CCG1_MOUSE
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 03-AUG-2022, entry version 143.
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 GlyGen; O70578; 2 sites.
DR PhosphoSitePlus; O70578; -.
DR PaxDb; O70578; -.
DR PRIDE; O70578; -.
DR ProteomicsDB; 265720; -.
DR Antibodypedia; 19201; 188 antibodies from 27 providers.
DR DNASU; 12299; -.
DR Ensembl; ENSMUST00000021065; ENSMUSP00000021065; ENSMUSG00000020722.
DR GeneID; 12299; -.
DR KEGG; mmu:12299; -.
DR UCSC; uc007may.1; mouse.
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; LVGMSSM; -.
DR OrthoDB; 1261253at2759; -.
DR PhylomeDB; O70578; -.
DR TreeFam; TF331651; -.
DR BioGRID-ORCS; 12299; 1 hit in 72 CRISPR screens.
DR PRO; PR:O70578; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O70578; protein.
DR Bgee; ENSMUSG00000020722; Expressed in hindlimb stylopod muscle and 63 other tissues.
DR ExpressionAtlas; O70578; baseline and differential.
DR Genevisible; O70578; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:1990454; C:L-type voltage-gated calcium channel complex; 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; IC: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 InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR InterPro; IPR005421; VDCC_g1su.
DR InterPro; IPR008368; VDCC_gsu.
DR Pfam; PF13903; Claudin_2; 1.
DR PRINTS; PR01792; VDCCGAMMA.
DR PRINTS; PR01601; VDCCGAMMA1.
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
