CCG1_RABIT
ID CCG1_RABIT Reviewed; 222 AA.
AC P19518;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 132.
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; Synonyms=CACNLG;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-9, SUBCELLULAR LOCATION,
RP SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Skeletal muscle;
RX PubMed=2158672; DOI=10.1126/science.2158672;
RA Jay S.D., Ellis S.B., McCue A.F., Williams M.E., Vedvick T.S.,
RA Harpold M.M., Campbell K.P.;
RT "Primary structure of the gamma subunit of the DHP-sensitive calcium
RT channel from skeletal muscle.";
RL Science 248:490-492(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=2163895; DOI=10.1016/0014-5793(90)80312-7;
RA Bosse E., Regulla S., Biel M., Ruth P., Meyer H.E., Flockerzi V.,
RA Hofmann F.;
RT "The cDNA and deduced amino acid sequence of the gamma subunit of the L-
RT type calcium channel from rabbit skeletal muscle.";
RL FEBS Lett. 267:153-156(1990).
RN [3]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
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).
RN [4] {ECO:0007744|PDB:3JBR}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS) IN COMPLEX WITH CACNA1S;
RP CACNB2 AND CACNA2D1, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE
RP SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=26680202; DOI=10.1126/science.aad2395;
RA Wu J., Yan Z., Li Z., Yan C., Lu S., Dong M., Yan N.;
RT "Structure of the voltage-gated calcium channel Cav1.1 complex.";
RL Science 350:2395-2395(2015).
RN [5] {ECO:0007744|PDB:5GJV, ECO:0007744|PDB:5GJW}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) IN COMPLEX WITH CACNA1S;
RP CACNB1 AND CACNA2D1, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP TOPOLOGY, IDENTIFICATION BY MASS SPECTROMETRY, AND DISULFIDE BONDS.
RX PubMed=27580036; DOI=10.1038/nature19321;
RA Wu J., Yan Z., Li Z., Qian X., Lu S., Dong M., Zhou Q., Yan N.;
RT "Structure of the voltage-gated calcium channel Ca(v)1.1 at 3.6A
RT resolution.";
RL Nature 537:191-196(2016).
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: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:2158672, PubMed:12409298,
CC PubMed:26680202, PubMed:27580036). The channel complex contains alpha,
CC beta, gamma and delta subunits in a 1:1:1:1 ratio, i.e. it contains
CC either CACNB1 or CACNB2 (PubMed:26680202, PubMed:27580036).
CC {ECO:0000269|PubMed:12409298, ECO:0000269|PubMed:2158672,
CC ECO:0000269|PubMed:26680202, ECO:0000269|PubMed:27580036}.
CC -!- INTERACTION:
CC P19518; P07293: CACNA1S; NbExp=3; IntAct=EBI-9683808, EBI-8613624;
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:12409298, ECO:0000269|PubMed:26680202,
CC ECO:0000269|PubMed:27580036, ECO:0000305|PubMed:2158672}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:26680202,
CC ECO:0000269|PubMed:27580036}.
CC -!- TISSUE SPECIFICITY: Skeletal muscle (at protein level).
CC {ECO:0000269|PubMed:2158672, ECO:0000269|PubMed:26680202,
CC ECO:0000269|PubMed:27580036}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12409298}.
CC -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. CACNG subfamily.
CC {ECO:0000305}.
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DR EMBL; M32231; AAA31181.1; -; mRNA.
DR EMBL; X56031; CAA39505.1; -; mRNA.
DR PIR; S10728; S10728.
DR RefSeq; NP_001075862.1; NM_001082393.1.
DR RefSeq; XP_008269323.1; XM_008271101.2.
DR PDB; 3JBR; EM; 4.20 A; E=1-222.
DR PDB; 5GJV; EM; 3.60 A; E=1-222.
DR PDB; 5GJW; EM; 3.90 A; E=1-222.
DR PDB; 6JP5; EM; 2.90 A; E=1-222.
DR PDB; 6JP8; EM; 2.70 A; E=1-222.
DR PDB; 6JPA; EM; 2.60 A; E=1-222.
DR PDB; 6JPB; EM; 2.90 A; E=1-222.
DR PDB; 7JPK; EM; 3.00 A; E=1-222.
