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Junctophilin-3 (JP-3) (Junctophilin type 3)

 JPH3_MOUSE              Reviewed;         744 AA.
Q9ET77; Q3ZAS3; Q8BNM7; Q9EQZ2;
17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
07-JUN-2017, entry version 122.
RecName: Full=Junctophilin-3;
Short=JP-3;
AltName: Full=Junctophilin type 3;
Name=Jph3; Synonyms=Jp3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND SUBCELLULAR LOCATION.
STRAIN=129, and C57BL/6J; TISSUE=Brain;
PubMed=10949023; DOI=10.1016/S1097-2765(05)00005-5;
Takeshima H., Komazaki S., Nishi M., Iino M., Kangawa K.;
"Junctophilins: a novel family of junctional membrane complex
proteins.";
Mol. Cell 6:11-22(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=11906164; DOI=10.1006/bbrc.2002.6649;
Nishi M., Hashimoto K., Kuriyama K., Komazaki S., Kano M., Shibata S.,
Takeshima H.;
"Motor discoordination in mutant mice lacking junctophilin type 3.";
Biochem. Biophys. Res. Commun. 292:318-324(2002).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[6]
DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR
LOCATION.
PubMed=16809425; DOI=10.1073/pnas.0509863103;
Moriguchi S., Nishi M., Komazaki S., Sakagami H., Miyazaki T.,
Masumiya H., Saito S.Y., Watanabe M., Kondo H., Yawo H., Fukunaga K.,
Takeshima H.;
"Functional uncoupling between Ca2+ release and afterhyperpolarization
in mutant hippocampal neurons lacking junctophilins.";
Proc. Natl. Acad. Sci. U.S.A. 103:10811-10816(2006).
[7]
DISRUPTION PHENOTYPE.
PubMed=17904530; DOI=10.1016/j.bbrc.2007.09.062;
Ikeda A., Miyazaki T., Kakizawa S., Okuno Y., Tsuchiya S., Myomoto A.,
Saito S.Y., Yamamoto T., Yamazaki T., Iino M., Tsujimoto G.,
Watanabe M., Takeshima H.;
"Abnormal features in mutant cerebellar Purkinje cells lacking
junctophilins.";
Biochem. Biophys. Res. Commun. 363:835-839(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440; THR-451; SER-457;
THR-471; SER-475; SER-699 AND SER-706, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Junctophilins contribute to the formation of junctional
membrane complexes (JMCs) which link the plasma membrane with the
endoplasmic or sarcoplasmic reticulum in excitable cells. Provides
a structural foundation for functional cross-talk between the cell
surface and intracellular calcium release channels. JPH3 is brain-
specific and appears to have an active role in certain neurons
involved in motor coordination and memory.
{ECO:0000269|PubMed:11906164, ECO:0000269|PubMed:16809425}.
-!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
Endoplasmic reticulum membrane; Single-pass type IV membrane
protein. Note=Localized predominantly on the plasma membrane. The
transmembrane domain is anchored in endoplasmic reticulum
membrane, while the N-terminal part associates with the plasma
membrane.
-!- TISSUE SPECIFICITY: Specifically expressed in brain. Highest
levels in the olfactory tubercle, caudate putamen, nucleus
accumbens, hippocampal formation, piriform cortex and cerebellar
cortex. Expressed in disctete neurons sites. In hippocampal
formation, expressed in dendrites of hippocampal pyramidal and
denate granule cells. In cerebellum, it is highly expressed in
Purkinge cells, while it is weakly expressed in granular cells.
{ECO:0000269|PubMed:11906164, ECO:0000269|PubMed:16809425}.
-!- DOMAIN: The MORN (membrane occupation and recognition nexus)
repeats contribute to the plasma membrane binding, possibly by
interacting with phospholipids. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice are viable and fertile, but have
defects in balance/motor coordination tasks. Jph3 and Jph4 double
knockout mice exhibit atypical depolarizing responses, irregular
cerebellar plasticity due to abolished crosstalk in Purkinje
cells. There is hyperphosphorylation of PRKCG and mild impairment
of synaptic maturation. Exploratory activity, hippocampal
plasticity and memory are impaired and there is abnormal foot-
clasping reflex. {ECO:0000269|PubMed:11906164,
ECO:0000269|PubMed:16809425, ECO:0000269|PubMed:17904530}.
-!- SIMILARITY: Belongs to the junctophilin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC38666.1; Type=Erroneous termination; Positions=745; Note=Translated as stop.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB024449; BAB12046.1; -; mRNA.
EMBL; AB024450; BAB20320.1; -; Genomic_DNA.
EMBL; AK082880; BAC38666.1; ALT_SEQ; mRNA.
EMBL; BC103682; AAI03683.1; -; mRNA.
EMBL; BC104736; AAI04737.1; -; mRNA.
EMBL; BC105307; AAI05308.1; -; mRNA.
CCDS; CCDS22728.1; -.
RefSeq; NP_065630.1; NM_020605.3.
UniGene; Mm.306870; -.
ProteinModelPortal; Q9ET77; -.
SMR; Q9ET77; -.
