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Database: UniProt
Entry: ITPR3_MOUSE
LinkDB: ITPR3_MOUSE
Original site: 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   13-FEB-2019, entry version 162.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   Futatsugi A., Inoue T., Furuichi T., Michikawa T., Mikoshiba K.;
RT   "Molecular cloning of mouse type 2 and type 3 inositol 1,4,5-
RT   trisphosphate receptors and identification of a novel type 2 receptor
RT   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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: 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
RT   cloning and differential localization in brain and peripheral
RT   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
RT   types of 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
RP   BY 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
RP   AND SER-2669, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [9]
RP   INTERACTION WITH LRMP.
RX   PubMed=20071408; DOI=10.1093/chemse/bjp097;
RA   Shindo Y., Kim M.R., Miura H., Yuuki T., Kanda T., Hino A.,
RA   Kusakabe Y.;
RT   "Lrmp/Jaw1 is expressed in sweet, bitter, and umami receptor-
RT   expressing 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
RT   mediates functional coupling between ligand binding and channel
RT   opening.";
RL   J. Biol. Chem. 285:36081-36091(2010).
RN   [11]
RP   FUNCTION, INTERACTION WITH PML AND AKT1, PHOSPHORYLATION, AND
RP   SUBCELLULAR 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
RT   calcium 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
RT   protein in 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
CC       messenger that mediates the release of intracellular calcium.
CC       {ECO:0000269|PubMed:20813840, ECO:0000269|PubMed:21030605}.
CC   -!- SUBUNIT: Homotetramer. Interacts with TRPC1, TRPC3, TRPC4.
CC       Interacts with TRPV4 (By similarity). Interacts with SIGMAR1
CC       (PubMed:11149946). Interacts with AKT1 and PML (PubMed:21030605).
CC       Interacts with LRMP (via coiled-coil domain) (PubMed:20071408).
CC       Interacts with CABP1 (By similarity). Interacts with TMBIM4/LFG4
CC       (By similarity). Interacts with CEMIP (By similarity). Interacts
CC       with TESPA1 (PubMed:23650607). Interacts with TMEM203 (By
CC       similarity). Interacts with BOK; regulates ITPR3 expression (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-
CC       pass 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}.
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   UniGene; Mm.458106; -.
DR   PDB; 3JRR; X-ray; 1.90 A; A/B=1-224.
DR   PDBsum; 3JRR; -.
DR   ProteinModelPortal; P70227; -.
DR   SMR; P70227; -.
DR   BioGrid; 200849; 5.
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   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   eggNOG; KOG3533; Eukaryota.
DR   eggNOG; ENOG410XR97; LUCA.
DR   GeneTree; ENSGT00940000157078; -.
DR   HOGENOM; HOG000007660; -.
DR   HOVERGEN; HBG052158; -.
DR   InParanoid; P70227; -.
DR   KO; K04960; -.
DR   OMA; SFYNLMT; -.
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-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR   ChiTaRS; Itpr3; mouse.
DR   EvolutionaryTrace; P70227; -.
DR   PRO; PR:P70227; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   Bgee; ENSMUSG00000042644; Expressed in 210 organ(s), highest expression level in zone of skin.
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: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:0006816; P:calcium ion transport; IDA:MGI.
DR   GO; GO:0060402; P:calcium ion transport into cytosol; IDA:UniProtKB.
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:0051291; P:protein heterooligomerization; ISO:MGI.
DR   GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central.
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; IPR015925; Ryanodine_recept-rel.
DR   InterPro; IPR035910; RyR/IP3R_RIH_dom_sf.
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; Calcium; Calcium channel; Calcium transport;
KW   Complete proteome; Endoplasmic reticulum; Ion channel; Ion transport;
KW   Ligand-gated ion channel; Membrane; Phosphoprotein; Receptor;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1   2670       Inositol 1,4,5-trisphosphate receptor
FT                                type 3.
