ID A0A091N5S0_APAVI Unreviewed; 73 AA.
AC A0A091N5S0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Guanine nucleotide-binding protein subunit gamma {ECO:0000256|RuleBase:RU004973};
DE Flags: Fragment;
GN ORFNames=N311_07744 {ECO:0000313|EMBL:KFP84342.1};
OS Apaloderma vittatum (Bar-tailed trogon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Trogoniformes; Trogonidae; Apaloderma.
OX NCBI_TaxID=57397 {ECO:0000313|EMBL:KFP84342.1, ECO:0000313|Proteomes:UP000054244};
RN [1] {ECO:0000313|EMBL:KFP84342.1, ECO:0000313|Proteomes:UP000054244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N311 {ECO:0000313|EMBL:KFP84342.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as a modulator or transducer in various transmembrane signaling
CC systems. The beta and gamma chains are required for the GTPase
CC activity, for replacement of GDP by GTP, and for G protein-effector
CC interaction. {ECO:0000256|RuleBase:RU004973}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma.
CC {ECO:0000256|RuleBase:RU004973}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU004973};
CC Lipid-anchor {ECO:0000256|RuleBase:RU004973}; Cytoplasmic side
CC {ECO:0000256|RuleBase:RU004973}.
CC -!- SIMILARITY: Belongs to the G protein gamma family.
CC {ECO:0000256|ARBA:ARBA00007431, ECO:0000256|RuleBase:RU004973}.
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DR EMBL; KL376626; KFP84342.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091N5S0; -.
DR Proteomes; UP000054244; Unassembled WGS sequence.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:InterPro.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IEA:InterPro.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR CDD; cd00068; GGL; 1.
DR Gene3D; 4.10.260.10; Transducin (heterotrimeric G protein), gamma chain; 1.
DR InterPro; IPR015898; G-protein_gamma-like_dom.
DR InterPro; IPR036284; GGL_sf.
DR InterPro; IPR001770; Gprotein-gamma.
DR PANTHER; PTHR13809:SF28; GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)_G(S)_G(O) SUBUNIT GAMMA-T2; 1.
DR PANTHER; PTHR13809; GUANINE NUCLEOTIDE-BINDING PROTEIN GAMMA SUBUNIT; 1.
DR Pfam; PF00631; G-gamma; 1.
DR PRINTS; PR00321; GPROTEING.
DR SMART; SM01224; G_gamma; 1.
DR SMART; SM00224; GGL; 1.
DR SUPFAM; SSF48670; Transducin (heterotrimeric G protein), gamma chain; 1.
DR PROSITE; PS50058; G_PROTEIN_GAMMA; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU004973}; Coiled coil {ECO:0000256|SAM:Coils};
KW Lipoprotein {ECO:0000256|RuleBase:RU004973};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004973};
KW Reference proteome {ECO:0000313|Proteomes:UP000054244};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU004973}.
FT DOMAIN 5..73
FT /note="G protein gamma"
FT /evidence="ECO:0000259|PROSITE:PS50058"
FT REGION 51..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 5..39
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 51..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP84342.1"
FT NON_TER 73
FT /evidence="ECO:0000313|EMBL:KFP84342.1"
SQ SEQUENCE 73 AA; 8288 MW; 6B306A57FA234986 CRC64;
LQATMAQDMT EKELLKMELD QLKKEVKNER QMVSKTGKEI KEYIESMAGE DPLLKGVPED
KNPFKEKGGC TIS
//
