ITPR2_MOUSE
ID ITPR2_MOUSE Reviewed; 2701 AA.
AC Q9Z329; B2KF91; P70226; Q5DWM3; Q5DWM5; Q61744; Q8R3B0;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 185.
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=Inositol 1,4,5-trisphosphate type V receptor;
DE AltName: Full=Type 2 inositol 1,4,5-trisphosphate receptor;
DE Short=Type 2 InsP3 receptor;
GN Name=Itpr2; Synonyms=Itpr5;
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] (ISOFORMS 1 AND 3), FUNCTION, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 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 [MRNA] (ISOFORM 2).
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 [MRNA], AND FUNCTION.
RX PubMed=20189985; DOI=10.1074/jbc.m109.096016;
RA Tovey S.C., Dedos S.G., Rahman T., Taylor E.J., Pantazaka E., Taylor C.W.;
RT "Regulation of inositol 1,4,5-trisphosphate receptors by cAMP independent
RT of cAMP-dependent protein kinase.";
RL J. Biol. Chem. 285:12979-12989(2010).
RN [4]
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., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1290-2701.
RC STRAIN=Czech II; 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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1693-2701 (ISOFORM 1).
RC STRAIN=C3H/HeJ; TISSUE=Embryo;
RX PubMed=8063813; DOI=10.1016/s0021-9258(17)31861-6;
RA De Smedt H., Missiaen L., Parys J.B., Bootman M.D., Mertens L.,
RA Van Den Bosch L., Casteels R.;
RT "Determination of relative amounts of inositol trisphosphate receptor mRNA
RT isoforms by ratio polymerase chain reaction.";
RL J. Biol. Chem. 269:21691-21698(1994).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2238-2646 (ISOFORM 1).
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-937, 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 [10]
RP PHOSPHORYLATION AT SER-937, FUNCTION, AND MUTAGENESIS OF SER-937; SER-990;
RP SER-1190; SER-1351; SER-1581 AND SER-2633.
RX PubMed=19608738; DOI=10.1074/jbc.m109.010132;
RA Betzenhauser M.J., Fike J.L., Wagner L.E. II, Yule D.I.;
RT "Protein kinase A increases type-2 inositol 1,4,5-trisphosphate receptor
RT activity by phosphorylation of serine 937.";
RL J. Biol. Chem. 284:25116-25125(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-937; SER-1709; SER-1711;
RP SER-2633 AND SER-2636, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [12]
RP DISRUPTION PHENOTYPE.
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).
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.
CC {ECO:0000269|PubMed:15632133, ECO:0000269|PubMed:19608738,
CC ECO:0000269|PubMed:20189985}.
CC -!- FUNCTION: Isoform 3 has neither inositol 1,4,5-trisphosphate binding
CC activity nor calcium releasing activity. {ECO:0000269|PubMed:15632133}.
CC -!- SUBUNIT: Homotetramer. Interacts with CABP1. Interacts with BOK;
CC regulates ITPR2 expression. Interacts with BCL2L10 (By similarity).
CC Interacts with TRPC4 (By similarity). {ECO:0000250|UniProtKB:P29995,
CC ECO:0000250|UniProtKB:Q14571}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15632133}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15632133}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Long;
CC IsoId=Q9Z329-1; Sequence=Displayed;
CC Name=2; Synonyms=Short, TIPR;
CC IsoId=Q9Z329-2; Sequence=VSP_002701, VSP_002702;
CC Name=3; Synonyms=Itpr2v;
CC IsoId=Q9Z329-3; Sequence=VSP_016026;
CC -!- TISSUE SPECIFICITY: Isoforms 1 and 3 are widely expressed. Isoform 2 is
CC found in skeletal muscle and heart. {ECO:0000269|PubMed:15632133}.
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:0000269|PubMed:19608738}.
CC -!- DISRUPTION PHENOTYPE: There is a 3-fold reduction in the number of
CC pilocarpine-responsive sweat glands in knockout animals. The sweat
CC glands of these animals show a significant reduction in Ca(2+) response
CC following acetylcholine stimulation compared with those of wild-type
CC animals. The Itpr2-null animals retained some residual sweat
CC production, in contrast to the human phenotype of anhidrosis. This
CC phenotypic discrepancy may be due to differences between humans and
CC mice in the expression of the 3 ITPR isoforms, as well as to the
CC different stimuli used to provoke sweat production in Itpr2-null
CC animals. {ECO:0000269|PubMed:25329695}.
