ID A0A3P8SLQ2_AMPPE Unreviewed; 339 AA.
AC A0A3P8SLQ2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Voltage-dependent calcium channel gamma-7 subunit {ECO:0000256|RuleBase:RU363085};
GN Name=CACNG7 {ECO:0000313|Ensembl:ENSAPEP00000013009.1};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000013009.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000013009.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000013009.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Regulates the activity of L-type calcium channels that
CC contain CACNA1C as pore-forming subunit (By similarity). Regulates the
CC trafficking and gating properties of AMPA-selective glutamate receptors
CC (AMPARs). Promotes their targeting to the cell membrane and synapses
CC and modulates their gating properties by slowing their rates of
CC activation, deactivation and desensitization and by mediating their
CC resensitization. Shows specificity only for GRIA1 and GRIA2.
CC {ECO:0000256|RuleBase:RU363085}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU363085}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU363085}.
CC -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. CACNG subfamily.
CC {ECO:0000256|ARBA:ARBA00007111, ECO:0000256|RuleBase:RU363085}.
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 AlphaFoldDB; A0A3P8SLQ2; -.
DR STRING; 161767.ENSAPEP00000013009; -.
DR Ensembl; ENSAPET00000013357.1; ENSAPEP00000013009.1; ENSAPEG00000009253.1.
DR GeneTree; ENSGT01050000244961; -.
DR OMA; QRTLFIY; -.
DR Proteomes; UP000265080; Chromosome 7.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005262; F:calcium channel activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.140.150; -; 1.
DR InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR InterPro; IPR008371; VDCC_g7su.
DR InterPro; IPR008368; VDCC_gsu.
DR PANTHER; PTHR12107; VOLTAGE-DEPENDENT CALCIUM CHANNEL GAMMA SUBUNIT; 1.
DR PANTHER; PTHR12107:SF12; VOLTAGE-DEPENDENT CALCIUM CHANNEL GAMMA-7 SUBUNIT; 1.
DR Pfam; PF13903; Claudin_2; 1.
DR PRINTS; PR01792; VDCCGAMMA.
DR PRINTS; PR01795; VDCCGAMMA7.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|RuleBase:RU363085};
KW Calcium channel {ECO:0000256|RuleBase:RU363085};
KW Calcium transport {ECO:0000256|RuleBase:RU363085};
KW Ion channel {ECO:0000256|RuleBase:RU363085};
KW Ion transport {ECO:0000256|RuleBase:RU363085};
KW Membrane {ECO:0000256|RuleBase:RU363085};
KW Reference proteome {ECO:0000313|Proteomes:UP000265080};
KW Transmembrane {ECO:0000256|RuleBase:RU363085};
KW Transmembrane helix {ECO:0000256|RuleBase:RU363085};
KW Transport {ECO:0000256|RuleBase:RU363085};
KW Voltage-gated channel {ECO:0000256|RuleBase:RU363085}.
FT TRANSMEM 15..37
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363085"
FT TRANSMEM 98..115
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363085"
FT TRANSMEM 127..153
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363085"
FT TRANSMEM 173..199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363085"
FT REGION 226..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..327
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 339 AA; 37400 MW; F4541D21E73E7234 CRC64;
MSSCSSRALT ILSTVFGACG LLLVGVAVST DYWLIMVEGV ILQQNQSMEV KMALHSGLWR
VCFVAGTGQR TLFIYLLMEE TRITTENTAN ILKMVSDATP FPMVSLLFVF TAFVIGNIGH
IRPQRTILAF VSGIFFILSG LSLVVGLVLY ISSINDEVMN RPREPEQFFN YHYGWSFAFA
ASSFLLKEGA GVMSVYLFMK RYAEEEMYRP HPALYRPRLS ESSDYSGQFL HPESSWPPPK
RPRSSSSVSS DVSIQLTQTP PPKPSLQPLQ TSPPSASSST SYQAGYPPST HTLPRAPHPQ
GPHPQGPNPQ GQALPLTRPP SPTPPPHYHT HMHMSASPC
//
