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Protein

Junctophilin-3

Gene

Jph3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  • calcium-release channel activity Source: UniProtKB

GO - Biological processi

  • exploration behavior Source: UniProtKB
  • learning Source: MGI
  • locomotion Source: MGI
  • memory Source: UniProtKB
  • neuromuscular process controlling balance Source: MGI
  • regulation of neuronal synaptic plasticity Source: UniProtKB
  • regulation of ryanodine-sensitive calcium-release channel activity Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Junctophilin-3
Short name:
JP-3
Alternative name(s):
Junctophilin type 3
Gene namesi
Name:Jph3
Synonyms:Jp3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1891497. Jph3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 723723CytoplasmicSequence analysisAdd
BLAST
Transmembranei724 – 74421Helical; Anchor for type IV membrane proteinSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB
  • integral component of membrane Source: MGI
  • junctional membrane complex Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

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.3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 744744Junctophilin-3PRO_0000159851Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei440 – 4401PhosphoserineCombined sources
Modified residuei451 – 4511PhosphothreonineCombined sources
Modified residuei457 – 4571PhosphoserineCombined sources
Modified residuei471 – 4711PhosphothreonineCombined sources
Modified residuei475 – 4751PhosphoserineCombined sources
Modified residuei506 – 5061PhosphoserineCombined sources
Modified residuei699 – 6991PhosphoserineCombined sources
Modified residuei706 – 7061PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9ET77.
PaxDbiQ9ET77.
PRIDEiQ9ET77.

PTM databases

iPTMnetiQ9ET77.
PhosphoSiteiQ9ET77.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiQ9ET77.
CleanExiMM_JPH3.
GenevisibleiQ9ET77. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000026357.

Structurei

3D structure databases

ProteinModelPortaliQ9ET77.
SMRiQ9ET77. Positions 5-146, 288-342.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati15 – 3723MORN 1Add
BLAST
Repeati39 – 6022MORN 2Add
BLAST
Repeati61 – 8222MORN 3Add
BLAST
Repeati83 – 10523MORN 4Add
BLAST
Repeati107 – 12923MORN 5Add
BLAST
Repeati130 – 15223MORN 6Add
BLAST
Repeati288 – 31023MORN 7Add
BLAST
Repeati311 – 33323MORN 8Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 143140Gly-richAdd
BLAST
Compositional biasi366 – 41651Ala-richAdd
BLAST

Domaini

The MORN (membrane occupation and recognition nexus) repeats contribute to the plasma membrane binding, possibly by interacting with phospholipids.By similarity

Sequence similaritiesi

Belongs to the junctophilin family.Curated
Contains 8 MORN repeats.Curated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0231. Eukaryota.
COG4642. LUCA.
GeneTreeiENSGT00730000110639.
HOGENOMiHOG000264244.
HOVERGENiHBG031648.
InParanoidiQ9ET77.
KOiK19530.
OMAiHPQKRRY.
OrthoDBiEOG7J4463.
PhylomeDBiQ9ET77.
TreeFamiTF317210.

Family and domain databases

InterProiIPR017191. Junctophilin.
IPR003409. MORN.
[Graphical view]
PfamiPF02493. MORN. 7 hits.
[Graphical view]
PIRSFiPIRSF037387. Junctophilin. 1 hit.
SMARTiSM00698. MORN. 7 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ET77-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSGGRFNFD DGGSYCGGWE DGKAHGHGVC TGPKGQGEYT GSWSHGFEVL
60 70 80 90 100
GVYTWPSGNT YQGTWAQGKR HGIGLESKGK WVYKGEWTHG FKGRYGVREC
110 120 130 140 150
TGNGAKYEGT WSNGLQDGYG TETYSDGGTY QGQWVGGMRQ GYGVRQSVPY
160 170 180 190 200
GMAAVIRSPL RTSINSLRSE HTNGAALHPD ASPAVAGSPA VSRGGFVLVA
210 220 230 240 250
HSDSEILKSK KKGLFRRSLL SGLKLRKSES KSSLASQRSK QSSFRSEAGM
260 270 280 290 300
STVSSTASDI HSTISLGEAE AELAVIEDDI DATTTETYVG EWKNDKRSGF
310 320 330 340 350
GVSQRSDGLK YEGEWVSNRR HGYGCMTFPD GTKEEGKYKQ NVLVSGKRKN
360 370 380 390 400
LIPLRASKIR EKVDRAVEAA ERAATIAKQK AEIAASRTSH SRAKAEAALT
410 420 430 440 450
AAQKAQEEAR IARITAKEFS PSFQHRENGL EYQRPKHQMS CDDIEVLSTG
460 470 480 490 500
TPLQQESPEL YRKGTTPSDL TPDDSPLQSF PASPTSTPPP APASRTKMAH
510 520 530 540 550
FSRQVSVDEE RSGDIQMLLE GRGGDYARNS WGEEKAGASR GIRSGALRSG
560 570 580 590 600
QPTEDFRTRG SGHKQPGNPK PRERRTESPT TFSWTSHHRA GNPCSGGPKL
610 620 630 640 650
LEPDEEQLSN YKLEMKPLLR MDACPQDTHP QRRRHSRGAG GDRGFGLQRL
660 670 680 690 700
RSKSQNKENL RPASSAEPTV QKLESLRLGD RPEPRLLRWD LTFSPPQKSL
710 720 730 740
PVALESDEET GDELKSSTGS APILVVMVIL LNIGVAILFI NFFI
Length:744
Mass (Da):81,229
Last modified:March 1, 2001 - v1
Checksum:i3D72AED6A6FDA914
GO