CC -!- SIMILARITY: Belongs to the InsP3 receptor family. {ECO:0000305}.
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DR EMBL; AB182288; BAD90682.1; -; mRNA.
DR EMBL; AB182290; BAD90684.1; -; mRNA.
DR EMBL; AB012393; BAA33960.1; -; mRNA.
DR EMBL; GU980658; ADG01867.1; -; mRNA.
DR EMBL; CU207302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU207317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU207333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466572; EDL10703.1; -; Genomic_DNA.
DR EMBL; BC025805; AAH25805.1; -; mRNA.
DR EMBL; Z71173; CAA94861.1; -; mRNA.
DR EMBL; Z33908; CAA83957.1; -; mRNA.
DR CCDS; CCDS39708.1; -. [Q9Z329-3]
DR CCDS; CCDS39709.1; -. [Q9Z329-1]
DR PIR; I48607; I48607.
DR RefSeq; NP_034716.1; NM_010586.2. [Q9Z329-3]
DR RefSeq; NP_064307.2; NM_019923.4. [Q9Z329-1]
DR SMR; Q9Z329; -.
DR BioGRID; 200848; 3.
DR CORUM; Q9Z329; -.
DR STRING; 10090.ENSMUSP00000049584; -.
DR iPTMnet; Q9Z329; -.
DR PhosphoSitePlus; Q9Z329; -.
DR EPD; Q9Z329; -.
DR jPOST; Q9Z329; -.
DR MaxQB; Q9Z329; -.
DR PaxDb; Q9Z329; -.
DR PeptideAtlas; Q9Z329; -.
DR PRIDE; Q9Z329; -.
DR ProteomicsDB; 269014; -. [Q9Z329-1]
DR ProteomicsDB; 269015; -. [Q9Z329-2]
DR ProteomicsDB; 269016; -. [Q9Z329-3]
DR Antibodypedia; 24309; 126 antibodies from 30 providers.
DR DNASU; 16439; -.
DR Ensembl; ENSMUST00000053273; ENSMUSP00000049584; ENSMUSG00000030287. [Q9Z329-1]
DR Ensembl; ENSMUST00000079573; ENSMUSP00000078526; ENSMUSG00000030287. [Q9Z329-3]
DR GeneID; 16439; -.
DR KEGG; mmu:16439; -.
DR UCSC; uc009erw.2; mouse. [Q9Z329-1]
DR UCSC; uc009erx.2; mouse. [Q9Z329-3]
DR CTD; 3709; -.
DR MGI; MGI:99418; Itpr2.
DR VEuPathDB; HostDB:ENSMUSG00000030287; -.
DR eggNOG; KOG3533; Eukaryota.
DR GeneTree; ENSGT00940000156039; -.
DR HOGENOM; CLU_000206_1_0_1; -.
DR InParanoid; Q9Z329; -.
DR OMA; NHNSELQ; -.
DR PhylomeDB; Q9Z329; -.
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 BioGRID-ORCS; 16439; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Itpr2; mouse.
DR PRO; PR:Q9Z329; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9Z329; protein.
DR Bgee; ENSMUSG00000030287; Expressed in ileal epithelium and 242 other tissues.
DR ExpressionAtlas; Q9Z329; baseline and differential.
DR Genevisible; Q9Z329; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005938; C:cell cortex; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043209; C:myelin sheath; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:MGI.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISO:MGI.
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: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:MGI.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0006816; P:calcium ion transport; IDA:MGI.
DR GO; GO:0071320; P:cellular response to cAMP; IDA:UniProtKB.
DR GO; GO:0071361; P:cellular response to ethanol; IMP:MGI.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; ISO:MGI.
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 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_0000153925"
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..2520
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2521..2541
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2542..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 1135..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..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:0000269|PubMed:19608738,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 1160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14571"
FT MOD_RES 1709
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1711
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2607
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 2633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2636
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 175
FT /note="N -> NDMGAVI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9729462"
FT /id="VSP_002701"
FT VAR_SEQ 176..1281
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9729462"
FT /id="VSP_002702"
FT VAR_SEQ 176..208
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15632133"
FT /id="VSP_016026"
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 MUTAGEN 937
FT /note="S->A: Abolishes PKA-mediated phosphorylation. No
FT enhanced calcium release. Abolishes PKA-mediated
FT phosphorylation: When associated with A-990; A-1190; A-1351
FT and A-1581."
