity). {ECO:0000250|UniProtKB:Q14573,
CC ECO:0000250|UniProtKB:Q63269, ECO:0000269|PubMed:11149946,
CC ECO:0000269|PubMed:20071408, ECO:0000269|PubMed:21030605,
CC ECO:0000269|PubMed:23650607}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15632133, ECO:0000269|PubMed:21030605}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:15632133,
CC ECO:0000269|PubMed:21030605}.
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 (By similarity).
CC Phosphorylated by AKT1 on serine and/or threonine residues.
CC {ECO:0000250, ECO:0000269|PubMed:21030605}.
CC -!- SIMILARITY: Belongs to the InsP3 receptor family. {ECO:0000305}.
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DR EMBL; AB182289; BAD90683.1; -; mRNA.
DR EMBL; AK028491; BAC25977.1; -; mRNA.
DR EMBL; BC010323; AAH10323.1; -; mRNA.
DR EMBL; M90088; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; Z71174; CAA94862.1; -; mRNA.
DR CCDS; CCDS28560.1; -.
DR RefSeq; NP_542120.2; NM_080553.3.
DR PDB; 3JRR; X-ray; 1.90 A; A/B=1-224.
DR PDBsum; 3JRR; -.
DR AlphaFoldDB; P70227; -.
DR SMR; P70227; -.
DR BioGRID; 200849; 11.
DR IntAct; P70227; 2.
DR STRING; 10090.ENSMUSP00000038150; -.
DR iPTMnet; P70227; -.
DR PhosphoSitePlus; P70227; -.
DR EPD; P70227; -.
DR jPOST; P70227; -.
DR MaxQB; P70227; -.
DR PaxDb; P70227; -.
DR PeptideAtlas; P70227; -.
DR PRIDE; P70227; -.
DR ProteomicsDB; 269413; -.
DR Antibodypedia; 1294; 159 antibodies from 27 providers.
DR DNASU; 16440; -.
DR Ensembl; ENSMUST00000049308; ENSMUSP00000038150; ENSMUSG00000042644.
DR GeneID; 16440; -.
DR KEGG; mmu:16440; -.
DR UCSC; uc008bfi.2; mouse.
DR CTD; 3710; -.
DR MGI; MGI:96624; Itpr3.
DR VEuPathDB; HostDB:ENSMUSG00000042644; -.
DR eggNOG; KOG3533; Eukaryota.
DR GeneTree; ENSGT00940000157078; -.
DR HOGENOM; CLU_000206_1_0_1; -.
DR InParanoid; P70227; -.
DR OMA; WLMWTDK; -.
DR OrthoDB; 94996at2759; -.
DR PhylomeDB; P70227; -.
DR TreeFam; TF312815; -.
DR Reactome; R-MMU-114508; Effects of PIP2 hydrolysis.
DR Reactome; R-MMU-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-MMU-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-MMU-5578775; Ion homeostasis.
DR Reactome; R-MMU-9717207; Sensory perception of sweet, bitter, and umami (glutamate) taste.
DR Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR BioGRID-ORCS; 16440; 5 hits in 77 CRISPR screens.
DR ChiTaRS; Itpr3; mouse.
DR EvolutionaryTrace; P70227; -.
DR PRO; PR:P70227; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P70227; protein.
DR Bgee; ENSMUSG00000042644; Expressed in molar tooth and 183 other tissues.
DR Genevisible; P70227; MM.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0005903; C:brush border; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0005640; C:nuclear outer membrane; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO: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; ISO:MGI.
DR GO; GO:0015278; F:calcium-release channel activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0043533; F:inositol 1,3,4,5 tetrakisphosphate binding; ISO:MGI.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; ISO:MGI.
DR GO; GO:0005220; F:inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; IDA:UniProtKB.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; ISO:MGI.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0006816; P:calcium ion transport; IDA:MGI.
DR GO; GO:0071320; P:cellular response to cAMP; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
DR GO; GO:0007613; P:memory; IMP:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0051592; P:response to calcium ion; ISO:MGI.
DR GO; GO:0050913; P:sensory perception of bitter taste; IMP:MGI.
DR GO; GO:0050916; P:sensory perception of sweet taste; IMP:MGI.
DR GO; GO:0050917; P:sensory perception of umami taste; IMP:MGI.
