JPH2_MOUSE
ID JPH2_MOUSE Reviewed; 696 AA.
AC Q9ET78; Q3U077; Q9ET79;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 17-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Junctophilin-2 {ECO:0000303|PubMed:10949023};
DE Short=JP-2 {ECO:0000303|PubMed:10949023};
DE AltName: Full=Junctophilin type 2 {ECO:0000303|PubMed:10949023};
DE Contains:
DE RecName: Full=Junctophilin-2 N-terminal fragment {ECO:0000303|PubMed:30409805};
DE Short=JP2NT {ECO:0000303|PubMed:30409805};
GN Name=Jph2 {ECO:0000312|MGI:MGI:1891496};
GN Synonyms=Jp2 {ECO:0000303|PubMed:10949023};
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 [GENOMIC DNA / MRNA], DISRUPTION PHENOTYPE, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND FUNCTION.
RC STRAIN=129, and C57BL/6J; TISSUE=Heart;
RX PubMed=10949023; DOI=10.1016/s1097-2765(00)00003-4;
RA Takeshima H., Komazaki S., Nishi M., Iino M., Kangawa K.;
RT "Junctophilins: a novel family of junctional membrane complex proteins.";
RL Mol. Cell 6:11-22(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Spleen;
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 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 [4]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19095005; DOI=10.1016/j.pharmthera.2008.11.004;
RA Yamazaki D., Yamazaki T., Takeshima H.;
RT "New molecular components supporting ryanodine receptor-mediated Ca(2+)
RT release: roles of junctophilin and TRIC channel in embryonic
RT cardiomyocytes.";
RL Pharmacol. Ther. 121:265-272(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-462; THR-470; SER-479;
RP THR-483; SER-593; SER-597 AND SER-613, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, 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 [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=21339484; DOI=10.1161/circulationaha.110.006437;
RA van Oort R.J., Garbino A., Wang W., Dixit S.S., Landstrom A.P., Gaur N.,
RA De Almeida A.C., Skapura D.G., Rudy Y., Burns A.R., Ackerman M.J.,
RA Wehrens X.H.;
RT "Disrupted junctional membrane complexes and hyperactive ryanodine
RT receptors after acute junctophilin knockdown in mice.";
RL Circulation 123:979-988(2011).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [8]
RP PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF 153-VAL--PRO-158 AND
RP 563-ALA--PRO-568.
RX PubMed=26063807; DOI=10.1074/jbc.m115.652396;
RA Guo A., Hall D., Zhang C., Peng T., Miller J.D., Kutschke W., Grueter C.E.,
RA Johnson F.L., Lin R.Z., Song L.S.;
RT "Molecular determinants of Calpain-dependent cleavage of Junctophilin-2
RT protein in cardiomyocytes.";
RL J. Biol. Chem. 290:17946-17955(2015).
RN [9]
RP MUTAGENESIS OF ALA-399.
RX PubMed=28393127; DOI=10.1016/j.jacbts.2016.11.004;
RA Quick A.P., Landstrom A.P., Wang Q., Beavers D.L., Reynolds J.O.,
RA Barreto-Torres G., Tran V., Showell J., Philippen L.E., Morris S.A.,
RA Skapura D., Bos J.M., Pedersen S.E., Pautler R.G., Ackerman M.J.,
RA Wehrens X.H.;
RT "Novel junctophilin-2 mutation A405S is associated with basal septal
RT hypertrophy and diastolic dysfunction.";
RL JACC Basic Transl. Sci. 2:56-67(2017).
RN [10]
RP FUNCTION (JUNCTOPHILIN-2 N-TERMINAL FRAGMENT), SUBCELLULAR LOCATION
RP (JUNCTOPHILIN-2 N-TERMINAL FRAGMENT), INTERACTION WITH MEF2C
RP (JUNCTOPHILIN-2 N-TERMINAL FRAGMENT), PROTEOLYTIC CLEAVAGE, DOMAIN
RP (JUNCTOPHILIN-2 N-TERMINAL FRAGMENT), AND MUTAGENESIS OF 488-LYS--PRO-492.
RX PubMed=30409805; DOI=10.1126/science.aan3303;
RA Guo A., Wang Y., Chen B., Wang Y., Yuan J., Zhang L., Hall D., Wu J.,
RA Shi Y., Zhu Q., Chen C., Thiel W.H., Zhan X., Weiss R.M., Zhan F.,
RA Musselman C.A., Pufall M., Zhu W., Au K.F., Hong J., Anderson M.E.,
RA Grueter C.E., Song L.S.;
RT "E-C coupling structural protein junctophilin-2 encodes a stress-adaptive
RT transcription regulator.";
RL Science 0:0-0(2018).