FT                                /FTId=PRO_0000153929.
FT   TOPO_DOM      1   2233       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2234   2254       Helical. {ECO:0000255}.
FT   TOPO_DOM   2255   2262       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2263   2283       Helical. {ECO:0000255}.
FT   TOPO_DOM   2284   2292       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2293   2310       Helical. {ECO:0000255}.
FT   TOPO_DOM   2311   2324       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2325   2345       Helical. {ECO:0000255}.
FT   TOPO_DOM   2346   2367       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2368   2388       Helical. {ECO:0000255}.
FT   TOPO_DOM   2389   2495       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2496   2516       Helical. {ECO:0000255}.
FT   TOPO_DOM   2517   2670       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      113    173       MIR 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      174    224       MIR 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      232    288       MIR 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      295    372       MIR 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      378    434       MIR 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   REGION      266    270       Inositol 1,4,5-trisphosphate binding.
FT   REGION      507    510       Inositol 1,4,5-trisphosphate binding.
FT   REGION      567    569       Inositol 1,4,5-trisphosphate binding.
FT   MOD_RES     916    916       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES     934    934       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1813   1813       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14573}.
FT   MOD_RES    1832   1832       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1834   1834       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14573}.
FT   MOD_RES    2608   2608       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14573}.
FT   MOD_RES    2669   2669       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MUTAGEN     168    168       W->A: Loss of calcium flux.
FT                                {ECO:0000269|PubMed:20813840}.
FT   MUTAGEN     507    507       K->A: Loss of binding activity.
FT                                {ECO:0000269|PubMed:15632133}.
FT   MUTAGEN     510    510       R->A: Loss of binding activity.
FT                                {ECO:0000269|PubMed:15632133}.
FT   CONFLICT   2406   2413       SRASPLGM -> FPPSRARR (in Ref. 4).
FT                                {ECO:0000305}.
FT   CONFLICT   2430   2430       D -> E (in Ref. 4; M90088).
FT                                {ECO:0000305}.
FT   CONFLICT   2447   2447       P -> L (in Ref. 4; M90088).
FT                                {ECO:0000305}.
FT   CONFLICT   2605   2609       RAMSL -> LGSTS (in Ref. 4; M90088).
FT                                {ECO:0000305}.
FT   STRAND       13     29       {ECO:0000244|PDB:3JRR}.
FT   STRAND       35     38       {ECO:0000244|PDB:3JRR}.
FT   HELIX        40     42       {ECO:0000244|PDB:3JRR}.
FT   STRAND       45     47       {ECO:0000244|PDB:3JRR}.
FT   HELIX        52     55       {ECO:0000244|PDB:3JRR}.
FT   STRAND       57     60       {ECO:0000244|PDB:3JRR}.
FT   HELIX        66     74       {ECO:0000244|PDB:3JRR}.
FT   HELIX        84    110       {ECO:0000244|PDB:3JRR}.
FT   TURN        111    113       {ECO:0000244|PDB:3JRR}.
FT   STRAND      121    126       {ECO:0000244|PDB:3JRR}.
FT   TURN        127    130       {ECO:0000244|PDB:3JRR}.
FT   STRAND      131    140       {ECO:0000244|PDB:3JRR}.
FT   STRAND      142    144       {ECO:0000244|PDB:3JRR}.
FT   STRAND      147    155       {ECO:0000244|PDB:3JRR}.
FT   HELIX       158    160       {ECO:0000244|PDB:3JRR}.
FT   STRAND      162    166       {ECO:0000244|PDB:3JRR}.
FT   STRAND      182    187       {ECO:0000244|PDB:3JRR}.
FT   TURN        188    190       {ECO:0000244|PDB:3JRR}.
FT   STRAND      194    201       {ECO:0000244|PDB:3JRR}.
FT   STRAND      204    214       {ECO:0000244|PDB:3JRR}.
FT   STRAND      218    223       {ECO:0000244|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
//
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