JPH3_MOUSE
ID JPH3_MOUSE Reviewed; 744 AA.
AC Q9ET77; Q3ZAS3; Q8BNM7; Q9EQZ2;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Junctophilin-3;
DE Short=JP-3;
DE AltName: Full=Junctophilin type 3;
GN Name=Jph3; Synonyms=Jp3;
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], AND SUBCELLULAR LOCATION.
RC STRAIN=129, and C57BL/6J; TISSUE=Brain;
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=C57BL/6J;
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].
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 FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=11906164; DOI=10.1006/bbrc.2002.6649;
RA Nishi M., Hashimoto K., Kuriyama K., Komazaki S., Kano M., Shibata S.,
RA Takeshima H.;
RT "Motor discoordination in mutant mice lacking junctophilin type 3.";
RL Biochem. Biophys. Res. Commun. 292:318-324(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16809425; DOI=10.1073/pnas.0509863103;
RA Moriguchi S., Nishi M., Komazaki S., Sakagami H., Miyazaki T., Masumiya H.,
RA Saito S.Y., Watanabe M., Kondo H., Yawo H., Fukunaga K., Takeshima H.;
RT "Functional uncoupling between Ca2+ release and afterhyperpolarization in
RT mutant hippocampal neurons lacking junctophilins.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10811-10816(2006).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=17904530; DOI=10.1016/j.bbrc.2007.09.062;
RA Ikeda A., Miyazaki T., Kakizawa S., Okuno Y., Tsuchiya S., Myomoto A.,
RA Saito S.Y., Yamamoto T., Yamazaki T., Iino M., Tsujimoto G., Watanabe M.,
RA Takeshima H.;
RT "Abnormal features in mutant cerebellar Purkinje cells lacking
RT junctophilins.";
RL Biochem. Biophys. Res. Commun. 363:835-839(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440; THR-451; SER-457;
RP THR-471; SER-475; SER-699 AND SER-706, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Junctophilins contribute to the formation of junctional
CC membrane complexes (JMCs) which link the plasma membrane with the
CC endoplasmic or sarcoplasmic reticulum in excitable cells. Provides a
CC structural foundation for functional cross-talk between the cell
CC surface and intracellular calcium release channels. JPH3 is brain-
CC specific and appears to have an active role in certain neurons involved
CC in motor coordination and memory. {ECO:0000269|PubMed:11906164,
CC ECO:0000269|PubMed:16809425}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC Endoplasmic reticulum membrane; Single-pass type IV membrane protein.
CC Note=Localized predominantly on the plasma membrane. The transmembrane
CC domain is anchored in endoplasmic reticulum membrane, while the N-
CC terminal part associates with the plasma membrane.
CC -!- TISSUE SPECIFICITY: Specifically expressed in brain. Highest levels in
CC the olfactory tubercle, caudate putamen, nucleus accumbens, hippocampal
CC formation, piriform cortex and cerebellar cortex. Expressed in disctete
CC neurons sites. In hippocampal formation, expressed in dendrites of
CC hippocampal pyramidal and denate granule cells. In cerebellum, it is
CC highly expressed in Purkinge cells, while it is weakly expressed in
CC granular cells. {ECO:0000269|PubMed:11906164,
CC ECO:0000269|PubMed:16809425}.
CC -!- DOMAIN: The MORN (membrane occupation and recognition nexus) repeats
CC contribute to the plasma membrane binding, possibly by interacting with
CC phospholipids. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile, but have defects in
CC balance/motor coordination tasks. Jph3 and Jph4 double knockout mice
CC exhibit atypical depolarizing responses, irregular cerebellar
CC plasticity due to abolished crosstalk in Purkinje cells. There is
CC hyperphosphorylation of PRKCG and mild impairment of synaptic
CC maturation. Exploratory activity, hippocampal plasticity and memory are
CC impaired and there is abnormal foot-clasping reflex.
CC {ECO:0000269|PubMed:11906164, ECO:0000269|PubMed:16809425,
CC ECO:0000269|PubMed:17904530}.