CC -!- FUNCTION: [Junctophilin-2]: Membrane-binding protein that provides a
CC structural bridge between the plasma membrane and the sarcoplasmic
CC reticulum and is required for normal excitation-contraction coupling in
CC cardiomyocytes (PubMed:10949023, PubMed:19095005, PubMed:21339484).
CC Provides a structural foundation for functional cross-talk between the
CC cell surface and intracellular Ca(2+) release channels by maintaining
CC the 12-15 nm gap between the sarcolemma and the sarcoplasmic reticulum
CC membranes in the cardiac dyads (PubMed:10949023, PubMed:19095005,
CC PubMed:21339484). Necessary for proper intracellular Ca(2+) signaling
CC in cardiac myocytes via its involvement in ryanodine receptor-mediated
CC calcium ion release (PubMed:10949023, PubMed:19095005,
CC PubMed:21339484). Contributes to the construction of skeletal muscle
CC triad junctions (PubMed:10949023). {ECO:0000269|PubMed:10949023,
CC ECO:0000269|PubMed:19095005, ECO:0000269|PubMed:21339484}.
CC -!- FUNCTION: [Junctophilin-2 N-terminal fragment]: Transcription repressor
CC required to safeguard against the deleterious effects of cardiac stress
CC (PubMed:30409805). Generated following cleavage of the Junctophilin-2
CC chain by calpain in response to cardiac stress in cardiomyocytes
CC (PubMed:30409805). Following cleavage and release from the membrane,
CC translocates to the nucleus, binds DNA and represses expression of
CC genes implicated in cell growth and differentiation, hypertrophy,
CC inflammation and fibrosis (PubMed:30409805). Modifies the transcription
CC profile and thereby attenuates pathological remodeling in response to
CC cardiac stress (PubMed:30409805). Probably acts by competing with MEF2
CC transcription factors and TATA-binding proteins (PubMed:30409805).
CC {ECO:0000269|PubMed:30409805}.
CC -!- SUBUNIT: Interacts with TRPC3 (By similarity).
CC {ECO:0000250|UniProtKB:Q9BR39}.
CC -!- SUBUNIT: [Junctophilin-2 N-terminal fragment]: Interacts with MEF2C
CC (PubMed:30409805). {ECO:0000269|PubMed:30409805}.
CC -!- INTERACTION:
CC Q9ET78; G1U2U3: TRPC3; Xeno; NbExp=4; IntAct=EBI-8350389, EBI-10055313;
CC -!- SUBCELLULAR LOCATION: [Junctophilin-2]: Cell membrane
CC {ECO:0000269|PubMed:10949023}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10949023}. Sarcoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10949023}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:10949023}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10949023}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:10949023}. Note=The transmembrane domain is
CC anchored in sarcoplasmic reticulum membrane, while the N-terminal part
CC associates with the plasma membrane (PubMed:10949023). In heart cells,
CC it predominantly associates along Z lines within myocytes
CC (PubMed:10949023). In skeletal muscle, it is specifically localized at
CC the junction of A and I bands (PubMed:10949023).
CC {ECO:0000269|PubMed:10949023}.
CC -!- SUBCELLULAR LOCATION: [Junctophilin-2 N-terminal fragment]: Nucleus
CC {ECO:0000269|PubMed:30409805}. Note=Accumulates in the nucleus of
CC stressed hearts. {ECO:0000269|PubMed:30409805}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in skeletal muscle and heart
CC (PubMed:10949023). Weak expression in stomach and lung
CC (PubMed:10949023). {ECO:0000269|PubMed:10949023}.
CC -!- DEVELOPMENTAL STAGE: At 9.5 dpc, it is expressed in the periphery of
CC cardiac myocytes in the looped cardiac tube of the developing heart
CC (PubMed:10949023). In skeletal muscle, expression increases during
CC muscle maturation (PubMed:10949023). {ECO:0000269|PubMed:10949023}.
CC -!- DOMAIN: [Junctophilin-2]: The MORN (membrane occupation and recognition
CC nexus) repeats contribute to the plasma membrane binding, by
CC interacting with phospholipids. Has affinity for phosphatidylserine,
CC and phosphorylated phosphatidylinositols including PtdIns3P, PtdIns4P,
CC PtdIns5P, PtdIns(3,5)P2 and PtdIns(3,4,5)P3.
CC {ECO:0000250|UniProtKB:Q9BR39}.