Sequence cautioni

The sequence BAC38666.1 differs from that shown. Reason: Erroneous termination at position 745. Translated as stop.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024449 mRNA. Translation: BAB12046.1.
AB024450 Genomic DNA. Translation: BAB20320.1.
AK082880 mRNA. Translation: BAC38666.1. Sequence problems.
BC103682 mRNA. Translation: AAI03683.1.
BC104736 mRNA. Translation: AAI04737.1.
BC105307 mRNA. Translation: AAI05308.1.
CCDSiCCDS22728.1.
RefSeqiNP_065630.1. NM_020605.3.
UniGeneiMm.306870.

Genome annotation databases

EnsembliENSMUST00000026357; ENSMUSP00000026357; ENSMUSG00000025318.
ENSMUST00000167439; ENSMUSP00000126190; ENSMUSG00000025318.
GeneIDi57340.
KEGGimmu:57340.
UCSCiuc009nrz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024449 mRNA. Translation: BAB12046.1.
AB024450 Genomic DNA. Translation: BAB20320.1.
AK082880 mRNA. Translation: BAC38666.1. Sequence problems.
BC103682 mRNA. Translation: AAI03683.1.
BC104736 mRNA. Translation: AAI04737.1.
BC105307 mRNA. Translation: AAI05308.1.
CCDSiCCDS22728.1.
RefSeqiNP_065630.1. NM_020605.3.
UniGeneiMm.306870.

3D structure databases

ProteinModelPortaliQ9ET77.
SMRiQ9ET77. Positions 5-146, 288-342.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000026357.

PTM databases

iPTMnetiQ9ET77.
PhosphoSiteiQ9ET77.

Proteomic databases

MaxQBiQ9ET77.
PaxDbiQ9ET77.
PRIDEiQ9ET77.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026357; ENSMUSP00000026357; ENSMUSG00000025318.
ENSMUST00000167439; ENSMUSP00000126190; ENSMUSG00000025318.
GeneIDi57340.
KEGGimmu:57340.
UCSCiuc009nrz.2. mouse.

Organism-specific databases

CTDi57338.
MGIiMGI:1891497. Jph3.

Phylogenomic databases

eggNOGiKOG0231. Eukaryota.
COG4642. LUCA.
GeneTreeiENSGT00730000110639.
HOGENOMiHOG000264244.
HOVERGENiHBG031648.
InParanoidiQ9ET77.
KOiK19530.
OMAiHPQKRRY.
OrthoDBiEOG7J4463.
PhylomeDBiQ9ET77.
TreeFamiTF317210.

Miscellaneous databases

ChiTaRSiJph3. mouse.
PROiQ9ET77.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ET77.
CleanExiMM_JPH3.
GenevisibleiQ9ET77. MM.

Family and domain databases

InterProiIPR017191. Junctophilin.
IPR003409. MORN.
[Graphical view]
PfamiPF02493. MORN. 7 hits.
[Graphical view]
PIRSFiPIRSF037387. Junctophilin. 1 hit.
SMARTiSM00698. MORN. 7 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Junctophilins: a novel family of junctional membrane complex proteins."
    Takeshima H., Komazaki S., Nishi M., Iino M., Kangawa K.
    Mol. Cell 6:11-22(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION.
    Strain: 129 and C57BL/6J.
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  5. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  6. "Functional uncoupling between Ca2+ release and afterhyperpolarization in mutant hippocampal neurons lacking junctophilins."
    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.
    Proc. Natl. Acad. Sci. U.S.A. 103:10811-10816(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  7. Cited for: DISRUPTION PHENOTYPE.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440; THR-451; SER-457; THR-471; SER-475; SER-699 AND SER-706, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiJPH3_MOUSE
AccessioniPrimary (citable) accession number: Q9ET77
Secondary accession number(s): Q3ZAS3, Q8BNM7, Q9EQZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: March 1, 2001
Last modified: July 6, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.