CC -!- SIMILARITY: Belongs to the junctophilin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC38666.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB024449; BAB12046.1; -; mRNA.
DR EMBL; AB024450; BAB20320.1; -; Genomic_DNA.
DR EMBL; AK082880; BAC38666.1; ALT_SEQ; mRNA.
DR EMBL; BC103682; AAI03683.1; -; mRNA.
DR EMBL; BC104736; AAI04737.1; -; mRNA.
DR EMBL; BC105307; AAI05308.1; -; mRNA.
DR CCDS; CCDS22728.1; -.
DR RefSeq; NP_065630.1; NM_020605.3.
DR AlphaFoldDB; Q9ET77; -.
DR SMR; Q9ET77; -.
DR BioGRID; 208262; 1.
DR STRING; 10090.ENSMUSP00000026357; -.
DR iPTMnet; Q9ET77; -.
DR PhosphoSitePlus; Q9ET77; -.
DR MaxQB; Q9ET77; -.
DR PaxDb; Q9ET77; -.
DR PRIDE; Q9ET77; -.
DR ProteomicsDB; 269035; -.
DR Antibodypedia; 17225; 186 antibodies from 25 providers.
DR DNASU; 57340; -.
DR Ensembl; ENSMUST00000026357; ENSMUSP00000026357; ENSMUSG00000025318.
DR Ensembl; ENSMUST00000167439; ENSMUSP00000126190; ENSMUSG00000025318.
DR GeneID; 57340; -.
DR KEGG; mmu:57340; -.
DR UCSC; uc009nrz.2; mouse.
DR CTD; 57338; -.
DR MGI; MGI:1891497; Jph3.
DR VEuPathDB; HostDB:ENSMUSG00000025318; -.
DR eggNOG; KOG0231; Eukaryota.
DR GeneTree; ENSGT00940000158707; -.
DR HOGENOM; CLU_008078_2_0_1; -.
DR InParanoid; Q9ET77; -.
DR OMA; RHYSKAG; -.
DR OrthoDB; 904294at2759; -.
DR PhylomeDB; Q9ET77; -.
DR TreeFam; TF317210; -.
DR BioGRID-ORCS; 57340; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q9ET77; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9ET77; protein.
DR Bgee; ENSMUSG00000025318; Expressed in CA3 field of hippocampus and 100 other tissues.
DR Genevisible; Q9ET77; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:MGI.
DR GO; GO:0030314; C:junctional membrane complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0035640; P:exploration behavior; IMP:UniProtKB.
DR GO; GO:0007612; P:learning; IGI:MGI.
DR GO; GO:0040011; P:locomotion; IMP:MGI.
DR GO; GO:0007613; P:memory; IMP:UniProtKB.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IGI:MGI.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IMP:UniProtKB.
DR GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IMP:UniProtKB.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IBA:GO_Central.
DR InterPro; IPR017191; Junctophilin.
DR InterPro; IPR003409; MORN.
DR PANTHER; PTHR23085; PTHR23085; 2.
DR Pfam; PF02493; MORN; 7.
DR PIRSF; PIRSF037387; Junctophilin; 1.
DR SMART; SM00698; MORN; 7.
PE 1: Evidence at protein level;
KW Cell membrane; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..744
FT /note="Junctophilin-3"
FT /id="PRO_0000159851"
FT TOPO_DOM 1..723
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 724..744
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT REPEAT 15..37
FT /note="MORN 1"
FT REPEAT 39..60
FT /note="MORN 2"
FT REPEAT 61..82
FT /note="MORN 3"
FT REPEAT 83..105
FT /note="MORN 4"
FT REPEAT 107..129
FT /note="MORN 5"
FT REPEAT 130..152
FT /note="MORN 6"
FT REPEAT 288..310
FT /note="MORN 7"
FT REPEAT 311..333
FT /note="MORN 8"
FT REGION 230..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 451
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 471
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 699
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 706
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ 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
