ID   GNA11_MOUSE             Reviewed;         359 AA.
AC   P21278; Q61939;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   24-JAN-2024, entry version 199.
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; Synonyms=Gna-11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2123549; DOI=10.1073/pnas.87.23.9113;
RA   Strathmann M., Simon M.I.;
RT   "G protein diversity: a distinct class of alpha subunits is present in
RT   vertebrates and invertebrates.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:9113-9117(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   PubMed=8838318; DOI=10.1006/geno.1996.0059;
RA   Davignon I., Barnard M., Gavrilova O., Sweet K.K., Wilkie T.M.;
RT   "Gene structure of murine Gna11 and Gna15: tandemly duplicated Gq class G
RT   protein alpha subunit genes.";
RL   Genomics 31:359-366(1996).
RN   [3]
RP   PROTEIN SEQUENCE OF 21-27; 121-133; 159-166; 203-210; 312-338 AND 346-354,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 211-271.
RX   PubMed=2508088; DOI=10.1073/pnas.86.19.7407;
RA   Strathmann M., Wilkie T.M., Simon M.I.;
RT   "Diversity of the G-protein family: sequences from five additional alpha
RT   subunits in the mouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:7407-7409(1989).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=9687499; DOI=10.1093/emboj/17.15.4304;
RA   Offermanns S., Zhao L.P., Gohla A., Sarosi I., Simon M.I., Wilkie T.M.;
RT   "Embryonic cardiomyocyte hypoplasia and craniofacial defects in G alpha q/G
RT   alpha 11-mutant mice.";
RL   EMBO J. 17:4304-4312(1998).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC       as modulators or transducers in various transmembrane signaling systems
CC       (PubMed:9687499). Acts as an activator of phospholipase C
CC       (PubMed:9687499). Transduces FFAR4 signaling in response to long-chain
CC       fatty acids (LCFAs) (By similarity). Together with GNAQ, required for
CC       heart development (PubMed:9687499). {ECO:0000250|UniProtKB:P29992,
CC       ECO:0000269|PubMed:9687499}.
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   -!- DISRUPTION PHENOTYPE: No visible phenoptype (PubMed:9687499). Mice
CC       lacking Gnaq and Gna11 are embryonic lethal due to cardiomyocyte
CC       hypoplasia (PubMed:9687499). Mice lacking Gnaq and with one single
CC       intact copy of Gna11, as well as mice lacking Gna11 and with one single
CC       intact copy of Gnaq die shortly after birth; lethality is caused by
CC       heart malformations (PubMed:9687499). Newborns display craniofacial
CC       defects (PubMed:9687499). {ECO:0000269|PubMed:9687499}.
CC   -!- SIMILARITY: Belongs to the G-alpha family. G(q) subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M55411; AAA63305.1; -; mRNA.
DR   EMBL; U37413; AAB36839.1; -; Genomic_DNA.
DR   EMBL; U37411; AAB36839.1; JOINED; Genomic_DNA.
DR   EMBL; U37412; AAB36839.1; JOINED; Genomic_DNA.
DR   EMBL; M57617; AAA63301.1; -; mRNA.
DR   CCDS; CCDS24061.1; -.
DR   PIR; B33833; B33833.
DR   PIR; B38414; RGMS11.
DR   RefSeq; NP_034431.1; NM_010301.3.
DR   AlphaFoldDB; P21278; -.
DR   SMR; P21278; -.
DR   BioGRID; 199961; 17.
DR   DIP; DIP-603N; -.
DR   IntAct; P21278; 2.
DR   STRING; 10090.ENSMUSP00000043190; -.
DR   GlyGen; P21278; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P21278; -.
DR   PhosphoSitePlus; P21278; -.
DR   SwissPalm; P21278; -.
DR   EPD; P21278; -.
DR   jPOST; P21278; -.
DR   PaxDb; 10090-ENSMUSP00000043190; -.
DR   PeptideAtlas; P21278; -.
DR   ProteomicsDB; 271410; -.
DR   Pumba; P21278; -.
DR   Antibodypedia; 53288; 284 antibodies from 26 providers.
DR   DNASU; 14672; -.
DR   Ensembl; ENSMUST00000043604.6; ENSMUSP00000043190.6; ENSMUSG00000034781.6.
DR   GeneID; 14672; -.