FT /evidence="ECO:0000269|PubMed:19608738"
FT MUTAGEN 990
FT /note="S->A: No effect on PKA-mediated phosphorylation.
FT Abolishes PKA-mediated phosphorylation: When associated
FT with A-937; A-1190; A-1351 and A-1581."
FT /evidence="ECO:0000269|PubMed:19608738"
FT MUTAGEN 1190
FT /note="S->A: No effect on PKA-mediated phosphorylation.
FT Abolishes PKA-mediated phosphorylation: When associated
FT with A-937; A-990; A-1351 and A-1581."
FT /evidence="ECO:0000269|PubMed:19608738"
FT MUTAGEN 1351
FT /note="S->A: No effect on PKA-mediated phosphorylation.
FT Abolishes PKA-mediated phosphorylation: When associated
FT with A-937; A-990; A-1190 and A-1581."
FT /evidence="ECO:0000269|PubMed:19608738"
FT MUTAGEN 1581
FT /note="S->A: No effect on PKA-mediated phosphorylation.
FT Abolishes PKA-mediated phosphorylation: When associated
FT with A-937; A-990; A-1190 and A-1351."
FT /evidence="ECO:0000269|PubMed:19608738"
FT MUTAGEN 2633
FT /note="S->A: No effect on PKA-mediated phosphorylation.
FT Enhanced calcium release on PKA activation."
FT /evidence="ECO:0000269|PubMed:19608738"
FT CONFLICT 1710
FT /note="I -> V (in Ref. 6; AAH25805)"
FT /evidence="ECO:0000305"
FT CONFLICT 1729
FT /note="S -> G (in Ref. 6; AAH25805)"
FT /evidence="ECO:0000305"
FT CONFLICT 1738
FT /note="K -> T (in Ref. 6; AAH25805)"
FT /evidence="ECO:0000305"
FT CONFLICT 2196
FT /note="F -> L (in Ref. 7; CAA94861)"
FT /evidence="ECO:0000305"
FT CONFLICT 2223
FT /note="S -> P (in Ref. 6; AAH25805)"
FT /evidence="ECO:0000305"
FT CONFLICT 2265
FT /note="V -> A (in Ref. 6; AAH25805, 7; CAA94861 and 8;
FT CAA83957)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2701 AA; 307475 MW; E7853104F0BD9B08 CRC64;
MSDKMSSFLY IGDIVSLYAE GSVNGFISTL GLVDDRCVVH PEAGDLANPP KKFRDCLFKV
CPMNRYSAQK QYWKAKQAKQ GNHTEAALLK KLQHAAELEQ KQNESENRKL LGEIVKYSNV
IQLLHIKSNK YLTVNKRLPA LLEKNAMRVS LDAAGNEGSW FYIHPFWKLR SEGDNIVVGD
KVVLMPVNAG QPLHASNVEL LDNPGCKEVN AVNCNTSWKI TLFMKFSSYR EDVLKGGDVV
RLFHAEQEKF LTCDDYEKKQ HIFLRTTLRQ SATSATSSKA LWEIEVVHHD PCRGGAGQWN
SLFRFKHLAT GNYLAAELNP DYRDAQNEGK NVKDGEIPTP KKKRQAGEKI MYTLVSVPHG
NDIASLFELD ATTLQRADCL VPRNSYVRLR HLCTNTWVTS TTIPIDTEEE RPVMLKIGTC
QTKEDKEAFA IVCVPLSEVR DLDFANDANK VLATTVKKLE NGSITQNERR FVTKLLEDLI
FFVADVTNNG QDVLDVVITK PNRERQKLMR EQNILAQVFG ILKAPFKEKA GEGSMLRLED
LGDQRYAPYK YVLRLCYRVL RHSQQDYRKN QEYIAKNFCV MQSQIGYDIL AEDTITALLH
