JPH4_RAT
ID JPH4_RAT Reviewed; 630 AA.
AC Q69FB3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Junctophilin-4;
DE Short=JP-4;
DE AltName: Full=Junctophilin-like 1 protein;
GN Name=Jph4 {ECO:0000312|RGD:1303170};
GN Synonyms=Jphl1 {ECO:0000250|UniProtKB:Q96JJ6};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAR08902.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar {ECO:0000312|EMBL:AAR08902.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAR08902.1};
RA Savaskan N.E., Brauer A.U.;
RT "Molecular cloning and functional characterization of a novel subclass of
RT junctophilins in the brain.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
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. JPH4 is brain-
CC specific and appears to have an active role in certain neurons involved
CC in motor coordination and memory (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q9ET77}.
CC Note=Localized predominantly on the plasma membrane. The transmembrane
CC domain is anchored in endoplasmic reticulum membrane, while the N-
CC terminal part associates with the plasma membrane (By similarity).
CC {ECO:0000250}.
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|UniProtKB:Q9GKY7}.
CC -!- SIMILARITY: Belongs to the junctophilin family. {ECO:0000255}.
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DR EMBL; AY341260; AAR08902.1; -; mRNA.
DR RefSeq; NP_001003711.1; NM_001003711.1.
DR AlphaFoldDB; Q69FB3; -.
DR SMR; Q69FB3; -.
DR BioGRID; 268735; 1.
DR STRING; 10116.ENSRNOP00000034702; -.
DR PaxDb; Q69FB3; -.
DR GeneID; 445271; -.
DR KEGG; rno:445271; -.
DR UCSC; RGD:1303170; rat.
DR CTD; 84502; -.
DR RGD; 1303170; Jph4.
DR eggNOG; KOG0231; Eukaryota.
DR InParanoid; Q69FB3; -.
DR OrthoDB; 904294at2759; -.
DR PhylomeDB; Q69FB3; -.
DR TreeFam; TF317210; -.
DR PRO; PR:Q69FB3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0043198; C:dendritic shaft; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030314; C:junctional membrane complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; ISO:RGD.
DR GO; GO:0007612; P:learning; ISO:RGD.
DR GO; GO:0050885; P:neuromuscular process controlling balance; ISO:RGD.
DR GO; GO:0001817; P:regulation of cytokine production; ISO:RGD.
DR GO; GO:2001256; P:regulation of store-operated calcium entry; ISO:RGD.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISO:RGD.
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; 6.
PE 2: Evidence at transcript level;
KW Cell membrane; Endoplasmic reticulum; Membrane; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..630
FT /note="Junctophilin-4"
FT /id="PRO_0000259404"
FT TOPO_DOM 1..608
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 609..629
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 17..39
FT /note="MORN 1"
FT /evidence="ECO:0000255"
FT REPEAT 41..62
FT /note="MORN 2"
FT /evidence="ECO:0000255"
FT REPEAT 63..84
FT /note="MORN 3"
FT /evidence="ECO:0000255"
FT REPEAT 85..107
FT /note="MORN 4"
FT /evidence="ECO:0000255"
FT REPEAT 108..130
FT /note="MORN 5"
FT /evidence="ECO:0000255"
FT REPEAT 131..153
FT /note="MORN 6"
FT /evidence="ECO:0000255"
FT REPEAT 284..306
FT /note="MORN 7"
FT /evidence="ECO:0000255"
FT REPEAT 307..329
FT /note="MORN 8"
FT /evidence="ECO:0000255"
FT REGION 160..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..184
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 630 AA; 66441 MW; EE0DB8E0444A41E8 CRC64;
MHVPLGRKFD FDDGGCYVGG WEAGRAHGYG VCTGPGAQGE YSGCWAHGFE SLGVFTGPGG
HSYQGHWQQG KREGLGVERK SRWTYRGEWL GGLKGRSGVW ESVSGLRYAG LWKDGFQDGY
GTETYSDGGT YQGQWQAGKR HGYGVRQSVP YHQAALLRSP RRTSLDSGHS DPPTPPPPLP
LPGDEGGSPA SGSRGGFVLA GPGDADGASS RKRTPAAGGF FRRSLLLSGL RAGGRRSSLG
SKRGSLRSEV SSEVGSTGPP GSEASGPPIP APPALIEGSA TEVYAGEWRA DRRSGYGVSQ
RSNGLRYEGE WLGNRRHGYG RTTRPDGSRE EGKYKRNRLV HGGRVRSLLP LALRRGKVKE
KVDRAVEGAR RAVSAARQRQ EIAAARAADA LLKAVAASSV AEKAVEAARM AKLIAQDLQP
MLEAPGRRPR QDSGGSDTEP LDEDSPGVYE NGLTPSEGSP ELPSSPASSH QPWRAPPCRS
PLPPGGNWGP FSSPKAWPEE WGGPGEQAEE LAGYEAEDEA GMQGPGPRDG SPLLGGCSDS
SGSLREEEGE DEESLPQLRA PGGSESEPVT TPVLRGLSSR GPDAGCLTEE FEEPAATERP
AQPGAANPLV VGAVALLDLS LAFLFSQLLT