DR   KEGG; mmu:14672; -.
DR   UCSC; uc007gil.1; mouse.
DR   AGR; MGI:95766; -.
DR   CTD; 2767; -.
DR   MGI; MGI:95766; Gna11.
DR   VEuPathDB; HostDB:ENSMUSG00000034781; -.
DR   eggNOG; KOG0085; Eukaryota.
DR   GeneTree; ENSGT00940000161033; -.
DR   HOGENOM; CLU_014184_6_0_1; -.
DR   InParanoid; P21278; -.
DR   OMA; FEHRYVN; -.
DR   OrthoDB; 2897309at2759; -.
DR   PhylomeDB; P21278; -.
DR   TreeFam; TF300673; -.
DR   Reactome; R-MMU-112043; PLC beta mediated events.
DR   Reactome; R-MMU-202040; G-protein activation.
DR   Reactome; R-MMU-399997; Acetylcholine regulates insulin secretion.
DR   Reactome; R-MMU-416476; G alpha (q) signalling events.
DR   Reactome; R-MMU-418592; ADP signalling through P2Y purinoceptor 1.
DR   Reactome; R-MMU-428930; Thromboxane signalling through TP receptor.
DR   Reactome; R-MMU-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR   Reactome; R-MMU-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR   Reactome; R-MMU-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   BioGRID-ORCS; 14672; 5 hits in 81 CRISPR screens.
DR   ChiTaRS; Gna11; mouse.
DR   PRO; PR:P21278; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; P21278; Protein.
DR   Bgee; ENSMUSG00000034781; Expressed in small intestine Peyer's patch and 265 other cell types or tissues.
DR   ExpressionAtlas; P21278; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; ISA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0047391; F:alkylglycerophosphoethanolamine phosphodiesterase activity; ISO:MGI.
DR   GO; GO:0030234; F:enzyme regulator activity; IMP:MGI.
DR   GO; GO:0003925; F:G protein activity; IMP:MGI.
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; ISA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0001508; P:action potential; IDA:MGI.
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; IMP:MGI.
DR   GO; GO:1904888; P:cranial skeletal system development; IGI:MGI.
DR   GO; GO:0048066; P:developmental pigmentation; IMP:MGI.
DR   GO; GO:0086100; P:endothelin receptor signaling pathway; IGI:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0099105; P:ion channel modulating, G protein-coupled receptor signaling pathway; IGI:MGI.
DR   GO; GO:1990806; P:ligand-gated ion channel signaling pathway; IMP:MGI.
DR   GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IGI:MGI.
DR   GO; GO:0007207; P:phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway; IGI:MGI.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IMP:MGI.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; IMP:MGI.
DR   GO; GO:0008217; P:regulation of blood pressure; IGI:MGI.
DR   GO; GO:0045634; P:regulation of melanocyte differentiation; IMP:MGI.
DR   GO; GO:0001501; P:skeletal system development; IMP:MGI.
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.
DR   Genevisible; P21278; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; Direct protein sequencing; GTP-binding;
KW   Lipoprotein; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW   Palmitate; Reference proteome; Transducer.
FT   CHAIN           1..359
FT                   /note="Guanine nucleotide-binding protein subunit alpha-11"
FT                   /id="PRO_0000203747"
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"
FT   CONFLICT        77
FT                   /note="K -> L (in Ref. 2; AAB36839)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   359 AA;  42024 MW;  A33D2D6C6C62F8D5 CRC64;
     MTLESMMACC LSDEVKESKR INAEIEKQLR RDKRDARREL KLLLLGTGES GKSTFIKQMR
     IIHGAGYSEE DKRGFTKLVY QNIFTAMQAM VRAMETLKIL YKYEQNKANA LLIREVDVEK
     VTTFEHQYVN AIKTLWSDPG VQECYDRRRE FQLSDSAKYY LTDVDRIATV GYLPTQQDVL
     RVRVPTTGII EYPFDLENII FRMVDVGGQR SERRKWIHCF ENVTSIMFLV ALSEYDQVLV
     ESDNENRMEE SKALFRTIIT YPWFQNSSVI LFLNKKDLLE DKILHSHLVD YFPEFDGPQR
     DAQAAREFIL KMFVDLNPDS DKIIYSHFTC ATDTENIRFV FAAVKDTILQ LNLKEYNLV
//