ID A0A087QLL4_APTFO Unreviewed; 315 AA.
AC A0A087QLL4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Voltage-dependent calcium channel gamma-2 subunit {ECO:0000256|RuleBase:RU363085};
DE Flags: Fragment;
GN ORFNames=AS27_07826 {ECO:0000313|EMBL:KFM02118.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM02118.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM02118.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM02118.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulates the trafficking and gating properties of AMPA-
CC selective glutamate receptors (AMPARs). Promotes their targeting to the
CC cell membrane and synapses and modulates their gating properties by
CC slowing their rates of activation, deactivation and desensitization.
CC Does not show subunit-specific AMPA receptor regulation and regulates
CC all AMPAR subunits. Thought to stabilize the calcium channel in an
CC inactivated (closed) state. {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}.
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DR EMBL; KL225739; KFM02118.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087QLL4; -.
DR STRING; 9233.A0A087QLL4; -.
DR Proteomes; UP000053286; Unassembled WGS sequence.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR Gene3D; 1.20.140.150; -; 1.
DR InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR InterPro; IPR005422; VDCC_g2su.
DR InterPro; IPR008368; VDCC_gsu.
DR PANTHER; PTHR12107; VOLTAGE-DEPENDENT CALCIUM CHANNEL GAMMA SUBUNIT; 1.
DR PANTHER; PTHR12107:SF1; VOLTAGE-DEPENDENT CALCIUM CHANNEL GAMMA-2 SUBUNIT; 1.
DR Pfam; PF00822; PMP22_Claudin; 1.
DR PRINTS; PR01792; VDCCGAMMA.
DR PRINTS; PR01602; VDCCGAMMA2.
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:UP000053286};
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..35
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363085"
FT TRANSMEM 106..128
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363085"
FT TRANSMEM 135..158
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363085"
FT TRANSMEM 178..202
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363085"
FT REGION 233..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 315
FT /evidence="ECO:0000313|EMBL:KFM02118.1"
SQ SEQUENCE 315 AA; 35159 MW; 2D1F91CA6AD5890F CRC64;
MGLFDRGVQM LLTTVGAFAA FSLMTIAVGT DYWLYSRGVC KTKTVSENET SKKNEEVMTH
SGLWRTCCLE GNFKGLCKQI DHFPEDADYE ADTAEYFLRA VRASSIFPIL SVILLFMGGL
CIAASEFYKT RHNIILSAGI FFVSAGLSNI IGIIVYISAN AGDPSKSDSK KNSYSYGWSF
YFGALSFIIA EMVGVLAVHM FIDRHKQLRA NARATDYLQS SAITRIPSYR YRYQRRSRSS
SRSTEPSHSR DASPVGIKGF NTLPSTEISM YTLTREALKA TTTPTATYNS DRDNSFLQVH
NCIQKENKDS IHTNT
//
