JPH1_MOUSE
ID JPH1_MOUSE Reviewed; 660 AA.
AC Q9ET80; Q0VB08; Q9EQZ3;
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-1;
DE Short=JP-1;
DE AltName: Full=Junctophilin type 1;
GN Name=Jph1; Synonyms=Jp1;
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 TISSUE SPECIFICITY.
RC STRAIN=129, and C57BL/6J; TISSUE=Skeletal muscle;
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 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 [3]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11535622; DOI=10.1083/jcb.200105040;
RA Ito K., Komazaki S., Sasamoto K., Yoshida M., Nishi M., Kitamura K.,
RA Takeshima H.;
RT "Deficiency of triad junction and contraction in mutant skeletal muscle
RT lacking junctophilin type 1.";
RL J. Cell Biol. 154:1059-1067(2001).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12135771; DOI=10.1016/s0014-5793(02)03042-9;
RA Komazaki S., Ito K., Takeshima H., Nakamura H.;
RT "Deficiency of triad formation in developing skeletal muscle cells lacking
RT junctophilin type 1.";
RL FEBS Lett. 524:225-229(2002).
RN [5]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=12729900; DOI=10.1016/s0014-5793(03)00340-5;
RA Komazaki S., Nishi M., Takeshima H.;
RT "Abnormal junctional membrane structures in cardiac myocytes expressing
RT ectopic junctophilin type 1.";
RL FEBS Lett. 542:69-73(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
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. JPH1 contributes to
CC the construction of the skeletal muscle triad by linking the t-tubule
CC (transverse-tubule) and SR (sarcoplasmic reticulum) membranes.
CC {ECO:0000269|PubMed:11535622, ECO:0000269|PubMed:12135771,
CC ECO:0000269|PubMed:12729900}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC Endoplasmic reticulum membrane; Single-pass type IV membrane protein.
CC Sarcoplasmic reticulum membrane; Single-pass type IV membrane protein.
CC Note=Predominantly on the plasma membrane. The transmembrane domain is
CC anchored in endoplasmic/sarcoplasmic reticulum membrane, while the N-
CC terminal part associates with the plasma membrane. In skeletal muscle
CC cells, it is predominantly localized at the junction of the A and I
CC bands.
CC -!- TISSUE SPECIFICITY: Specifically expressed in skeletal muscle. Weakly
CC expressed in embryos and neonates. Abundant in young adult muscles.
CC {ECO:0000269|PubMed:10949023, ECO:0000269|PubMed:11535622}.
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 unable to suckle probably due to
CC defective E-C coupling in jaw muscles, and die shortly after birth. In
CC skeletal muscles, triad junctions are reduced in number. Mutant mice
CC developed less contractile force and abnormal sensitivities to
CC extracellular Ca(2+) were observed. Sarcoplasmic reticulum is often
CC structurally abnormal. {ECO:0000269|PubMed:11535622,
CC ECO:0000269|PubMed:12135771}.
CC -!- SIMILARITY: Belongs to the junctophilin family. {ECO:0000305}.
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DR EMBL; AB024445; BAB12043.1; -; mRNA.
DR EMBL; AB024446; BAB20319.1; -; Genomic_DNA.
DR EMBL; BC120839; AAI20840.1; -; mRNA.
DR EMBL; BC137669; AAI37670.1; -; mRNA.
DR CCDS; CCDS14833.1; -.
DR RefSeq; NP_065629.1; NM_020604.2.
DR RefSeq; XP_011236698.1; XM_011238396.2.
DR RefSeq; XP_011236699.1; XM_011238397.2.
DR RefSeq; XP_011236700.1; XM_011238398.2.
DR RefSeq; XP_011236701.1; XM_011238399.2.
DR AlphaFoldDB; Q9ET80; -.
DR SMR; Q9ET80; -.
DR IntAct; Q9ET80; 1.
DR STRING; 10090.ENSMUSP00000039072; -.
DR iPTMnet; Q9ET80; -.
DR PhosphoSitePlus; Q9ET80; -.
DR MaxQB; Q9ET80; -.
DR PaxDb; Q9ET80; -.
