ID M4AJL6_XIPMA Unreviewed; 228 AA.
AC M4AJL6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Voltage-dependent calcium channel gamma-1 subunit {ECO:0000256|ARBA:ARBA00019950, ECO:0000256|RuleBase:RU363085};
DE AltName: Full=Dihydropyridine-sensitive L-type, skeletal muscle calcium channel subunit gamma {ECO:0000256|ARBA:ARBA00029680, ECO:0000256|RuleBase:RU363085};
GN Name=CACNG1 {ECO:0000313|Ensembl:ENSXMAP00000014660.1};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000014660.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000014660.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000014660.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Regulatory subunit of the voltage-gated calcium channel that
CC gives rise to L-type calcium currents in skeletal muscle. Regulates
CC channel inactivation kinetics. {ECO:0000256|ARBA:ARBA00003367,
CC ECO:0000256|RuleBase:RU363085}.
CC -!- SUBUNIT: Component of a calcium channel complex consisting of a pore-
CC forming alpha subunit (CACNA1S) and the ancillary subunits CACNB1 or
CC CACNB2, CACNG1 and CACNA2D1. The channel complex contains alpha, beta,
CC gamma and delta subunits in a 1:1:1:1 ratio, i.e. it contains either
CC CACNB1 or CACNB2. {ECO:0000256|RuleBase:RU363085}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000256|ARBA:ARBA00004415}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004415}. Membrane
CC {ECO:0000256|RuleBase:RU363085}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU363085}.
CC -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. CACNG subfamily.
CC {ECO:0000256|ARBA:ARBA00007111, ECO:0000256|RuleBase:RU363085}.
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DR RefSeq; XP_005808803.1; XM_005808746.1.
DR AlphaFoldDB; M4AJL6; -.
DR STRING; 8083.ENSXMAP00000014660; -.
DR Ensembl; ENSXMAT00000014680.2; ENSXMAP00000014660.1; ENSXMAG00000014634.2.
DR GeneID; 102237380; -.
DR KEGG; xma:102237380; -.
DR eggNOG; ENOG502QT5N; Eukaryota.
DR GeneTree; ENSGT00390000007786; -.
DR HOGENOM; CLU_093876_0_0_1; -.
DR InParanoid; M4AJL6; -.
DR OMA; FMQEQGP; -.
DR OrthoDB; 4230292at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR Gene3D; 1.20.140.150; -; 1.
DR InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR InterPro; IPR005421; VDCC_g1su.
DR InterPro; IPR008368; VDCC_gsu.
DR PANTHER; PTHR15025:SF1; VOLTAGE-DEPENDENT CALCIUM CHANNEL GAMMA-1 SUBUNIT; 1.
DR PANTHER; PTHR15025; VOLTAGE-DEPENDENT CALCIUM CHANNEL GAMMA-1 SUBUNIT-RELATED; 1.
DR Pfam; PF13903; Claudin_2; 1.
DR PRINTS; PR01792; VDCCGAMMA.
DR PRINTS; PR01601; VDCCGAMMA1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU363085};
KW Calcium channel {ECO:0000256|ARBA:ARBA00022673,
KW ECO:0000256|RuleBase:RU363085};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW ECO:0000256|RuleBase:RU363085};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU363085};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU363085};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363085};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363085};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363085};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU363085};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW ECO:0000256|RuleBase:RU363085}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363085"
FT TRANSMEM 109..133
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363085"
FT TRANSMEM 140..161
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363085"
FT TRANSMEM 181..206
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363085"
SQ SEQUENCE 228 AA; 25483 MW; 3DA8FE51496EB671 CRC64;
MFEEQVTKVK ITSVVIVVGM SAMLAAVVTD HWAVLSPRVE KLNATCEAAH FGLWRLCKKT
IFMMKEDPQG KGCGPISLPG AKNCSYFKHF TSGEEAEVFE VKTQKEYNIS AAAIAIFSLF
FMILGTLCVI FSFGKGRDYL LRPAGMFFAF AGLCIIISVE VMRQSVKRMI DSDETIWIEY
YYSWSFTCAC ASFTLLILSG AALLLISMPH MPRNPWETCM DAEPDTLD
//