ID A0A452HKH3_9SAUR Unreviewed; 186 AA.
AC A0A452HKH3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Voltage-dependent calcium channel gamma-7 subunit {ECO:0000256|RuleBase:RU363085};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000015400.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000015400.1}
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU363085}.
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DR AlphaFoldDB; A0A452HKH3; -.
DR STRING; 38772.ENSGAGP00000015400; -.
DR Ensembl; ENSGAGT00000017592.1; ENSGAGP00000015400.1; ENSGAGG00000011622.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
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; PF00822; PMP22_Claudin; 1.
DR PRINTS; PR01792; VDCCGAMMA.
DR PRINTS; PR01795; VDCCGAMMA7.
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:UP000291020};
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 12..28
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363085"
FT TRANSMEM 40..66
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363085"
FT TRANSMEM 86..112
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363085"
SQ SEQUENCE 186 AA; 21038 MW; 884978D11EA6E532 CRC64;
VGWGTGTVRT ATPFPMVSLF LVFTAFVISN IGHIRPQRTI LAFVSGIFFI LSGLSLVVGL
VLYISSINDE VMNRPSGSEQ YFHYRYGWSF AFAASSFLLK EGAGVMSVYL FTKRYAEEEM
YRPHPAFYRP RLSDCSDYSG QFLHPEVWHR GRSPSDISSD VSIQMTQNYP PAIKYPEHMH
ISTSPC
//