DR PeptideAtlas; Q9ET80; -.
DR PRIDE; Q9ET80; -.
DR ProteomicsDB; 301700; -.
DR Antibodypedia; 2291; 157 antibodies from 27 providers.
DR DNASU; 57339; -.
DR Ensembl; ENSMUST00000038382; ENSMUSP00000039072; ENSMUSG00000042686.
DR GeneID; 57339; -.
DR KEGG; mmu:57339; -.
DR UCSC; uc007aka.2; mouse.
DR CTD; 56704; -.
DR MGI; MGI:1891495; Jph1.
DR VEuPathDB; HostDB:ENSMUSG00000042686; -.
DR eggNOG; KOG0231; Eukaryota.
DR GeneTree; ENSGT00940000156130; -.
DR HOGENOM; CLU_008078_1_0_1; -.
DR InParanoid; Q9ET80; -.
DR OMA; NFHADTE; -.
DR OrthoDB; 904294at2759; -.
DR PhylomeDB; Q9ET80; -.
DR TreeFam; TF317210; -.
DR BioGRID-ORCS; 57339; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q9ET80; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9ET80; protein.
DR Bgee; ENSMUSG00000042686; Expressed in triceps brachii and 195 other tissues.
DR ExpressionAtlas; Q9ET80; baseline and differential.
DR Genevisible; Q9ET80; 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; IEA:UniProtKB-KW.
DR GO; GO:0030314; C:junctional membrane complex; IDA:UniProtKB.
DR GO; GO:0014701; C:junctional sarcoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0008307; F:structural constituent of muscle; IMP:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; IMP: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; 7.
PE 1: Evidence at protein level;
KW Cell membrane; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Sarcoplasmic reticulum; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..660
FT /note="Junctophilin-1"
FT /id="PRO_0000159845"
FT TOPO_DOM 1..638
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 639..659
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT REPEAT 14..36
FT /note="MORN 1"
FT REPEAT 38..59
FT /note="MORN 2"
FT REPEAT 60..82
FT /note="MORN 3"
FT REPEAT 106..128
FT /note="MORN 4"
FT REPEAT 129..151
FT /note="MORN 5"
FT REPEAT 281..303
FT /note="MORN 6"
FT REPEAT 304..326
FT /note="MORN 7"
FT REGION 228..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HDC5"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HDC5"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HDC5"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HDC5"
FT MOD_RES 461
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HDC5"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HDC5"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HDC5"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HDC5"
SQ SEQUENCE 660 AA; 71905 MW; CC307C68F1250831 CRC64;
MTGGRFDFDD GGTYCGGWEE GKAHGHGICT GPKGQGEYSG SWSHGFEVVG VYTWPSGNTY
QGYWAQGKRH GLGVETKGKW MYRGEWSHGF KGRYGVRQSL CTPARYEGTW SNGLQDGYGV
ETYGDGGTYQ GQWAGGMRHG YGVRQSVPYG MATVIRSPLR TSLASLRSEQ SNGSVLHEAA
AAAADSPAGT RGGFVLNFHA DTELGKKKGG LFRRGSLLGS MKLRKSESKS SISSKRSSVR
SDAAMSRISS SDANSTISFG DVDCDFCPVE DHVDATTTET YMGEWKNDKR NGFGISERSN
GMKYEGEWAN NKRHGYGCTV FPDGSKEEGK YKNNILVRGI RKQLIPIRNT KTREKVDRAI
EGAQRAAAMA RTKVEIANSR TAHARAKADA ADQAALAARQ ECDIARAVAR ELSPDFYQPG
PDYIKQRCQE GGDIKENPEE KVLEKPPSPK ESPHFYRKGT TPPRSPESSP KQSHSPQPSS
PEPSKKQNPS PGARLSQDKQ SLAEEQVTAF VNKPSMSKAP AKELGASVSK YSGRHHVPNP
SNGELHSQYH GYYVKLNTPQ HPPEDREDDR GVSQSSSALV PRPSPNKWGP PKSVTKPVAK
ESKTEPKAKK SELAIPKNPA SNDTCPSLEK EANSGPNSIM IVLVMLLNIG LAILFVHFLT