CC -!- DOMAIN: [Junctophilin-2 N-terminal fragment]: The bipartite nuclear
CC localization signal (bNLS) and Ala-rich (alanine-rich; ARR) regions are
CC involved in DNA-binding. {ECO:0000269|PubMed:30409805}.
CC -!- PTM: Proteolytically cleaved by calpain in response to cardiac stress
CC (PubMed:26063807). The major cleavage site takes place at the C-
CC terminus and leads to the release of the Junctophilin-2 N-terminal
CC fragment chain (JP2NT) (PubMed:26063807, PubMed:30409805).
CC {ECO:0000269|PubMed:26063807, ECO:0000269|PubMed:30409805}.
CC -!- PTM: Phosphorylation on Ser-165, probably by PKC, affects RYR1-mediated
CC calcium ion release, interaction with TRPC3, and skeletal muscle
CC myotubule development. {ECO:0000250|UniProtKB:Q9BR39}.
CC -!- DISRUPTION PHENOTYPE: Null mice possess cardiomyocytes with
CC deficiencies in the junctional membrane complexes and have abnormal
CC Ca(2+) transients (PubMed:10949023, PubMed:19095005, PubMed:21339484).
CC Mice die from cardiac arrest at 10.5 dpc (PubMed:10949023).
CC {ECO:0000269|PubMed:10949023, ECO:0000269|PubMed:19095005,
CC ECO:0000269|PubMed:21339484}.
CC -!- SIMILARITY: Belongs to the junctophilin family. {ECO:0000305}.
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DR EMBL; AB024447; BAB12044.1; -; mRNA.
DR EMBL; AB024448; BAB12045.1; -; Genomic_DNA.
DR EMBL; AK157145; BAE33978.1; -; mRNA.
DR EMBL; AL589876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS17008.1; -.
DR RefSeq; NP_001192005.1; NM_001205076.1.
DR RefSeq; NP_067541.1; NM_021566.2.
DR RefSeq; XP_006500035.1; XM_006499972.2.
DR AlphaFoldDB; Q9ET78; -.
DR SMR; Q9ET78; -.
DR BioGRID; 208526; 1.
DR IntAct; Q9ET78; 4.
DR STRING; 10090.ENSMUSP00000017961; -.
DR iPTMnet; Q9ET78; -.
DR PhosphoSitePlus; Q9ET78; -.
DR SwissPalm; Q9ET78; -.
DR MaxQB; Q9ET78; -.
DR PaxDb; Q9ET78; -.
DR PeptideAtlas; Q9ET78; -.
DR PRIDE; Q9ET78; -.
DR ProteomicsDB; 269034; -.
DR Antibodypedia; 27340; 339 antibodies from 32 providers.
DR DNASU; 59091; -.
DR Ensembl; ENSMUST00000017961; ENSMUSP00000017961; ENSMUSG00000017817.
DR Ensembl; ENSMUST00000109425; ENSMUSP00000105052; ENSMUSG00000017817.
DR GeneID; 59091; -.
DR KEGG; mmu:59091; -.
DR UCSC; uc008nsp.2; mouse.
DR CTD; 57158; -.
DR MGI; MGI:1891496; Jph2.
DR VEuPathDB; HostDB:ENSMUSG00000017817; -.
DR eggNOG; KOG0231; Eukaryota.
DR GeneTree; ENSGT00940000159411; -.
DR HOGENOM; CLU_008078_1_0_1; -.
DR InParanoid; Q9ET78; -.
DR OMA; AWNGEPS; -.
DR OrthoDB; 904294at2759; -.
DR PhylomeDB; Q9ET78; -.
DR TreeFam; TF317210; -.
DR BioGRID-ORCS; 59091; 4 hits in 72 CRISPR screens.
DR PRO; PR:Q9ET78; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9ET78; protein.
DR Bgee; ENSMUSG00000017817; Expressed in hindlimb stylopod muscle and 97 other tissues.
DR Genevisible; Q9ET78; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030314; C:junctional membrane complex; IMP:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:MGI.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0070300; F:phosphatidic acid binding; ISS:UniProtKB.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISS:UniProtKB.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; ISS:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; ISS:UniProtKB.
DR GO; GO:0055074; P:calcium ion homeostasis; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:MGI.
DR GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; ISO:MGI.
DR GO; GO:0055024; P:regulation of cardiac muscle tissue development; IMP:UniProtKB.
DR InterPro; IPR017191; Junctophilin.
DR InterPro; IPR003409; MORN.
DR PANTHER; PTHR23085; PTHR23085; 1.
DR Pfam; PF02493; MORN; 8.
