ID   CCG1_RAT                Reviewed;         223 AA.
AC   P97707;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 111.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RC   TISSUE=Skeletal muscle;
RX   PubMed=9049149; DOI=10.1007/s004240050324;
RA   Eberst R., Dai S., Klugbauer N., Hofmann F.;
RT   "Identification and functional characterization of a calcium channel gamma
RT   subunit.";
RL   Pflugers Arch. 433:633-637(1997).
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:9049149}.
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 (Probable). The channel complex contains
CC       alpha, beta, gamma and delta subunits in a 1:1:1:1 ratio, i.e. it
CC       contains either CACNB1 or CACNB2 (By similarity).
CC       {ECO:0000250|UniProtKB:P19518, ECO:0000305|PubMed:9049149}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC       {ECO:0000250|UniProtKB:P19518}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P19518}.
CC   -!- TISSUE SPECIFICITY: Skeletal muscle. {ECO:0000269|PubMed:9049149}.
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; Y09453; CAA70602.1; -; mRNA.
DR   RefSeq; NP_062128.1; NM_019255.1.
DR   AlphaFoldDB; P97707; -.
DR   SMR; P97707; -.
DR   STRING; 10116.ENSRNOP00000004349; -.
DR   GlyGen; P97707; 2 sites.
DR   PaxDb; P97707; -.
DR   GeneID; 29658; -.
DR   KEGG; rno:29658; -.
DR   UCSC; RGD:2249; rat.
DR   CTD; 786; -.
DR   RGD; 2249; Cacng1.
DR   eggNOG; ENOG502QT5N; Eukaryota.
DR   InParanoid; P97707; -.
DR   OrthoDB; 1261253at2759; -.
DR   PhylomeDB; P97707; -.
DR   PRO; PR:P97707; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:1990454; C:L-type voltage-gated calcium channel complex; IMP: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; IMP:UniProtKB.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; ISO:RGD.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; ISO:RGD.
DR   GO; GO:1902514; P:regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; IDA:UniProtKB.
DR   GO; GO:0070296; P:sarcoplasmic reticulum calcium ion transport; ISO:RGD.
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_0000164672"
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;  25119 MW;  A9EA30B625E41CCC CRC64;
     MSQTKTAKVR VTLFFILAGG VLAMVAVVTD HWAVLSPHLE HHNETCVAAH FGLWRICTTW
     VAMHNQDKNC DGTIPAGEKN CSYFRHFNPG ESSEIFEFTT QKEYSISAAA IAIFSLGFII
     IGSICAFLSF GNKRDYLLRP ASMFYAFAGL CLIVSVEVMR QSVKRMIDSE DTVWIEYYYS
     WSFACACAGF TLLFLGGLFL LLFSLPRMPQ NPWESCMDTE SEH