ID   GBG11_RAT               Reviewed;          73 AA.
AC   P61954; P50152; Q4V8M0;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-11;
DE   Flags: Precursor;
GN   Name=Gng11; Synonyms=Gngt11;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
RA   Costain W.J., Mishra R.K.;
RT   "Identification and cloning of rat G protein gamma 11 subunit.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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.
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; AF257110; AAF68984.1; -; mRNA.
DR   EMBL; BC097320; AAH97320.1; -; mRNA.
DR   RefSeq; NP_071791.1; NM_022396.2.
DR   RefSeq; XP_003749746.1; XM_003749698.3.
DR   AlphaFoldDB; P61954; -.
DR   SMR; P61954; -.
DR   STRING; 10116.ENSRNOP00000065818; -.
DR   PhosphoSitePlus; P61954; -.
DR   PaxDb; P61954; -.
DR   Ensembl; ENSRNOT00000074048; ENSRNOP00000065818; ENSRNOG00000050469.
DR   GeneID; 64199; -.
DR   KEGG; rno:64199; -.
DR   UCSC; RGD:621515; rat.
DR   CTD; 2791; -.
DR   RGD; 621515; Gng11.
DR   eggNOG; KOG4119; Eukaryota.
DR   GeneTree; ENSGT01050000244876; -.
DR   HOGENOM; CLU_168377_2_0_1; -.
DR   InParanoid; P61954; -.
DR   OMA; DCQRDDI; -.
DR   OrthoDB; 1573820at2759; -.
DR   PhylomeDB; P61954; -.
DR   TreeFam; TF319909; -.
DR   Reactome; R-RNO-1296041; Activation of G protein gated Potassium channels.
DR   Reactome; R-RNO-202040; G-protein activation.
DR   Reactome; R-RNO-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR   Reactome; R-RNO-392170; ADP signalling through P2Y purinoceptor 12.
DR   Reactome; R-RNO-392451; G beta:gamma signalling through PI3Kgamma.
DR   Reactome; R-RNO-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR   Reactome; R-RNO-4086398; Ca2+ pathway.
DR   Reactome; R-RNO-416476; G alpha (q) signalling events.
DR   Reactome; R-RNO-418594; G alpha (i) signalling events.
DR   Reactome; R-RNO-418597; G alpha (z) signalling events.
DR   Reactome; R-RNO-420092; Glucagon-type ligand receptors.
DR   Reactome; R-RNO-428930; Thromboxane signalling through TP receptor.
DR   Reactome; R-RNO-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR   Reactome; R-RNO-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR   Reactome; R-RNO-8964616; G beta:gamma signalling through CDC42.
DR   Reactome; R-RNO-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR   PRO; PR:P61954; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000047914; Expressed in heart and 19 other tissues.
DR   Genevisible; P61954; RN.
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_0000012663"
FT   PROPEP          71..73
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000012664"
FT   REGION          51..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..66
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         70
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000255"
FT   LIPID           70
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   73 AA;  8481 MW;  2B13935E3AEFB9E8 CRC64;
     MPALHIEDLP EKEKLKMEVE QLRKEVKLQR QQVSKCSEEI KNYIEERSGE DPLVKGIPED
     KNPFKEKGSC VIS