DR PIRSF; PIRSF037387; Junctophilin; 1.
DR SMART; SM00698; MORN; 6.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; DNA-binding; Endoplasmic reticulum;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Sarcoplasmic reticulum; Transcription; Transcription regulation;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..696
FT /note="Junctophilin-2"
FT /id="PRO_0000159848"
FT CHAIN 1..565
FT /note="Junctophilin-2 N-terminal fragment"
FT /evidence="ECO:0000305|PubMed:30409805"
FT /id="PRO_0000446376"
FT TOPO_DOM 1..674
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 675..695
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT REPEAT 14..36
FT /note="MORN 1"
FT /evidence="ECO:0000255"
FT REPEAT 38..59
FT /note="MORN 2"
FT /evidence="ECO:0000255"
FT REPEAT 60..79
FT /note="MORN 3"
FT /evidence="ECO:0000255"
FT REPEAT 82..104
FT /note="MORN 4"
FT /evidence="ECO:0000255"
FT REPEAT 106..128
FT /note="MORN 5"
FT /evidence="ECO:0000255"
FT REPEAT 129..151
FT /note="MORN 6"
FT /evidence="ECO:0000255"
FT REPEAT 285..307
FT /note="MORN 7"
FT /evidence="ECO:0000255"
FT REPEAT 308..330
FT /note="MORN 8"
FT /evidence="ECO:0000255"
FT REGION 164..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 345..359
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:30409805"
FT MOTIF 488..492
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:30409805"
FT COMPBIAS 473..491
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..615
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 155..156
FT /note="Cleavage; by calpain"
FT /evidence="ECO:0000269|PubMed:26063807"
FT SITE 201..202
FT /note="Cleavage; by calpain"
FT /evidence="ECO:0000269|PubMed:26063807"
FT SITE 565..566
FT /note="Cleavage; by calpain"
FT /evidence="ECO:0000269|PubMed:26063807"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2PS20"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BR39"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2PS20"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2PS20"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 470
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 483
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2PS20"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2PS20"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 153..158
FT /note="Missing: Abolishes cleavage by calpain at the N-
FT terminus."
FT /evidence="ECO:0000269|PubMed:26063807"
FT MUTAGEN 399
FT /note="A->S: Decreased transverse tubule regularity and
FT aberrant calcium handling in septal cardiomyocytes."
FT /evidence="ECO:0000269|PubMed:28393127"
FT MUTAGEN 488..492
FT /note="Missing: Abolishes nuclear localization of the
FT Junctophilin-2 N-terminal fragment chain."
FT /evidence="ECO:0000269|PubMed:30409805"
FT MUTAGEN 563..568
FT /note="Missing: Abolishes cleavage by calpain at the C-
FT terminus."
FT /evidence="ECO:0000269|PubMed:26063807"
SQ SEQUENCE 696 AA; 74692 MW; 346BA284E076A7FB CRC64;
MSGGRFDFDD GGAYCGGWEG GKAHGHGLCT GPKGQGEYSG SWNFGFEVAG VYTWPSGNTF
EGYWSQGKRH GLGIETKGRW LYKGEWTHGF KGRYGIRQST NSGAKYEGTW NNGLQDGYGT
ETYADGGTYQ GQFTNGMRHG YGVRQSVPYG MAVVVRSPLR TSLSSLRSEH SNGTVAPDSP
AADGPMLPSP PVPRGGFALT LLATAEAARP QGLFTRGTLL GRLRRSESRT SLGSQRSRLS
FLKSELSSGA SDAASTGSLA EGAEGPDDAA APFDADIDAT TTETYMGEWK NDKRSGFGVS
ERSSGLRYEG EWLDNLRHGY GRTTLPDGHR EEGKYRHNVL VKGTKRRVLP LKSSKVRQKV
EHGVEGAQRA AAIARQKAEI AASRTSHAKA KAEAAEQAAL AANQESNIAR TLAKELAPDF
YQPGPEYQKR RLLQEILENS ESLLEPPERG LGTGLPERPR ESPQLHERET PQPEGGPPSP
AGTPPQPKRP RPGASKDGLL SPGSWNGEPG GEGSRPATPS DGAGRRSPAR PASEHMAIEA
LQPPPAPSQE PEVAMYRGYH SYAVRTGPPE PPPLEDEQEP EPEPEPEVRR SDSAPPSPVS
ATVPEEEPPA PRSPVPAKQA TLEPKPIVPK AEPKAKARKT EARGLSKAGA KKKGRKEVAQ
AKEAEVEVEE VPNTVLICMV ILLNIGLAIL FVHLLT
