JPH4_MOUSE
ID JPH4_MOUSE Reviewed; 628 AA.
AC Q80WT0; Q69FB2; Q8BMI1;
DT 09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Junctophilin-4;
DE Short=JP-4;
DE AltName: Full=Junctophilin-like 1 protein;
GN Name=Jph4; Synonyms=Jphl1;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND POSSIBLE
RP FUNCTION.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=14559359; DOI=10.1016/s0169-328x(03)00341-3;
RA Nishi M., Sakagami H., Komazaki S., Kondo H., Takeshima H.;
RT "Coexpression of junctophilin type 3 and type 4 in brain.";
RL Brain Res. Mol. Brain Res. 118:102-110(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Savaskan N.E., Brauer A.U.;
RT "Molecular cloning and functional characterization of a novel subclass of
RT junctophilins in the brain.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Forelimb;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [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).
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. JPH4 is brain-
CC specific and appears to have an active role in certain neurons involved
CC in motor coordination and memory. {ECO:0000269|PubMed:16809425}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16809425}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:16809425}. Note=Localized predominantly on the
CC plasma membrane. The transmembrane domain is anchored in endoplasmic
CC reticulum membrane, while the N-terminal part associates with the
CC plasma membrane (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80WT0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80WT0-2; Sequence=VSP_008197, VSP_008198;
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 Purkinje cells, while it is weakly expressed in
CC granular cells. {ECO:0000269|PubMed:14559359,
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: Jph3 and Jph4 double null mutants exhibit
CC atypical depolarizing responses, irregular cerebellar plasticity due to
CC abolished crosstalk in Purkinje cells. There is hyperphosphorylation of
CC PRKCG and mild impairment of synaptic maturation. Exploratory activity,
CC hippocampal plasticity and memory are impaired and there is abnormal
CC foot-clasping reflex. {ECO:0000269|PubMed:16809425,
CC ECO:0000269|PubMed:17904530}.
CC -!- MISCELLANEOUS: [Isoform 2]: Due to intron retention. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the junctophilin family. {ECO:0000305}.
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DR EMBL; AB099712; BAD01498.1; -; mRNA.
DR EMBL; AY341261; AAR08903.1; -; mRNA.
DR EMBL; AK148135; BAE28365.1; -; mRNA.
DR EMBL; AK031092; BAC27249.1; -; mRNA.
DR EMBL; CH466535; EDL36304.1; -; Genomic_DNA.
DR EMBL; BC052049; AAH52049.1; -; mRNA.
DR EMBL; BC052376; AAH52376.1; -; mRNA.
DR EMBL; BC052722; AAH52722.1; -; mRNA.
DR CCDS; CCDS27109.1; -. [Q80WT0-1]
DR RefSeq; NP_796023.2; NM_177049.5. [Q80WT0-1]
DR AlphaFoldDB; Q80WT0; -.
DR SMR; Q80WT0; -.
DR STRING; 10090.ENSMUSP00000022819; -.
DR iPTMnet; Q80WT0; -.
DR PhosphoSitePlus; Q80WT0; -.
DR MaxQB; Q80WT0; -.
DR PaxDb; Q80WT0; -.
DR PRIDE; Q80WT0; -.
DR ProteomicsDB; 301701; -. [Q80WT0-1]
DR ProteomicsDB; 301702; -. [Q80WT0-2]
DR Antibodypedia; 22533; 115 antibodies from 23 providers.
DR DNASU; 319984; -.
DR Ensembl; ENSMUST00000022819; ENSMUSP00000022819; ENSMUSG00000022208. [Q80WT0-1]
DR Ensembl; ENSMUST00000124493; ENSMUSP00000121893; ENSMUSG00000022208. [Q80WT0-1]
DR GeneID; 319984; -.
DR KEGG; mmu:319984; -.
DR UCSC; uc007tyg.1; mouse. [Q80WT0-1]
DR CTD; 84502; -.
DR MGI; MGI:2443113; Jph4.
DR VEuPathDB; HostDB:ENSMUSG00000022208; -.
DR eggNOG; KOG0231; Eukaryota.
DR GeneTree; ENSGT00940000162272; -.
DR HOGENOM; CLU_008078_4_0_1; -.
DR InParanoid; Q80WT0; -.
DR OMA; PEAGCLM; -.
DR OrthoDB; 904294at2759; -.
DR PhylomeDB; Q80WT0; -.
DR TreeFam; TF317210; -.
DR BioGRID-ORCS; 319984; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Jph4; mouse.
DR PRO; PR:Q80WT0; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q80WT0; protein.
DR Bgee; ENSMUSG00000022208; Expressed in embryonic brain and 117 other tissues.
DR Genevisible; Q80WT0; MM.
DR GO; GO:0043198; C:dendritic shaft; IDA:MGI.
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; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:MGI.
DR GO; GO:0007612; P:learning; IGI:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IGI:MGI.
DR GO; GO:0001817; P:regulation of cytokine production; IMP:MGI.
DR GO; GO:2001256; P:regulation of store-operated calcium entry; IMP:MGI.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IGI:MGI.
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 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Endoplasmic reticulum; Membrane;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..628
FT /note="Junctophilin-4"
FT /id="PRO_0000159853"
FT TOPO_DOM 1..606
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 607..628
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 106..128
FT /note="MORN 5"
FT REPEAT 129..151
FT /note="MORN 6"
FT REPEAT 282..304
FT /note="MORN 7"
FT REPEAT 305..327
FT /note="MORN 8"
FT REGION 158..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..182
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 385..406
FT /note="AADALLKAVAASSVAEKAVEAA -> WASGAQIQLGLRGEVPLGTNHT (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008197"
FT VAR_SEQ 407..628
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008198"
SQ SEQUENCE 628 AA; 66000 MW; 97B6BEA4A02C6143 CRC64;
MSPGGKFDFD DGGCYVGGWE AGRAHGYGVC TGPGAQGEYS GCWAHGFESL GVFTGPGGHS
YQGHWQQGKR EGLGVERKSR WTYRGEWLGG LKGRSGVWES VSGLRYAGLW KDGFQDGYGT
ETYSDGGTYQ GQWQAGKRHG YGVRQSVPYH QAALLRSPRR TSLDSGHSDP PTPPPPLPLP
GDEGGSPASG SRGGFVLAGP GDADGASSRK RTPAAGGFFR RSLLLSGLRA GGRRSSLGSK
RGSLRSEVSS EVGSTGPPGS EASGPPIPAP PALIEGSATE VYAGEWRADR RSGYGVSQRS
NGLRYEGEWL GNRRHGYGRT TRPDGSREEG KYKRNRLVHG GRVRSLLPLA LRRGKVKEKV
DRAVEGARRA VSAARQRQEI AAARAADALL KAVAASSVAE KAVEAARMAK LIAQDLQPML
EAPGRRPRQD SGGSDTEPLD EDSPGVYENG LTPSEGSPEL PSSPASSHQP WRAPACRSPL
PPGGNWGPFS SPKAWPEEWG GPGEQAEELA GYEAEDEAGV QGPGPRDGSP LLGGCSDSSG
SLREEEGEDE ESLPQLRAPG GSESEPVTTP VLRGLSSRGP DAGCLTEEVE EPAPTERPAQ
PGAANPLVVG AVALLDLSLA FLFSQLLT
