GNAO_MOUSE
ID GNAO_MOUSE Reviewed; 354 AA.
AC P18872; P18873;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Guanine nucleotide-binding protein G(o) subunit alpha;
GN Name=Gnao1; Synonyms=Gna0, Gnao;
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] (ISOFORMS ALPHA-1 AND ALPHA-2).
RC TISSUE=Brain, and Spermatid;
RX PubMed=1697681; DOI=10.1073/pnas.87.17.6477;
RA Strathmann M., Wilkie T.M., Simon M.I.;
RT "Alternative splicing produces transcripts encoding two forms of the alpha
RT subunit of GTP-binding protein Go.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:6477-6481(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
RN [3]
RP PROTEIN SEQUENCE OF 22-32; 36-46; 55-100; 106-143; 146-177; 182-193;
RP 199-206 AND 244-272, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP FUNCTION, AND INTERACTION WITH RGS14.
RX PubMed=10926822; DOI=10.1042/bj3500019;
RA Traver S., Bidot C., Spassky N., Baltauss T., De Tand M.F., Thomas J.L.,
RA Zalc B., Janoueix-Lerosey I., Gunzburg J.D.;
RT "RGS14 is a novel Rap effector that preferentially regulates the GTPase
RT activity of galphao.";
RL Biochem. J. 350:19-29(2000).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=15585744; DOI=10.1124/mol.104.003913;
RA Nakata H., Kozasa T.;
RT "Functional characterization of Galphao signaling through G protein-
RT regulated inducer of neurite outgrowth 1.";
RL Mol. Pharmacol. 67:695-702(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, 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 [7]
RP HISTAMINYLATION AT GLN-205.
RX PubMed=23022564; DOI=10.1016/j.febslet.2012.09.027;
RA Vowinckel J., Stahlberg S., Paulmann N., Bluemlein K., Grohmann M.,
RA Ralser M., Walther D.J.;
RT "Histaminylation of glutamine residues is a novel posttranslational
RT modification implicated in G-protein signaling.";
RL FEBS Lett. 586:3819-3824(2012).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. Stimulated by RGS14. The G(o) protein function is not clear.
CC {ECO:0000269|PubMed:10926822}.
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 RGS14. {ECO:0000269|PubMed:10926822}.
CC -!- INTERACTION:
CC P18872-1; P97428: Rgs16; NbExp=2; IntAct=EBI-1018790, EBI-643424;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15585744}.
CC Membrane {ECO:0000250|UniProtKB:P09471}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P09471}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Alpha-1;
CC IsoId=P18872-1; Sequence=Displayed;
CC Name=Alpha-2;
CC IsoId=P18872-2, P18873-1;
CC Sequence=VSP_031251;
CC -!- PTM: Histaminylated at Gln-205 residues by TGM2.
CC {ECO:0000269|PubMed:23022564}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC {ECO:0000305}.
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DR EMBL; M36777; AAA37645.1; -; mRNA.
DR EMBL; M36778; AAA74566.1; -; mRNA.
DR EMBL; BC051989; AAH51989.1; -; mRNA.
DR CCDS; CCDS22532.1; -. [P18872-1]
DR CCDS; CCDS85585.1; -. [P18872-2]
DR PIR; A36038; RGMSO1.
DR PIR; B36038; RGMSO2.
DR RefSeq; NP_001106855.1; NM_001113384.1. [P18872-2]
DR RefSeq; NP_034438.1; NM_010308.3. [P18872-1]
DR PDB; 3C7K; X-ray; 2.90 A; A/C=22-354.
DR PDBsum; 3C7K; -.
DR AlphaFoldDB; P18872; -.
DR SMR; P18872; -.
DR BioGRID; 199970; 44.
DR DIP; DIP-29921N; -.
DR IntAct; P18872; 12.
DR MINT; P18872; -.
DR STRING; 10090.ENSMUSP00000114144; -.
DR iPTMnet; P18872; -.
DR PhosphoSitePlus; P18872; -.
DR SwissPalm; P18872; -.
DR jPOST; P18872; -.
DR MaxQB; P18872; -.
DR PaxDb; P18872; -.
DR PeptideAtlas; P18872; -.
DR PRIDE; P18872; -.
DR ProteomicsDB; 271021; -. [P18872-1]
DR ProteomicsDB; 271022; -. [P18872-2]
DR Antibodypedia; 3649; 269 antibodies from 34 providers.
DR DNASU; 14681; -.
DR Ensembl; ENSMUST00000034198; ENSMUSP00000034198; ENSMUSG00000031748. [P18872-1]
DR Ensembl; ENSMUST00000125716; ENSMUSP00000114144; ENSMUSG00000031748. [P18872-1]
DR Ensembl; ENSMUST00000138659; ENSMUSP00000148550; ENSMUSG00000031748. [P18872-2]
DR GeneID; 14681; -.
DR KEGG; mmu:14681; -.
DR UCSC; uc009mvk.2; mouse. [P18872-2]
DR UCSC; uc009mvl.1; mouse. [P18872-1]
DR CTD; 2775; -.
