JSPR1_MOUSE
ID JSPR1_MOUSE Reviewed; 332 AA.
AC Q3MI48; Q9D755;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Junctional sarcoplasmic reticulum protein 1;
DE AltName: Full=Junctional-face membrane protein of 45 kDa homolog;
DE Short=JP-45;
GN Name=Jsrp1; Synonyms=Jp45;
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), INTERACTION WITH CALSEQUESTRIN AND
RP CACNA1S, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Skeletal muscle;
RX PubMed=12871958; DOI=10.1074/jbc.m305016200;
RA Anderson A.A., Treves S., Biral D., Betto R., Sandona D., Ronjat M.,
RA Zorzato F.;
RT "The novel skeletal muscle sarcoplasmic reticulum JP-45 protein. Molecular
RT cloning, tissue distribution, developmental expression, and interaction
RT with alpha 1.1 subunit of the voltage-gated calcium channel.";
RL J. Biol. Chem. 278:39987-39992(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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] OF 16-332 (ISOFORM 1).
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, AND INTERACTION WITH CACNA1S AND CACNB1.
RX PubMed=16638807; DOI=10.1242/jcs.02935;
RA Anderson A.A., Altafaj X., Zheng Z., Wang Z.-M., Delbono O., Ronjat M.,
RA Treves S., Zorzato F.;
RT "The junctional SR protein JP-45 affects the functional expression of the
RT voltage-dependent Ca2+ channel Cav1.1.";
RL J. Cell Sci. 119:2145-2155(2006).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16423849; DOI=10.1113/jphysiol.2005.104406;
RA Gouadon E., Schuhmeier R.P., Ursu D., Anderson A.A., Treves S., Zorzato F.,
RA Lehmann-Horn F., Melzer W.;
RT "A possible role of the junctional face protein JP-45 in modulating Ca2+
RT release in skeletal muscle.";
RL J. Physiol. (Lond.) 572:269-280(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51; SER-223 AND SER-228, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Lung;
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: Involved in skeletal muscle excitation/contraction coupling
CC (EC), probably acting as a regulator of the voltage-sensitive calcium
CC channel CACNA1S (By similarity). EC is a physiological process whereby
CC an electrical signal (depolarization of the plasma membrane) is
CC converted into a chemical signal, a calcium gradient, by the opening of
CC ryanodine receptor calcium release channels. May regulate CACNA1S
CC membrane targeting and activity. {ECO:0000250,
CC ECO:0000269|PubMed:16423849, ECO:0000269|PubMed:16638807}.
CC -!- SUBUNIT: Interacts with CACNA1S, CACNB1 and calsequestrin.
CC {ECO:0000269|PubMed:12871958, ECO:0000269|PubMed:16638807}.
CC -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane. Endoplasmic
CC reticulum membrane. Note=Colocalizes with ryanodine receptors at the
CC sarcoplasmic reticulum triad membranes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3MI48-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3MI48-2; Sequence=VSP_030199, VSP_030200;
CC -!- TISSUE SPECIFICITY: Specifically expressed in skeletal muscle. Detected
CC in skeletal muscle and tongue (at protein level).
CC {ECO:0000269|PubMed:12871958}.
CC -!- DEVELOPMENTAL STAGE: Expression appears in 17 dpc embryos, peaks 2
CC months after birth and decreases during aging.
CC {ECO:0000269|PubMed:12871958}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK009016; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK009016; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK009578; BAB26371.1; -; mRNA.
DR EMBL; BC104136; AAI04137.1; -; mRNA.
DR EMBL; BC104137; AAI04138.1; -; mRNA.
DR CCDS; CCDS24034.2; -. [Q3MI48-1]
DR AlphaFoldDB; Q3MI48; -.
DR STRING; 10090.ENSMUSP00000137666; -.
DR iPTMnet; Q3MI48; -.
DR PhosphoSitePlus; Q3MI48; -.
DR MaxQB; Q3MI48; -.
DR PaxDb; Q3MI48; -.
DR PeptideAtlas; Q3MI48; -.
DR PRIDE; Q3MI48; -.
DR ProteomicsDB; 269426; -. [Q3MI48-1]
DR ProteomicsDB; 269427; -. [Q3MI48-2]
DR Antibodypedia; 42291; 42 antibodies from 15 providers.
DR Ensembl; ENSMUST00000020435; ENSMUSP00000020435; ENSMUSG00000020216. [Q3MI48-2]
DR UCSC; uc007geu.2; mouse. [Q3MI48-2]
DR MGI; MGI:1916700; Jsrp1.
DR VEuPathDB; HostDB:ENSMUSG00000020216; -.
DR eggNOG; ENOG502S4JK; Eukaryota.
DR GeneTree; ENSGT00390000012911; -.
DR HOGENOM; CLU_073497_0_0_1; -.
DR InParanoid; Q3MI48; -.
DR PhylomeDB; Q3MI48; -.
DR TreeFam; TF337976; -.
DR ChiTaRS; Jsrp1; mouse.
DR PRO; PR:Q3MI48; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q3MI48; protein.
DR Bgee; ENSMUSG00000020216; Expressed in hindlimb stylopod muscle and 78 other tissues.
DR ExpressionAtlas; Q3MI48; baseline and differential.
DR Genevisible; Q3MI48; MM.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:MGI.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0072657; P:protein localization to membrane; IMP:MGI.
DR GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IMP:MGI.
DR GO; GO:0003009; P:skeletal muscle contraction; ISS:UniProtKB.
DR InterPro; IPR026178; JSRP1.
DR PANTHER; PTHR22397; PTHR22397; 1.
DR Pfam; PF15312; JSRP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW Reference proteome; Sarcoplasmic reticulum.
FT CHAIN 1..332
FT /note="Junctional sarcoplasmic reticulum protein 1"
FT /id="PRO_0000314026"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..80
FT /note="Mediates interaction with CACNA1S"
FT REGION 159..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..119
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..201
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..40
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030199"
FT VAR_SEQ 41..52
FT /note="TSRRADSSDWTH -> MLGTESWLPACW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030200"
FT CONFLICT 34
FT /note="R -> P (in Ref. 3; AAI04137/AAI04138)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 36093 MW; 35A9DE3C332DC148 CRC64;
MTTRGLEDLD GGLGSCLPSD DLPFLEEPAS GRRRESKARG TSRRADSSDW THVLQDPVAA
GAGDAGLKKM EKELAGKEST AGKAGTSPRI VPARRKPQAP PPLQPPPPPL QPPPRTPSDD
LPWGDLTLNK CLVLASLVAL LGSALQLCRD AVAGEVVAAP HPWVPPSSPP KKEASPAPKP
PVLVSPSGSP QPKPGPPQAR MQDEPELPGS PEATETRVER GGSISEASGE ESVPLGDRGS
QEKPRKEKPS KGEKLKKEKP RREKPRREDK SQVTGEPRQS LPRRWEAREG GRRPWGRDSR
DLLEHGKLQA WAPRRRHDRD DRPRQKRGKG RD
