GBG12_PONAB
ID GBG12_PONAB Reviewed; 72 AA.
AC Q5RBQ0;
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-12;
DE Flags: Precursor;
GN Name=GNG12;
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=Kidney;
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.
CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma.
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; CR858588; CAH90810.1; -; mRNA.
DR EMBL; CR859714; CAH91873.1; -; mRNA.
DR RefSeq; NP_001126086.1; NM_001132614.1.
DR RefSeq; XP_009247387.1; XM_009249112.1.
DR RefSeq; XP_009247391.1; XM_009249116.1.
DR RefSeq; XP_009247396.1; XM_009249121.1.
DR AlphaFoldDB; Q5RBQ0; -.
DR SMR; Q5RBQ0; -.
DR STRING; 9601.ENSPPYP00000001459; -.
DR GeneID; 100173039; -.
DR KEGG; pon:100173039; -.
DR CTD; 55970; -.
DR eggNOG; KOG4119; Eukaryota.
DR HOGENOM; CLU_168377_3_1_1; -.
DR InParanoid; Q5RBQ0; -.
DR OrthoDB; 1581168at2759; -.
DR TreeFam; TF319909; -.
DR Proteomes; UP000001595; Chromosome 1.
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; -; 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 Phosphoprotein; Prenylation; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q28024"
FT CHAIN 2..69
FT /note="Guanine nucleotide-binding protein G(I)/G(S)/G(O)
FT subunit gamma-12"
FT /id="PRO_0000042167"
FT PROPEP 70..72
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042168"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q28024"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DAS9"
FT MOD_RES 42
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9DAS9"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBI6"
FT MOD_RES 69
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 69
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 72 AA; 8006 MW; A4C489A61697FAA9 CRC64;
MSSKTASTNN IAQARRTVQQ LRLEASIERI KVSKASADLM SYCEEHARSD PLLIGIPTSE
NPFKDKKTCI IL