ID H2MBD0_ORYLA Unreviewed; 740 AA.
AC H2MBD0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Junctophilin {ECO:0000256|PIRNR:PIRNR037387};
GN Name=jph3b {ECO:0000313|Ensembl:ENSORLP00000015851.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000015851.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000015851.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000015851.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000015851.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000015851.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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.
CC {ECO:0000256|PIRNR:PIRNR037387}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR037387};
CC Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR037387}.
CC Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004163,
CC ECO:0000256|PIRNR:PIRNR037387}; Single-pass type IV membrane protein
CC {ECO:0000256|ARBA:ARBA00004163}. Membrane
CC {ECO:0000256|ARBA:ARBA00004211}; Single-pass type IV membrane protein
CC {ECO:0000256|ARBA:ARBA00004211}.
CC -!- SIMILARITY: Belongs to the junctophilin family.
CC {ECO:0000256|ARBA:ARBA00008599, ECO:0000256|PIRNR:PIRNR037387}.
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DR AlphaFoldDB; H2MBD0; -.
DR Ensembl; ENSORLT00000015852.2; ENSORLP00000015851.2; ENSORLG00000012654.2.
DR eggNOG; KOG0231; Eukaryota.
DR GeneTree; ENSGT00940000158707; -.
DR HOGENOM; CLU_008078_2_0_1; -.
DR TreeFam; TF317210; -.
DR Proteomes; UP000001038; Chromosome 6.
DR Bgee; ENSORLG00000012654; Expressed in brain and 5 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030314; C:junctional membrane complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 2.20.110.10; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 3.
DR InterPro; IPR017191; Junctophilin.
DR InterPro; IPR003409; MORN.
DR PANTHER; PTHR23085; GH28348P; 1.
DR PANTHER; PTHR23085:SF7; JUNCTOPHILIN-3; 1.
DR Pfam; PF02493; MORN; 7.
DR PIRSF; PIRSF037387; Junctophilin; 1.
DR SMART; SM00698; MORN; 6.
DR SUPFAM; SSF82185; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 3.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|PIRNR:PIRNR037387};
KW Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR037387};
KW Membrane {ECO:0000256|PIRNR:PIRNR037387, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 716..739
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 234..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..501
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 740 AA; 80216 MW; 536E255E330C5D65 CRC64;
MSTGGRFNFD DGGSYCGGWE EGKAHGYGIC TGPKGQGEYC GSWAHGFELL GVYTWPSGNT
YQGTWAQGKR HGVGIENKGR WVYKGEWTHG FKGRYGLRES TGTSGKYEGT WNNGLQDGYG
TETYSDGGTF QGQWVGGMRH GYGVRQSVPY GMAAVIRSPL RTSINSLRSG SEHSNGTALV
SMCSTGSSGS SPAVSRGGFV LTAHSEAELL KGKRKSGLFR RSILSGLKLR KSESRSSLAS
QRSKQSSFRS EAGMSTVSSA ASDVNSTISL GDADAELAVA DDDVDATTTE TYCGEWKNDK
RTGFGVSRRS DGLQYEGEWL SNKRHGYGCT TFPDGTKEEG KYKQNILVSG KRKNLIPLRA
SKIREKVDRA VEGAQKAADI ARQKAEIALS RTAHAQGKAE AAVAAAQKAQ EESRMARVTA
KQFSPSFQHP GNGMEVQRPK RQVSSEVEGE GLSSSAGTAE SPDLYMKSVG SDDPSIDAVT
PDLSPPSSSP PHTPPPPARP SQRSKSARFH RQTAVDHGEK GKEGADRGEK SGEYTRANSW
SEDKKRGVFP KGGSGVSGRG TSRTNGHKHS SSNHKSREHG SSNHRQARGD MWTESSSSAT
WTSGHRGVHG RGGRLLEQDE EKISNYEMEM KPLQPRASIT HKPHGHGEDR HGEELSHGTT
RQRNKNRDSR DGGKDSLHKL DRLGEKVDSR PLRRDLTLSP PLKSSPIIPE RQDNSLTSIL
VVMVILLNIA VAILFIHFFI
//