STRING; 10090.ENSMUSP00000026357; -.
iPTMnet; Q9ET77; -.
PhosphoSitePlus; Q9ET77; -.
MaxQB; Q9ET77; -.
PaxDb; Q9ET77; -.
PRIDE; Q9ET77; -.
Ensembl; ENSMUST00000026357; ENSMUSP00000026357; ENSMUSG00000025318.
Ensembl; ENSMUST00000167439; ENSMUSP00000126190; ENSMUSG00000025318.
GeneID; 57340; -.
KEGG; mmu:57340; -.
UCSC; uc009nrz.2; mouse.
CTD; 57338; -.
MGI; MGI:1891497; Jph3.
eggNOG; KOG0231; Eukaryota.
eggNOG; COG4642; LUCA.
GeneTree; ENSGT00730000110639; -.
HOGENOM; HOG000264244; -.
HOVERGEN; HBG031648; -.
InParanoid; Q9ET77; -.
KO; K19530; -.
OMA; KLSNYEM; -.
OrthoDB; EOG091G03WX; -.
PhylomeDB; Q9ET77; -.
TreeFam; TF317210; -.
ChiTaRS; Jph3; mouse.
PRO; PR:Q9ET77; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000025318; -.
CleanEx; MM_JPH3; -.
Genevisible; Q9ET77; MM.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; TAS:MGI.
GO; GO:0030314; C:junctional membrane complex; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0015278; F:calcium-release channel activity; IMP:UniProtKB.
GO; GO:0035640; P:exploration behavior; IMP:UniProtKB.
GO; GO:0007612; P:learning; IGI:MGI.
GO; GO:0040011; P:locomotion; IMP:MGI.
GO; GO:0007613; P:memory; IMP:UniProtKB.
GO; GO:0050885; P:neuromuscular process controlling balance; IGI:MGI.
GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IMP:UniProtKB.
GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IMP:UniProtKB.
InterPro; IPR017191; Junctophilin.
InterPro; IPR003409; MORN.
Pfam; PF02493; MORN; 7.
PIRSF; PIRSF037387; Junctophilin; 1.
SMART; SM00698; MORN; 7.
1: Evidence at protein level;
Cell membrane; Complete proteome; Endoplasmic reticulum; Membrane;
Phosphoprotein; Reference proteome; Repeat; Transmembrane;
Transmembrane helix.
CHAIN 1 744 Junctophilin-3.
/FTId=PRO_0000159851.
TOPO_DOM 1 723 Cytoplasmic. {ECO:0000255}.
TRANSMEM 724 744 Helical; Anchor for type IV membrane
protein. {ECO:0000255}.
REPEAT 15 37 MORN 1.
REPEAT 39 60 MORN 2.
REPEAT 61 82 MORN 3.
REPEAT 83 105 MORN 4.
REPEAT 107 129 MORN 5.
REPEAT 130 152 MORN 6.
REPEAT 288 310 MORN 7.
REPEAT 311 333 MORN 8.
COMPBIAS 4 143 Gly-rich.
COMPBIAS 366 416 Ala-rich.
MOD_RES 440 440 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 451 451 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 457 457 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 471 471 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 475 475 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 506 506 Phosphoserine.
{ECO:0000244|PubMed:16452087}.
MOD_RES 699 699 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 706 706 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
SEQUENCE 744 AA; 81229 MW; 3D72AED6A6FDA914 CRC64;
MSSGGRFNFD DGGSYCGGWE DGKAHGHGVC TGPKGQGEYT GSWSHGFEVL GVYTWPSGNT
YQGTWAQGKR HGIGLESKGK WVYKGEWTHG FKGRYGVREC TGNGAKYEGT WSNGLQDGYG
TETYSDGGTY QGQWVGGMRQ GYGVRQSVPY GMAAVIRSPL RTSINSLRSE HTNGAALHPD
ASPAVAGSPA VSRGGFVLVA HSDSEILKSK KKGLFRRSLL SGLKLRKSES KSSLASQRSK
QSSFRSEAGM STVSSTASDI HSTISLGEAE AELAVIEDDI DATTTETYVG EWKNDKRSGF
GVSQRSDGLK YEGEWVSNRR HGYGCMTFPD GTKEEGKYKQ NVLVSGKRKN LIPLRASKIR
EKVDRAVEAA ERAATIAKQK AEIAASRTSH SRAKAEAALT AAQKAQEEAR IARITAKEFS
PSFQHRENGL EYQRPKHQMS CDDIEVLSTG TPLQQESPEL YRKGTTPSDL TPDDSPLQSF
PASPTSTPPP APASRTKMAH FSRQVSVDEE RSGDIQMLLE GRGGDYARNS WGEEKAGASR
GIRSGALRSG QPTEDFRTRG SGHKQPGNPK PRERRTESPT TFSWTSHHRA GNPCSGGPKL
LEPDEEQLSN YKLEMKPLLR MDACPQDTHP QRRRHSRGAG GDRGFGLQRL RSKSQNKENL
RPASSAEPTV QKLESLRLGD RPEPRLLRWD LTFSPPQKSL PVALESDEET GDELKSSTGS
APILVVMVIL LNIGVAILFI NFFI


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