CCG1_PIG
ID CCG1_PIG Reviewed; 224 AA.
AC Q2MJQ7;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle;
RA He B., Xiong Y.Z., Zheng R.;
RT "Isolation and characterization of the porcine CACNG1 gene.";
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P19518}.
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:0000250|UniProtKB:P19518}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P19518}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P19518}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P19518}.
CC -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. CACNG subfamily.
CC {ECO:0000305}.
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DR EMBL; DQ323981; ABC54852.1; -; mRNA.
DR RefSeq; NP_001038070.1; NM_001044605.1.
DR AlphaFoldDB; Q2MJQ7; -.
DR SMR; Q2MJQ7; -.
DR STRING; 9823.ENSSSCP00000018299; -.
DR PaxDb; Q2MJQ7; -.
DR PeptideAtlas; Q2MJQ7; -.
DR PRIDE; Q2MJQ7; -.
DR Ensembl; ENSSSCT00000018801; ENSSSCP00000018299; ENSSSCG00000017271.
DR Ensembl; ENSSSCT00015041199; ENSSSCP00015016282; ENSSSCG00015031045.
DR Ensembl; ENSSSCT00025079056; ENSSSCP00025034322; ENSSSCG00025057753.
DR Ensembl; ENSSSCT00030074053; ENSSSCP00030033910; ENSSSCG00030053066.
DR Ensembl; ENSSSCT00040018271; ENSSSCP00040007495; ENSSSCG00040013701.
DR Ensembl; ENSSSCT00060074592; ENSSSCP00060032194; ENSSSCG00060054779.
DR GeneID; 733677; -.
DR KEGG; ssc:733677; -.
DR CTD; 786; -.
DR VGNC; VGNC:86124; CACNG1.
DR eggNOG; ENOG502QT5N; Eukaryota.
DR GeneTree; ENSGT00390000007786; -.
DR HOGENOM; CLU_093876_0_0_1; -.
DR InParanoid; Q2MJQ7; -.
DR OMA; LVGMSSM; -.
DR OrthoDB; 1261253at2759; -.
DR TreeFam; TF331651; -.
DR Proteomes; UP000008227; Chromosome 12.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000017271; Expressed in longissimus lumborum muscle and 6 other tissues.
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; IEA:Ensembl.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
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; IEA:Ensembl.
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 2: Evidence at transcript 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..224
FT /note="Voltage-dependent calcium channel gamma-1 subunit"
FT /id="PRO_0000261026"
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..110
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P19518"
FT TOPO_DOM 132..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P19518"
FT TOPO_DOM 158..181
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 182..206
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P19518"
FT TOPO_DOM 207..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..82
FT /evidence="ECO:0000250|UniProtKB:P19518"
SQ SEQUENCE 224 AA; 25093 MW; 64190DF6DD72DA08 CRC64;
MSQTKALKVR VTLFCILVGI VLALVAVVTD HWAVLSPHVE HLNATCEAAH FGLWRICTKR
IAVGDSKDKS CGPITLPGEK NCSYFRHFNP GETSEIFHVT TQKEYSISAA AIAIFSLGFI
ILGTICGLLS FRKKRDYLLR PASMFYAFAG LCIFVSVEVM RQSVKRMIDS EDTVWIDYYY
GWSFACACAA FILLFLGGIA LLLFSLPRMP QYPWESCMDA EPEH