ID F6YGX0_HORSE Unreviewed; 657 AA.
AC F6YGX0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 2.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Junctophilin {ECO:0000256|PIRNR:PIRNR037387};
GN Name=JPH2 {ECO:0000313|VGNC:VGNC:51556};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000014371.2, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000014371.2, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000014371.2,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000014371.2}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000014371.2};
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; F6YGX0; -.
DR SMR; F6YGX0; -.
DR STRING; 9796.ENSECAP00000014371; -.
DR PaxDb; 9796-ENSECAP00000014371; -.
DR Ensembl; ENSECAT00000017678.4; ENSECAP00000014371.2; ENSECAG00000016786.4.
DR VGNC; VGNC:51556; JPH2.
DR GeneTree; ENSGT00940000159411; -.
DR HOGENOM; CLU_008078_4_1_1; -.
DR InParanoid; F6YGX0; -.
DR OMA; FEGYWSH; -.
DR TreeFam; TF317210; -.
DR Proteomes; UP000002281; Chromosome 22.
DR Bgee; ENSECAG00000016786; Expressed in triceps brachii and 14 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030314; C:junctional membrane complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0070300; F:phosphatidic acid binding; IEA:Ensembl.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IEA:Ensembl.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IEA:Ensembl.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:Ensembl.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IEA:Ensembl.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IEA:Ensembl.
DR GO; GO:0001786; F:phosphatidylserine binding; IEA:Ensembl.
DR GO; GO:0055074; P:calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR GO; GO:0055024; P:regulation of cardiac muscle tissue development; IEA:Ensembl.
DR Gene3D; 2.20.110.10; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 2.
DR InterPro; IPR017191; Junctophilin.
DR InterPro; IPR003409; MORN.
DR PANTHER; PTHR23085; GH28348P; 1.
DR PANTHER; PTHR23085:SF26; JUNCTOPHILIN-2; 1.
DR Pfam; PF02493; MORN; 8.
DR PIRSF; PIRSF037387; Junctophilin; 2.
DR SMART; SM00698; MORN; 6.
DR SUPFAM; SSF82185; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 2.
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:UP000002281};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 635..656
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 164..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..462
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 657 AA; 69925 MW; 5C1BF37D1C257358 CRC64;
MSGGRFDFDD GGAYCGGWEG GKAHGHGLCT GPKGQGEYSG SWNFGFEVAG VYTWPSGNTF
EGYWSHGKRH GLGIETKGRW LYKGEWTHGF KGRYGTRQSS SSGAKYEGTW NNGLQDGYGT
ETYADGGTYQ GQFTNGMRHG YGVRQSVPYG MAVVVRSPLR TSLSSLRSEH SNGTVGPDSP
TLLANATRPA RPARGLFPRS RTSVGSQRSR VSFLKSDLSS GSDAASTGSL GEGAEGADDA
APFEADIDAT TTETYMGEWK NDKRSGFGVS ERSSGLRYEG EWLDNLRHGY GCTTLPDGRR
EEGKYRHNVL VKGTKRRVLP LKSSKVRQKV EHGVEGAQRA AAIARQKAEI ALSRTSHAKA
KAEAAEQAAV AANQESNIAR TLARELAPDF YQPGPEYQKR RLLQEILENS ESLLEPPDRS
PGAAGLPERP RESPQLHERE TPRPEGGPPS PAGTPPQPKR PRPGASSKDG LLSPGAWNGE
SGPEGSRPAT PSEGAGRRSP ARPAAEHMAI EALQAPPAPS REPEVALYRG YHSYAVRTAP
PAPPPFDDEP EPDAAGSDSA PASPASAPAS PASAAAPDSP AKLEPKPIVP KAEPRAKARK
TEARGLTKGG AKKKARKEAA AAAEAEVEIE EVPNTVLICM VILLNIGLAI LFVHLLT
//
