CCG1_BOVIN
ID CCG1_BOVIN Reviewed; 223 AA.
AC Q08DE1;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC123800; AAI23801.1; -; mRNA.
DR RefSeq; NP_001073806.1; NM_001080337.1.
DR AlphaFoldDB; Q08DE1; -.
DR SMR; Q08DE1; -.
DR STRING; 9913.ENSBTAP00000009930; -.
DR PaxDb; Q08DE1; -.
DR Ensembl; ENSBTAT00000009930; ENSBTAP00000009930; ENSBTAG00000007547.
DR GeneID; 781184; -.
DR KEGG; bta:781184; -.
DR CTD; 786; -.
DR VEuPathDB; HostDB:ENSBTAG00000007547; -.
DR VGNC; VGNC:26686; CACNG1.
DR eggNOG; ENOG502QT5N; Eukaryota.
DR GeneTree; ENSGT00390000007786; -.
DR HOGENOM; CLU_093876_0_0_1; -.
DR InParanoid; Q08DE1; -.
DR OMA; WIEYYYG; -.
DR OrthoDB; 1261253at2759; -.
DR TreeFam; TF331651; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000007547; Expressed in laryngeal cartilage and 31 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..223
FT /note="Voltage-dependent calcium channel gamma-1 subunit"
FT /id="PRO_0000261025"
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; 24694 MW; 198E11649A515AA9 CRC64;
MSQTKTLKVR VALLCILVGI VLALVAVVTD HWAVLSPHVE HHNSTCEAAH FGLWRICTKR
IFVGDKERSC GPITLPGEKN CSYFRHFNPG ESSEIFEVTT QKEYSISAAA IAIFSLGFII
VGTLCALLSF RKKRDYLLRP ASMFYIFAGL CLSVSAEVMR QSVQRMVDSE HTAWIAHSLA
WSFICACVAA ALLLVGGLAL LLLALPRMPR DPWESCMDAE PEH