DR PDB; 7JPL; EM; 3.40 A; E=1-222.
DR PDB; 7JPV; EM; 3.40 A; E=1-222.
DR PDB; 7JPW; EM; 3.20 A; E=1-222.
DR PDB; 7JPX; EM; 2.90 A; E=1-222.
DR PDBsum; 3JBR; -.
DR PDBsum; 5GJV; -.
DR PDBsum; 5GJW; -.
DR PDBsum; 6JP5; -.
DR PDBsum; 6JP8; -.
DR PDBsum; 6JPA; -.
DR PDBsum; 6JPB; -.
DR PDBsum; 7JPK; -.
DR PDBsum; 7JPL; -.
DR PDBsum; 7JPV; -.
DR PDBsum; 7JPW; -.
DR PDBsum; 7JPX; -.
DR AlphaFoldDB; P19518; -.
DR SMR; P19518; -.
DR ComplexPortal; CPX-3189; Skeletal muscle VGCC complex.
DR DIP; DIP-61881N; -.
DR IntAct; P19518; 2.
DR STRING; 9986.ENSOCUP00000007638; -.
DR Ensembl; ENSOCUT00000008846; ENSOCUP00000007638; ENSOCUG00000008850.
DR GeneID; 100009263; -.
DR KEGG; ocu:100009263; -.
DR CTD; 786; -.
DR eggNOG; ENOG502QT5N; Eukaryota.
DR GeneTree; ENSGT00390000007786; -.
DR HOGENOM; CLU_093876_0_0_1; -.
DR InParanoid; P19518; -.
DR OMA; WIEYYYG; -.
DR OrthoDB; 1261253at2759; -.
DR TreeFam; TF331651; -.
DR Proteomes; UP000001811; Chromosome 19.
DR Bgee; ENSOCUG00000008850; Expressed in skeletal muscle tissue and 7 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:1990454; C:L-type voltage-gated calcium channel complex; IDA:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
DR GO; GO:0030315; C:T-tubule; IDA:UniProtKB.
DR GO; GO:0005246; F:calcium channel regulator activity; IDA:UniProtKB.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IC:ComplexPortal.
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; IDA:UniProtKB.
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 3D-structure; Calcium; Calcium channel; Calcium transport; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..222
FT /note="Voltage-dependent calcium channel gamma-1 subunit"
FT /id="PRO_0000164671"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26680202,
FT ECO:0000269|PubMed:27580036"
FT TRANSMEM 11..29
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26680202,
FT ECO:0000269|PubMed:27580036"
FT TOPO_DOM 30..108
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:26680202,
FT ECO:0000269|PubMed:27580036"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26680202,
FT ECO:0000269|PubMed:27580036"
FT TOPO_DOM 130..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26680202,
FT ECO:0000269|PubMed:27580036"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26680202,
FT ECO:0000269|PubMed:27580036"
FT TOPO_DOM 156..179
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:26680202,
FT ECO:0000269|PubMed:27580036"
FT TRANSMEM 180..204
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26680202,
FT ECO:0000269|PubMed:27580036"
FT TOPO_DOM 205..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26680202,
FT ECO:0000269|PubMed:27580036"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..80
FT /evidence="ECO:0000269|PubMed:27580036,
FT ECO:0007744|PDB:5GJV, ECO:0007744|PDB:5GJW"
FT TURN 2..4
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 8..26
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:7JPX"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 105..127
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:7JPV"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:7JPK"
FT HELIX 137..164
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:7JPX"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:6JPB"
FT HELIX 182..201
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:7JPW"
SQ SEQUENCE 222 AA; 25058 MW; 903B6FD8DD78F698 CRC64;
MSPTEAPKVR VTLFCILVGI VLAMTAVVSD HWAVLSPHME NHNTTCEAAH FGLWRICTKR
IALGEDRSCG PITLPGEKNC SYFRHFNPGE SSEIFEFTTQ KEYSISAAAI SVFSLGFLIM
GTICALMAFR KKRDYLLRPA SMFYVFAGLC LFVSLEVMRQ SVKRMIDSED TVWIEYYYSW
SFACACAAFV LLFLGGISLL LFSLPRMPQN PWESCMDAEP EH
