GNA11_MOUSE
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 03-AUG-2022, entry version 191.
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, Pancreas,
RC 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}.
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; 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 iPTMnet; P21278; -.
DR PhosphoSitePlus; P21278; -.
DR SwissPalm; P21278; -.
DR EPD; P21278; -.
DR jPOST; P21278; -.
DR PaxDb; P21278; -.
DR PeptideAtlas; P21278; -.
DR PRIDE; P21278; -.
DR ProteomicsDB; 271410; -.
DR Antibodypedia; 53288; 268 antibodies from 26 providers.
DR DNASU; 14672; -.
DR Ensembl; ENSMUST00000043604; ENSMUSP00000043190; ENSMUSG00000034781.
DR GeneID; 14672; -.
DR KEGG; mmu:14672; -.
DR UCSC; uc007gil.1; mouse.
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; AHYICAT; -.
DR OrthoDB; 754573at2759; -.
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 76 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 262 other tissues.
DR ExpressionAtlas; P21278; baseline and differential.
DR Genevisible; P21278; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; ISA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0047391; F:alkylglycerophosphoethanolamine phosphodiesterase activity; ISO: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:0010259; P:multicellular organism aging; IMP:MGI.
DR GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IGI: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; -; 1.
DR Gene3D; 3.40.50.300; -; 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; PTHR10218; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00442; GPROTEINAQ.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
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
