JPH1_RABIT
ID JPH1_RABIT Reviewed; 662 AA.
AC Q9GKY8;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Junctophilin-1;
DE Short=JP-1;
DE AltName: Full=Junctophilin type 1;
DE AltName: Full=Mitsugumin-72;
DE Short=Mg72;
GN Name=JPH1; Synonyms=JP1, MG72;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC 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).
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 (By
CC 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}. Sarcoplasmic
CC reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein
CC {ECO:0000250}. Note=Localized predominantly on the plasma membrane. The
CC transmembrane domain is anchored in endoplasmic/sarcoplasmic reticulum
CC membrane, while the N-terminal part associates with the plasma
CC membrane. In skeletal muscle cells, it is predominantly localized at
CC the junction of the A and I bands (By similarity). {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.
CC -!- SIMILARITY: Belongs to the junctophilin family. {ECO:0000305}.
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DR EMBL; AB023447; BAB20311.1; -; mRNA.
DR RefSeq; NP_001075465.1; NM_001081996.1.
DR RefSeq; XP_008253859.1; XM_008255637.2.
DR RefSeq; XP_008253860.1; XM_008255638.2.
DR RefSeq; XP_008253861.1; XM_008255639.2.
DR AlphaFoldDB; Q9GKY8; -.
DR SMR; Q9GKY8; -.
DR STRING; 9986.ENSOCUP00000006651; -.
DR PRIDE; Q9GKY8; -.
DR Ensembl; ENSOCUT00000007691; ENSOCUP00000006651; ENSOCUG00000007692.
DR GeneID; 100008611; -.
DR KEGG; ocu:100008611; -.
DR CTD; 56704; -.
DR eggNOG; KOG0231; Eukaryota.
DR GeneTree; ENSGT00940000156130; -.
DR InParanoid; Q9GKY8; -.
DR OrthoDB; 904294at2759; -.
DR Proteomes; UP000001811; Chromosome 3.
DR Bgee; ENSOCUG00000007692; Expressed in skeletal muscle tissue and 15 other tissues.
DR ExpressionAtlas; Q9GKY8; baseline.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030314; C:junctional membrane complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; Phosphoprotein;
KW Reference proteome; Repeat; Sarcoplasmic reticulum; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..662
FT /note="Junctophilin-1"
FT /id="PRO_0000159846"
FT TOPO_DOM 1..640
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 641..661
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 432..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..634
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 448
FT /note="Phosphothreonine"
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 662 AA; 71846 MW; 5FB9C991CBA8684B CRC64;
MTGGRFDFDD GGTYCGGWEE GKAHGHGICT GPKGQGEYSG SWSHGFEVVG GYTWPSGNTY
QGYWAQGKRH GLGVETKGKW MYRGEWSHGF KGRYGVRQSL CTPARYEGTW SNGLQDGYGV
ETYGDGGTYQ GQWAGGMRHG YGVRQSVPYG MATVIRSPLR TSLASLRSEQ SNGSVLHDAA
AAADTPTGTR GGFVLNFHAD AELAGKKKGG LFRRGSLLGS MKLRKSESKS SISSKRSSVR
SDAAMSRISS SDANSTISFG DVDCDFCPVE DHVDATTTET YMGEWKNDKR NGFGISERSN
GMKYEGEWAN NKRHGYGCTV FPDGSKEEGK YKNNILVRGI RKQLIPIRNT KTREKVDRAI
EGAQRAAAMA RTKVEIANSR TAHARAKADA ADQAALAARQ ECDIARAVAR ELSPDFYQPG
PDYIKQRLQE GVDAKENPEE KVPAKPPTPK ESPHFYRKGT TPPGSPEASP KYSRSPQPSP
PKPAKKQNPS SGARLNQDKR GVAEEQVTAI VNKPLTSKAP TKEVGAAVSQ SKYSGRHHVP
NPSNGELHSQ YHGYYVKLHA PQHPPVDAED DDRSSPSSSA LVHKPSPNKW SPPKSVTKPV
AKESKAEPKA KKSELAIPKN PASNDSCPSM EREANSGPNS VMIVLVMLLN IGLAILFVHF
LT