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..2670
FT /note="Inositol 1,4,5-trisphosphate receptor type 3"
FT /id="PRO_0000153929"
FT TOPO_DOM 1..2233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2234..2254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2255..2262
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2263..2283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2284..2292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2293..2310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2311..2324
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2325..2345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2346..2367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2368..2388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2389..2495
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2496..2516
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2517..2670
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 1138..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1807..1835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1161
FT /note="Basic and acidic 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 BINDING 507..510
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT BINDING 567..569
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT MOD_RES 916
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 934
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1813
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14573"
FT MOD_RES 1832
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1834
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14573"
FT MOD_RES 2608
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14573"
FT MOD_RES 2669
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 168
FT /note="W->A: Loss of calcium flux."
FT /evidence="ECO:0000269|PubMed:20813840"
FT MUTAGEN 507
FT /note="K->A: Loss of binding activity."
FT /evidence="ECO:0000269|PubMed:15632133"
FT MUTAGEN 510
FT /note="R->A: Loss of binding activity."
FT /evidence="ECO:0000269|PubMed:15632133"
FT CONFLICT 2406..2413
FT /note="SRASPLGM -> FPPSRARR (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 2430
FT /note="D -> E (in Ref. 4; M90088)"
FT /evidence="ECO:0000305"
FT CONFLICT 2447
FT /note="P -> L (in Ref. 4; M90088)"
FT /evidence="ECO:0000305"
FT CONFLICT 2605..2609
FT /note="RAMSL -> LGSTS (in Ref. 4; M90088)"
FT /evidence="ECO:0000305"
FT STRAND 13..29
FT /evidence="ECO:0007829|PDB:3JRR"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:3JRR"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:3JRR"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:3JRR"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:3JRR"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:3JRR"
FT HELIX 66..74
FT /evidence="ECO:0007829|PDB:3JRR"
FT HELIX 84..110
FT /evidence="ECO:0007829|PDB:3JRR"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:3JRR"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:3JRR"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:3JRR"
FT STRAND 131..140
FT /evidence="ECO:0007829|PDB:3JRR"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:3JRR"
FT STRAND 147..155
