ID GBG11_BOVIN Reviewed; 73 AA.
AC Q5E9F0; Q3SZW7;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-11;
DE Flags: Precursor;
GN Name=GNG11;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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 Interacts with beta-1 and beta-3, but not with beta-2 (By similarity).
CC {ECO:0000250}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BT020970; AAX08987.1; -; mRNA.
DR EMBL; BC102674; AAI02675.1; -; mRNA.
DR RefSeq; NP_001019694.1; NM_001024523.1.
DR AlphaFoldDB; Q5E9F0; -.
DR SMR; Q5E9F0; -.
DR STRING; 9913.ENSBTAP00000001086; -.
DR PaxDb; 9913-ENSBTAP00000001086; -.
DR Ensembl; ENSBTAT00000001086.5; ENSBTAP00000001086.4; ENSBTAG00000000820.5.
DR GeneID; 511812; -.
DR KEGG; bta:511812; -.
DR CTD; 2791; -.
DR VEuPathDB; HostDB:ENSBTAG00000000820; -.
DR VGNC; VGNC:53646; GNG11.
DR eggNOG; KOG4119; Eukaryota.
DR GeneTree; ENSGT01100000263525; -.
DR HOGENOM; CLU_168377_2_0_1; -.
DR InParanoid; Q5E9F0; -.
DR OMA; MPAFHIE; -.
DR OrthoDB; 5344095at2759; -.
DR TreeFam; TF319909; -.
DR Reactome; R-BTA-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-BTA-202040; G-protein activation.
DR Reactome; R-BTA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-BTA-392170; ADP signalling through P2Y purinoceptor 12.
DR Reactome; R-BTA-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-BTA-392851; Prostacyclin signalling through prostacyclin receptor.
DR Reactome; R-BTA-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR Reactome; R-BTA-4086398; Ca2+ pathway.
DR Reactome; R-BTA-416476; G alpha (q) signalling events.
DR Reactome; R-BTA-416482; G alpha (12/13) signalling events.
DR Reactome; R-BTA-418217; G beta:gamma signalling through PLC beta.
DR Reactome; R-BTA-418555; G alpha (s) signalling events.
DR Reactome; R-BTA-418592; ADP signalling through P2Y purinoceptor 1.
DR Reactome; R-BTA-418594; G alpha (i) signalling events.
DR Reactome; R-BTA-418597; G alpha (z) signalling events.
DR Reactome; R-BTA-420092; Glucagon-type ligand receptors.
DR Reactome; R-BTA-428930; Thromboxane signalling through TP receptor.
DR Reactome; R-BTA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-BTA-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-BTA-500657; Presynaptic function of Kainate receptors.
DR Reactome; R-BTA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR Reactome; R-BTA-8964315; G beta:gamma signalling through BTK.
DR Reactome; R-BTA-8964616; G beta:gamma signalling through CDC42.
DR Reactome; R-BTA-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-BTA-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000000820; Expressed in myometrium and 106 other cell types or tissues.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
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:SF1; GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)_G(S)_G(O) SUBUNIT GAMMA-11; 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; Lipoprotein; Membrane; Methylation; Prenylation;
KW Reference proteome; Transducer.
FT CHAIN 1..70
FT /note="Guanine nucleotide-binding protein G(I)/G(S)/G(O)
FT subunit gamma-11"
FT /id="PRO_0000042175"
FT PROPEP 71..73
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042176"
FT REGION 54..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 70
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 73 AA; 8594 MW; 3F42C4CE3AEFB9E8 CRC64;
MPALHIEDLP EKEKLKMEVE QLRKEVKLQR QQVSKCSEEI KNYIEERSRE DPLVKGIPED
KNPFKEKGSC IIS
//
