GBG2_PONAB
ID GBG2_PONAB Reviewed; 71 AA.
AC Q5R7U4; Q5RAI5;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2;
DE Flags: Precursor;
GN Name=GNG2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma (By
CC similarity). In this context, interacts with GNB2 (By similarity). The
CC heterodimer formed by GNB1 and GNG2 interacts with ARHGEF5 (By
CC similarity). The heterodimer formed by GNB1 and GNG2 interacts with
CC GRK2 (By similarity). {ECO:0000250|UniProtKB:P59768,
CC ECO:0000250|UniProtKB:P63212}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the G protein gamma family. {ECO:0000305}.
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DR EMBL; CR859030; CAH91225.1; -; mRNA.
DR EMBL; CR860015; CAH92166.1; -; mRNA.
DR RefSeq; NP_001125723.1; NM_001132251.1.
DR RefSeq; XP_009247325.1; XM_009249050.1.
DR AlphaFoldDB; Q5R7U4; -.
DR SMR; Q5R7U4; -.
DR STRING; 9601.ENSPPYP00000006605; -.
DR PRIDE; Q5R7U4; -.
DR Ensembl; ENSPPYT00000006867; ENSPPYP00000006605; ENSPPYG00000005812.
DR GeneID; 100172647; -.
DR KEGG; pon:100172647; -.
DR CTD; 54331; -.
DR eggNOG; KOG4119; Eukaryota.
DR GeneTree; ENSGT01050000244876; -.
DR HOGENOM; CLU_168377_0_1_1; -.
DR InParanoid; Q5R7U4; -.
DR OMA; GKQQPPM; -.
DR OrthoDB; 1581168at2759; -.
DR TreeFam; TF319909; -.
DR Proteomes; UP000001595; Chromosome 14.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:InterPro.
DR GO; GO:0031681; F:G-protein beta-subunit binding; ISS:CAFA.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR CDD; cd00068; GGL; 1.
DR Gene3D; 4.10.260.10; -; 1.
DR InterPro; IPR015898; G-protein_gamma-like_dom.
DR InterPro; IPR036284; GGL_sf.
DR InterPro; IPR001770; Gprotein-gamma.
DR PANTHER; PTHR13809; PTHR13809; 1.
DR Pfam; PF00631; G-gamma; 1.
DR PRINTS; PR00321; GPROTEING.
DR SMART; SM00224; GGL; 1.
DR SUPFAM; SSF48670; SSF48670; 1.
DR PROSITE; PS50058; G_PROTEIN_GAMMA; 1.
PE 3: Inferred from homology;
KW Acetylation; Cell membrane; Lipoprotein; Membrane; Methylation;
KW Prenylation; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P63212"
FT CHAIN 2..68
FT /note="Guanine nucleotide-binding protein G(I)/G(S)/G(O)
FT subunit gamma-2"
FT /id="PRO_0000042169"
FT PROPEP 69..71
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042170"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P63212"
FT MOD_RES 68
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 68
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 46
FT /note="K -> E (in Ref. 1; CAH91225)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 71 AA; 7850 MW; EDB74E4135E7A37A CRC64;
MASNNTASIA QARKLVEQLK MEANIDRIKV SKAAADLMAY CEAHAKEDPL LTPVPASENP
FREKKFFCAI L