ID G1QM66_NOMLE Unreviewed; 661 AA.
AC G1QM66;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Junctophilin {ECO:0000256|PIRNR:PIRNR037387};
GN Name=JPH1 {ECO:0000313|Ensembl:ENSNLEP00000002032.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000002032.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000002032.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000002032.1}
RP IDENTIFICATION.
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 EMBL; ADFV01050379; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01050380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01050381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01050382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003269497.1; XM_003269449.2.
DR RefSeq; XP_003269498.1; XM_003269450.2.
DR AlphaFoldDB; G1QM66; -.
DR STRING; 61853.ENSNLEP00000002032; -.
DR Ensembl; ENSNLET00000002144.3; ENSNLEP00000002032.1; ENSNLEG00000001671.3.
DR GeneID; 100600957; -.
DR KEGG; nle:100600957; -.
DR CTD; 56704; -.
DR eggNOG; KOG0231; Eukaryota.
DR GeneTree; ENSGT00940000156130; -.
DR HOGENOM; CLU_008078_1_0_1; -.
DR InParanoid; G1QM66; -.
DR OMA; FSAQHNA; -.
DR OrthoDB; 5393283at2759; -.
DR TreeFam; TF317210; -.
DR Proteomes; UP000001073; Chromosome 16.
DR GO; GO:0030314; C:junctional membrane complex; IEA:UniProtKB-UniRule.
DR GO; GO:0014701; C:junctional sarcoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0008307; F:structural constituent of muscle; IEA:Ensembl.
DR GO; GO:0007517; P:muscle organ development; IEA:Ensembl.
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:SF6; JUNCTOPHILIN-1; 1.
DR Pfam; PF02493; MORN; 8.
DR PIRSF; PIRSF037387; Junctophilin; 1.
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:UP000001073};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 640..660
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 228..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 661 AA; 71742 MW; 768DC9FFCFFC237C CRC64;
MTGGRFDFDD GGTYCGGWEE GKAHGHGICT GPKGQGEYSG SWSHGFEVVG GYTWPSGNTY
QGYWAQGKRH GLGVETKGKW MYRGEWSHGF KGRYGVRQSL CTPARYEGTW SNGLQDGYGV
ETYGDGGTYQ GQWAGGMRHG YGVRQSVPYG MATVIRSPLR TSLASLRSEQ SNGSVLHDAA
AAADIPAGTR GGFVLNFHAD AELAGKKKGG LFRRGSLLGS MKLRKSESKS SISSKRSSVR
SDAAMSRISS SDANSTISFG DVDCDFCPVE DHVDATTTET YMGEWKNDKR NGFGVSERSN
GMKYEGEWAN NKRHGYGCTV FPDGSKEEGK YKNNILVRGI RKQLIPIRHT KTREKVDRAI
EGAQRAAAMA RTKVEIANSR TAHARAKADA ADQAALAARQ ECDIARAVAR ELSPDFYQPG
PDYVKQRFQE GVDAKENPEE KVPEKPPTPK ESPHFYRKGT TPPRSPEASP KHSHSPTSSP
KPLKKQNPSS GARLNQDKRS VADEQVTAIV NKPLMSKAPT KEAGAVVPQS KYSGRHHIPN
PSNGELHSQY HGYYVKLNAP QHPPVDVEDG DGSSQSSSAL VHKPSANKWS PSKSVTKPVA
KESKAEPKAK KSELAIPKNP ASNDSCPALE KEANSGPNSI MIVLVMLLNI GLAILFVHFL
T
//