NNRKLLEKHI TAKEIETFVS LLRRNREPRF LDYLSDLCVS NSTAIPVTQE LICKFMLSPG
NADILIQTKL VSMQVENPME SSILPDDIDD EEVWLYWIDS NKEPHGKAIR HLAQEAREGT
KADLEVLTYY RYQLNLFARM CLDRQYLAIN QISTQLSVDL ILRCVSDESL PFDLRASFCR
LMLHMHVDRD PQESVVPVRY ARLWTEIPTK ITIHEYDSIT DSSRNDMKRK FALTMEFVEE
YLKEVVNQPF PFGDKEKNKL TFEVVHLARN LIYFGFYSFS ELLRLTRTLL AILDIVQAPM
SSYFERLSKF QDGSNNVMRT IHGVGEMMTQ MVLSRGSIFP VSVPDAQPIV HPSKQASPGE
QEDVTVMDTK LKVIEILQFI LSVRLDYRIS YMLSIYKKEF GDNNDNGDPS ASGTPDTLLP
SALVPDIDEI AAQAETMFAG RKEKTPVQLD DEGGRTFLRV LIHLIMHDYA PLLSGALQLL
FKHFSQRAEV LQAFKQVQLL VSNQDVDNYK QIKADLDQLR LTVEKSELWV EKSGSYENGD
VGEGQAKGGE EANEESNLLS PVQDGAKTPQ IDSNKGNNYR IVKEILIRLS KLCVQNKKCR
NQHQRLLKNM GAHSVVLDLL QIPYEKTDEK MNEVMDLAHT FLQNFCRGNP QNQVLLHKHL
NLFLTPGLLE AETMRHIFMN NYHLCNEISE RVVQHFVHCI ETHGRHVEYL RFLQTIVKAD
GKYVKKCQDM VMTELINGGE DVLIFYNDRA SFPILLNMMC SERARGDESG PLAYHITLVE
LLAACTEGKN VYTEIKCNSL LPLDDIVRVV THDDCIPEVK IAYVNFVNHC YVDTEVEMKE
IYTSNHIWKL FENFLVDMAR VCNTTTDRKH ADTFLERCVT ESVMNIVSGF FNSPFSDNST
SLQTHQPVFI QLLQSAFRIY NCTWPNPAQK ASVESCIRAL AEVAKNRGIA IPVDLDSQVN
TLFMKNHSST VQRAAMGWRL SARSGPRFKE ALGGPAWDYR NIIEKLQDVV ASLEQQFSPM
MQAEFSVLVD VLYSPELLFP EGSDARIRCG AFMSKLINHT KKLMEKEEKL CIKILQTLRE
MLEKKDSFME EGSTLRRILL NRYFKGDHSI SVNGPLSGAY AKTAQVGGSF SGQDSDKKGI
SMSDIQCLLD KEGASELVID VIVNTKNDRI FSEGILLGIA LLEGGNTQTQ YSFYQQLHEQ
KKSEKFFKVL YDRMKAAQKE IRSTVTVNTI DLGSKKREED SDVMALGPRM RVRDSSLHLR
EGMKGQLTEA SSATSKAYCV YRREMDPEID TMCPGQEAGS AEEKSAEEVT MSPAITIMRP
ILRFLQLLCE NHNRELQNFL RNQNNKTNYN LVCETLQFLD CICGSTTGGL GLLGLYINER
NVALVNQTLE SLTEYCQGPC HENQTCIATH ESNGIDIIIA LILNDINPLG KYRMDLVLQL
KNNASKLLLA IMESRHDSEN AERILFNMRP RELVDVMKNA YNQGLECDHG DEEGGDDGVS
PKDVGHNIYI LAHQLARHNK LLQQMLKPGS DPEEGDEALK YYANHTAQIE IVRHDRTMEQ
IVFPVPNICE FLTRESKYRV FNTTERDEQG SKVNDFFQQT EDLYNEMKWQ KKIRNNPALF
WFSRHISLWG SISFNLAVFI NLAVALFYPF GDDGDEGTLS PMFSVLLWVA VAICTSMLFF
FSKPVGIRPF LVSVMLRSIY TIGLGPTLIL LGAANLCNKI VFLVSFVGNR GTFTRGYRAV
ILDMAFLYHV AYVLVCMLGL FVHEFFYSFL LFDLVYREET LLNVIKSVTR NGRSIILTAV
LALILVYLFS IIGFLFLKDD FTMEVDRLKN RTPVTGNHGV PTMTLSSMME TCQKENCSPT
IPSSNTAGEE GEDGIERTCD TLLMCIVTVL NQGLRNGGGV GDVLRRPSKD EPLFAARVVY
DLLFFFIVII IVLNLIFGVI IDTFADLRSE KQKKEEILKT TCFICGLERD KFDNKTVSFE
EHIKSEHNMW HYLYFIVLVK VKDPTEYTGP ESYVAQMITE KNLDWFPRMR AMSLVSNEGD
SEQNEIRNLQ EKLESTMSLV KQLSGQLAEL KEQMTEQRKN KQRLGFLGSN TPHVNHHMPP
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