ID   GNA11_RAT               Reviewed;         359 AA.
AC   Q9JID2;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-NOV-2023, entry version 146.
DE   RecName: Full=Guanine nucleotide-binding protein subunit alpha-11;
DE            Short=G alpha-11;
DE            Short=G-protein subunit alpha-11;
GN   Name=Gna11;
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   TISSUE=Brain;
RA   Strotmann R.;
RT   "Rattus norvegicus guanine nucleotide binding protein alpha 11 subunit
RT   (G11).";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC       as modulators or transducers in various transmembrane signaling
CC       systems. Acts as an activator of phospholipase C (By similarity).
CC       Transduces FFAR4 signaling in response to long-chain fatty acids
CC       (LCFAs) (By similarity). Together with GNAQ, required for heart
CC       development (By similarity). {ECO:0000250|UniProtKB:P21278,
CC       ECO:0000250|UniProtKB:P29992}.
CC   -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC       alpha chain contains the guanine nucleotide binding site. Interacts
CC       with RGS22. Interacts with NTSR1. {ECO:0000250|UniProtKB:P29992}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P29992};
CC       Lipid-anchor {ECO:0000250|UniProtKB:P29992}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P29992}.
CC   -!- SIMILARITY: Belongs to the G-alpha family. G(q) subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF239674; AAF81690.1; -; mRNA.
DR   RefSeq; NP_112295.1; NM_031033.1.
DR   AlphaFoldDB; Q9JID2; -.
DR   SMR; Q9JID2; -.
DR   BioGRID; 249562; 1.
DR   STRING; 10116.ENSRNOP00000007498; -.
DR   iPTMnet; Q9JID2; -.
DR   PhosphoSitePlus; Q9JID2; -.
DR   SwissPalm; Q9JID2; -.
DR   jPOST; Q9JID2; -.
DR   PaxDb; 10116-ENSRNOP00000007498; -.
DR   GeneID; 81662; -.
DR   KEGG; rno:81662; -.
DR   UCSC; RGD:619749; rat.
DR   AGR; RGD:619749; -.
DR   CTD; 2767; -.
DR   RGD; 619749; Gna11.
DR   eggNOG; KOG0085; Eukaryota.
DR   InParanoid; Q9JID2; -.
DR   OrthoDB; 2897309at2759; -.
DR   PhylomeDB; Q9JID2; -.
DR   Reactome; R-RNO-112043; PLC beta mediated events.
DR   Reactome; R-RNO-202040; G-protein activation.
DR   Reactome; R-RNO-399997; Acetylcholine regulates insulin secretion.
DR   Reactome; R-RNO-416476; G alpha (q) signalling events.
DR   Reactome; R-RNO-418592; ADP signalling through P2Y purinoceptor 1.
DR   Reactome; R-RNO-428930; Thromboxane signalling through TP receptor.
DR   Reactome; R-RNO-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR   Reactome; R-RNO-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR   PRO; PR:Q9JID2; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0047391; F:alkylglycerophosphoethanolamine phosphodiesterase activity; IDA:MGI.
DR   GO; GO:0030234; F:enzyme regulator activity; ISO:RGD.
DR   GO; GO:0003925; F:G protein activity; ISO:RGD.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR   GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0019001; F:guanyl nucleotide binding; TAS:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR   GO; GO:0001508; P:action potential; ISO:RGD.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0071467; P:cellular response to pH; ISO:RGD.
DR   GO; GO:1904888; P:cranial skeletal system development; ISO:RGD.
DR   GO; GO:0048066; P:developmental pigmentation; ISO:RGD.
DR   GO; GO:0086100; P:endothelin receptor signaling pathway; ISO:RGD.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR   GO; GO:0007507; P:heart development; ISO:RGD.
DR   GO; GO:0099105; P:ion channel modulating, G protein-coupled receptor signaling pathway; ISO:RGD.
DR   GO; GO:1990806; P:ligand-gated ion channel signaling pathway; ISO:RGD.
DR   GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; ISO:RGD.
DR   GO; GO:0007207; P:phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway; ISO:RGD.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISO:RGD.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; ISO:RGD.
DR   GO; GO:0008217; P:regulation of blood pressure; ISO:RGD.
DR   GO; GO:0045634; P:regulation of melanocyte differentiation; ISO:RGD.
DR   GO; GO:0001501; P:skeletal system development; ISO:RGD.
DR   CDD; cd00066; G-alpha; 1.
DR   Gene3D; 1.10.400.10; GI Alpha 1, domain 2-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR000654; Gprotein_alpha_Q.
DR   InterPro; IPR001019; Gprotein_alpha_su.
DR   InterPro; IPR011025; GproteinA_insert.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10218; GTP-BINDING PROTEIN ALPHA SUBUNIT; 1.
DR   PANTHER; PTHR10218:SF328; GUANINE NUCLEOTIDE-BINDING PROTEIN SUBUNIT ALPHA-11; 1.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR00442; GPROTEINAQ.
DR   SMART; SM00275; G_alpha; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF47895; Transducin (alpha subunit), insertion domain; 1.
DR   PROSITE; PS51882; G_ALPHA; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasm; GTP-binding; Lipoprotein; Magnesium; Membrane;
KW   Metal-binding; Nucleotide-binding; Palmitate; Reference proteome;
KW   Transducer.
FT   CHAIN           1..359
FT                   /note="Guanine nucleotide-binding protein subunit alpha-11"
FT                   /id="PRO_0000203748"
FT   DOMAIN          38..359
FT                   /note="G-alpha"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          41..54
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          178..186
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          201..210
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          270..277
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          329..334
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   BINDING         46..53
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P29992"
FT   BINDING         53
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P27600"
FT   BINDING         180..183
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P27600"
FT   BINDING         186
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P27600"
FT   BINDING         274..277
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P27600"
FT   BINDING         331
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P27600"
FT   LIPID           9
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P29992"
FT   LIPID           10
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P29992"
SQ   SEQUENCE   359 AA;  42026 MW;  B4CD057E9FC7092A CRC64;
     MTLESMIACC LSDEVKESKR INAEIEKQLR RDKRDARREL KLLLLGTGES GKSTFIKQMR
     IIHGAGYSEE DKRGFTKLVY QNIFTAMQAV VRAMDTLKIR YKYEQNKANA LLIREVDVEK
     VTTFEHQYVN AIKTLWSDPG VQECYDRRRE FQLSDSAKYY LTDVDRIATV GYLPTQQDVL
     RVRVPTTGII EYPFDLENII FRMVDVGGQR SERRKWIHCF ENVTSIMFLV ALSEYDQVLV
     ESDNENRMEE SKALFRTIIT YPWFQHSSVI LFLNKKDLLE DKILHSHLVD YFPEFDGPQR
     DAQAAREFIL KMFVDLNPDS DKIIYSHFTC ATDTENIRFV FAAVKDTILQ LNLKEYNLV
//