FT /evidence="ECO:0007829|PDB:3JRR"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:3JRR"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:3JRR"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:3JRR"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:3JRR"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:3JRR"
FT STRAND 204..214
FT /evidence="ECO:0007829|PDB:3JRR"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:3JRR"
SQ SEQUENCE 2670 AA; 304275 MW; 9B5BA808B195C58F CRC64;
MNEMSSFLHI GDIVSLYAEG SVNGFISTLG LVDDRCVVEP AAGDLDNPPK KFRDCLFKVC
PMNRYSAQKQ YWKAKQTKQD KEKIADVVLL QKLQHAAQME QKQNDTENKK VHGDVVKYGS
VIQLLHMKSN KYLTVNKRLP ALLEKNAMRV TLDATGNEGS WLFIQPFWKL RSNGDNVVVG
DKVILNPVNA GQPLHASNYE LSDNAGCKEV NSVNCNTSWK INLFMQFRDH LEEVLKGGDV
VRLFHAEQEK FLTCDEYRGK LQVFLRTTLR QSATSATSSN ALWEVEVVHH DPCRGGAGHW
NGLYRFKHLA TGNYLAAEEN PSYKGDVSDP KAAGLGAQGR TGRRNAGEKI KYRLVAVPHG
NDIASLFELD PTTLQKTDSF VPRNSYVRLR HLCTNTWIQS TNAPIDVEEE RPIRLMLGTC
PTKEDKEAFA IVSVPVSEIR DLDFANDASS MLASAVEKLN EGFISQNDRR FVIQLLEDLV
FFVSDVPNNG QNVLDIMVTK PNRERQKLMR EQNILKQIFG ILKAPFRDKG GEGPLVRLEE
LSDQKNAPYQ YMFRLCYRVL RHSQEDYRKN QEHIAKQFGM MQSQIGYDIL AEDTITALLH
NNRKLLEKHI TKTEVETFVS LVRKNREPRF LDYLSDLCVS NRIAIPVTQE LICKCVLDPK
NSDILIQTEL RPVKEMAQSH EYLSIEYSEE EVWLTWTDRN NEHHEKSVRQ LAQEARAGNA
HDENVLSYYR YQLKLFARMC LDRQYLAIDE ISKQLGVELL FLCMADEMLP FDLRASFCHL
MLHVHVDRDP QELVTPVKFA RLWTEIPTAI TIKDYDSNLN ASRDDKKNKF ASTMEFVEDY
LNNVVSEAVP FANDEKNILT FEVVSLAHNL IYFGFYSFSE LLRLTRTLLG IIDCIQAPAA
MLQAYEEPGG KNVRRSIQGV GHMMSTMVLS RKQSVFGASS LPAGVGVPEQ LDRSKFEDNE
HTVVMETKLK ILEILQFILN VRLDYRISYL LSVFKKEFVE VFPMQDSGAD GTAPAFDSST
ATMNLDRIGE QAEAMFGVGK TSSMLEVDDE GGRMFLRVLL HLTMHDYPSL VSGALQLLFK
HFSQRQEAMH TFKQVQLLIS AQDVENYKVI KSELDRLRTM VEKSELWVDK KGSVKGEEVE
AGATKDKKER PSDEEGFLQP HGEKSSENYQ IVKGILERLN KMCGVGEQMR KKQQRLLKNM
DAHKVMLDLL QIPYDKSDNK MLEILRYTHQ FLQKFCAGNP GNQALLHKHL QLFLTPGLLE
AETMQHIFLN NYQLCSEISE PVLQHFVHLL ATHGRHVQYL DFLHTVIKAE GKYVKKCQDM
IMTELTNAGD DVVVFYNDKA SLAHLLDMMK AARDGVEDHS PLMYHISLVD LLAACAEGKN
VYTEIKCTSL LPLEDVVTVV THEDCITEVK MAYVNFVNHC YVDTEVEMKE IYTSNHIWTL
FENFTLDMAL VCNKREKRLS DPTLEKYVLT VVLDTISAFF SSPFSENSTS LQTHQTIVVQ
LLQSTTRLLE CPWLQQQHKG SVEACVRTLA MVAKSRAILL PMDLDAHMSA LLSSGGSCSA
AAQRSAANYK TATRTFPRVI PTANQWDYKN IIEKLQDIIM ALEERLKPLV QAELSVLVDM
LHWPELLFPE GSEAYQRCES GGFLSKLIRH TKGLMESEEK LCVKVLRTLQ QMLLKKSKFG
DRGNQLRKML LQNYLQNRKS GARGELTDPT GSGLDQDWSA IAATQCRLDK EGATKLVCDL
ITSTKNEKIF QESIGLAIRL LDGGNTEIQK SFYNLMTSDK KSERFFKVLH DRMKRAQQET
KSTVAVNMSD LGSQPREDRE PADPATKGRV SSFSMPSSSR YLLGLGLHRG HDMSERAQNN
EMGTSVLIMR PILRFLQLLC ENHNRDLQNF LRCQNNKTNY NLVCETLQFL DIMCGSTTGG
LGLLGLYINE DNVGLVIQTL ETLTEYCQGP CHENQTCIVT HESNGIDIIT ALILNDISPL
CKYRMDLVLQ LKDNASKLLL ALMESRHDSE NAERILISLR PQELVDVIKK AYLQEEEREN
SEVSPREVGH NIYILALQLS RHNKQLQHLL KPVRRIQEEE AEGISSMLSL NNKQLSQMLK
SSAPAQEEEE DPLAYYENHT SQIEIVRQDR SMEQIVFPVP AICQFLTEET KHRLFTTTEQ
DEQGSKVSDF FDQSSFLHNE MEWQRRLRSM PLIYWFSRRM TLWGSISFNL AVFINIIIAF
FYPYVEGAST GVLGSPLISL LFWILICFSI AALFTKRYSV RPLIVALILR SIYYLGIGPT
LNILGALNLT NKIVFVVSFV GNRGTFIRGY KAMVMDMEFL YHVGYILTSV LGLFAHELFY
SILLFDLIYR EETLFNVIKS VTRNGRSILL TALLALILVY LFSIVGFLFL KDDFILEVDR
LPGNHSRASP LGMPHGAATF MGTCSGDKMD CVSEVSVPEI LEEDEEPDST ERACDTLLMC
IVTVMNHGLR NGGGVGDILR KPSKDESLFP ARVVYDLLFF FIVIIIVLNL IFGVIIDTFA
DLRSEKQKKE EILKTTCFIC GLERDKFDNK TVSFEEHIKL EHNMWNYLYF IVLVRVKNKT
DYTGPESYVA QMIKNKNLDW FPRMRAMSLV SGEGEGEQNE IRILQEKLGS TMKLVSHLTS
QLNELKEQMT EQRKRRQRLG FVDVQNCMSR
