ID   CCG1_MOUSE              Reviewed;         223 AA.
AC   O70578;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   24-JAN-2024, entry version 151.
DE   RecName: Full=Voltage-dependent calcium channel gamma-1 subunit;
DE   AltName: Full=Dihydropyridine-sensitive L-type, skeletal muscle calcium channel subunit gamma;
GN   Name=Cacng1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=129/SvJ; TISSUE=Skeletal muscle;
RX   PubMed=9504716; DOI=10.1515/bchm.1998.379.1.45;
RA   Wissenbach U., Bosse-Doenecke E., Freise D., Ludwig A., Murakami M.,
RA   Hofmann F., Flockerzi V.;
RT   "The structure of the murine calcium channel gamma-subunit gene and
RT   protein.";
RL   Biol. Chem. 379:45-50(1998).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=10799530; DOI=10.1074/jbc.275.19.14476;
RA   Freise D., Held B., Wissenbach U., Pfeifer A., Trost C., Himmerkus N.,
RA   Schweig U., Freichel M., Biel M., Hofmann F., Hoth M., Flockerzi V.;
RT   "Absence of the gamma subunit of the skeletal muscle dihydropyridine
RT   receptor increases L-type Ca2+ currents and alters channel inactivation
RT   properties.";
RL   J. Biol. Chem. 275:14476-14481(2000).
RN   [3]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=12409298; DOI=10.1074/jbc.m208689200;
RA   Arikkath J., Chen C.C., Ahern C., Allamand V., Flanagan J.D., Coronado R.,
RA   Gregg R.G., Campbell K.P.;
RT   "Gamma 1 subunit interactions within the skeletal muscle L-type voltage-
RT   gated calcium channels.";
RL   J. Biol. Chem. 278:1212-1219(2003).
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:0000269|PubMed:10799530,
CC       ECO:0000269|PubMed:12409298}.
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 (PubMed:10799530, PubMed:12409298). The
CC       channel complex contains alpha, beta, gamma and delta subunits in a
CC       1:1:1:1 ratio, i.e. it contains either CACNB1 or CACNB2 (By
CC       similarity). {ECO:0000250|UniProtKB:P19518,
CC       ECO:0000269|PubMed:10799530, ECO:0000269|PubMed:12409298}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC       {ECO:0000305|PubMed:10799530, ECO:0000305|PubMed:9504716}; Multi-pass
CC       membrane protein {ECO:0000250|UniProtKB:P19518}.
CC   -!- TISSUE SPECIFICITY: Detected in skeletal muscle (at protein level).
CC       {ECO:0000269|PubMed:10799530, ECO:0000269|PubMed:9504716}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P19518}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC       {ECO:0000269|PubMed:10799530}.
CC   -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. CACNG subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ006306; CAA06966.1; -; mRNA.
DR   CCDS; CCDS25570.1; -.
DR   RefSeq; NP_031608.1; NM_007582.2.
DR   AlphaFoldDB; O70578; -.
DR   SMR; O70578; -.
DR   ComplexPortal; CPX-3191; Skeletal muscle VGCC complex.
DR   STRING; 10090.ENSMUSP00000021065; -.
DR   GlyCosmos; O70578; 2 sites, No reported glycans.
DR   GlyGen; O70578; 2 sites.
DR   PhosphoSitePlus; O70578; -.
DR   PaxDb; 10090-ENSMUSP00000021065; -.
DR   ProteomicsDB; 265720; -.
DR   Antibodypedia; 19201; 206 antibodies from 28 providers.
DR   DNASU; 12299; -.
DR   Ensembl; ENSMUST00000021065.6; ENSMUSP00000021065.6; ENSMUSG00000020722.6.
DR   GeneID; 12299; -.
DR   KEGG; mmu:12299; -.
DR   UCSC; uc007may.1; mouse.
DR   AGR; MGI:1206582; -.
DR   CTD; 786; -.
DR   MGI; MGI:1206582; Cacng1.
DR   VEuPathDB; HostDB:ENSMUSG00000020722; -.
DR   eggNOG; ENOG502QT5N; Eukaryota.
DR   GeneTree; ENSGT00390000007786; -.
DR   HOGENOM; CLU_093876_0_0_1; -.
DR   InParanoid; O70578; -.
DR   OMA; LPGEQNC; -.
DR   OrthoDB; 4230292at2759; -.
DR   PhylomeDB; O70578; -.
DR   TreeFam; TF331651; -.
DR   BioGRID-ORCS; 12299; 1 hit in 77 CRISPR screens.
DR   PRO; PR:O70578; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; O70578; Protein.
DR   Bgee; ENSMUSG00000020722; Expressed in hindlimb stylopod muscle and 64 other cell types or tissues.
DR   ExpressionAtlas; O70578; baseline and differential.
DR   GO; GO:1990454; C:L-type voltage-gated calcium channel complex; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
DR   GO; GO:0030315; C:T-tubule; ISS:UniProtKB.
DR   GO; GO:0005246; F:calcium channel regulator activity; ISS:UniProtKB.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IMP:MGI.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; IMP:MGI.
DR   GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR   GO; GO:0045933; P:positive regulation of muscle contraction; NAS:ComplexPortal.
DR   GO; GO:1902514; P:regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; ISS:UniProtKB.
DR   GO; GO:0070296; P:sarcoplasmic reticulum calcium ion transport; IMP:MGI.
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.
DR   Genevisible; O70578; MM.
PE   1: Evidence at protein level;
KW   Calcium; Calcium channel; Calcium transport; Cell membrane; Disulfide bond;
KW   Glycoprotein; Ion channel; Ion transport; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..223
FT                   /note="Voltage-dependent calcium channel gamma-1 subunit"
FT                   /id="PRO_0000164670"
FT   TOPO_DOM        1..10
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        11..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P19518"
FT   TOPO_DOM        30..109
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P19518"
FT   TOPO_DOM        131..135
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P19518"
FT   TOPO_DOM        157..180
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        181..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P19518"
FT   TOPO_DOM        206..223
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        57..81
FT                   /evidence="ECO:0000250|UniProtKB:P19518"
SQ   SEQUENCE   223 AA;  25120 MW;  3712F856CAFAE5F9 CRC64;
     MSQTKTAKVR VTLFFILVGG VLAMVAVVTD HWAVLSPHLE HHNETCEAAH FGLWRICTAR
     VAVHNKDKSC EHVTPSGEKN CSYFRHFNPG ESSEIFEFTT QKEYSISAAA IAIFSLGFII
     VGSICAFLSF GNKRDYLLRP ASMFYAFAGL CLIVSVEVMR QSVKRMIDSE DTVWIEHYYS
     WSFACACAAF ILLFLGGLFL LLFSLPRMPQ NPWESCMDAE PEH
//