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   03-AUG-2022, entry version 110.
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}.
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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; Q5E9F0; -.
DR   Ensembl; ENSBTAT00000001086; ENSBTAP00000001086; ENSBTAG00000000820.
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; ENSGT01050000244876; -.
DR   HOGENOM; CLU_168377_2_0_1; -.
DR   InParanoid; Q5E9F0; -.
DR   OMA; DCQRDDI; -.
DR   OrthoDB; 1573820at2759; -.
DR   TreeFam; TF319909; -.
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-416476; G alpha (q) signalling events.
DR   Reactome; R-BTA-418594; G alpha (i) signalling events.
DR   Reactome; R-BTA-418597; G alpha (z) signalling events.
DR   Reactome; R-BTA-428930; Thromboxane signalling through TP receptor.
DR   Reactome; R-BTA-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR   Reactome; R-BTA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   Proteomes; UP000009136; Chromosome 4.
DR   Bgee; ENSBTAG00000000820; Expressed in myometrium and 106 other 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; -; 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   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