DR MGI; MGI:95775; Gnao1.
DR VEuPathDB; HostDB:ENSMUSG00000031748; -.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000155883; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P18872; -.
DR OMA; YTGLNTY; -.
DR PhylomeDB; P18872; -.
DR TreeFam; TF300673; -.
DR Reactome; R-MMU-4086398; Ca2+ pathway.
DR BioGRID-ORCS; 14681; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Gnao1; mouse.
DR EvolutionaryTrace; P18872; -.
DR PRO; PR:P18872; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P18872; protein.
DR Bgee; ENSMUSG00000031748; Expressed in perirhinal cortex and 233 other tissues.
DR ExpressionAtlas; P18872; baseline and differential.
DR Genevisible; P18872; MM.
DR GO; GO:0044297; C:cell body; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0051430; F:corticotropin-releasing hormone receptor 1 binding; ISO:MGI.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0031821; F:G protein-coupled serotonin receptor binding; ISO:MGI.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IMP:MGI.
DR GO; GO:0032794; F:GTPase activating protein binding; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031852; F:mu-type opioid receptor binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007568; P:aging; ISO:MGI.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; IMP:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0051926; P:negative regulation of calcium ion transport; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0008016; P:regulation of heart contraction; IMP:MGI.
DR GO; GO:0010243; P:response to organonitrogen compound; ISO:MGI.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001408; Gprotein_alpha_I.
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; PR00441; GPROTEINAI.
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 3D-structure; Alternative splicing; Cell membrane;
KW Direct protein sequencing; GTP-binding; Lipoprotein; Magnesium; Membrane;
KW Metal-binding; Myristate; Nucleotide-binding; Palmitate;
KW Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P08239"
FT CHAIN 2..354
FT /note="Guanine nucleotide-binding protein G(o) subunit
FT alpha"
FT /id="PRO_0000203704"
FT DOMAIN 32..354
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 35..48
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 174..182
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 197..206
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 266..273
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 324..329
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 40..47
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 176..182
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 201..205
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 270..273
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 205
FT /note="5-glutamyl histamine"
FT /evidence="ECO:0000269|PubMed:23022564"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P09471"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 249..354
FT /note="MLFDSICNNKFFIDTSIILFLNKKDLFGEKIKKSPLTICFPEYPGSNTYEDA
FT AAYIQTQFESKNRSPNKEIYCHMTCATDTNNIQVVFDAVTDIIIANNLRGCGLY -> K
FT LFDSICNNKWFTDTSIILFLNKKDIFEEKIKKSPLTICFPEYTGPSAFTEAVAHIQGQY
FT ESKNKSAHKEVYSHVTCATDTNNIQFVFDAVTDVIIAKNLRGCGLY (in isoform
FT Alpha-2)"
FT /evidence="ECO:0000303|PubMed:1697681"
FT /id="VSP_031251"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:3C7K"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:3C7K"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:3C7K"
FT HELIX 63..91
FT /evidence="ECO:0007829|PDB:3C7K"
FT HELIX 100..113
FT /evidence="ECO:0007829|PDB:3C7K"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:3C7K"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:3C7K"
FT HELIX 135..141
FT /evidence="ECO:0007829|PDB:3C7K"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:3C7K"
FT HELIX 153..157
FT /evidence="ECO:0007829|PDB:3C7K"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:3C7K"
FT TURN 172..176
FT /evidence="ECO:0007829|PDB:3C7K"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:3C7K"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:3C7K"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:3C7K"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:3C7K"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:3C7K"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:3C7K"
FT HELIX 228..232
FT /evidence="ECO:0007829|PDB:3C7K"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:3C7K"
FT HELIX 243..255
FT /evidence="ECO:0007829|PDB:3C7K"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:3C7K"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:3C7K"
FT HELIX 272..279
FT /evidence="ECO:0007829|PDB:3C7K"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:3C7K"
FT HELIX 297..310
FT /evidence="ECO:0007829|PDB:3C7K"
FT HELIX 329..344
FT /evidence="ECO:0007829|PDB:3C7K"
SQ SEQUENCE 354 AA; 40085 MW; B73A84F3BDB09F2C CRC64;
MGCTLSAEER AALERSKAIE KNLKEDGISA AKDVKLLLLG AGESGKSTIV KQMKIIHEDG
FSGEDVKQYK PVVYSNTIQS LAAIVRAMDT LGVEYGDKER KTDSKMVCDV VSRMEDTEPF
SAELLSAMMR LWGDSGIQEC FNRSREYQLN DSAKYYLDSL DRIGAGDYQP TEQDILRTRV
KTTGIVETHF TFKNLHFRLF DVGGQRSERK KWIHCFEDVT AIIFCVALSG YDQVLHEDET
TNRMHESLML FDSICNNKFF IDTSIILFLN KKDLFGEKIK KSPLTICFPE YPGSNTYEDA
AAYIQTQFES KNRSPNKEIY CHMTCATDTN NIQVVFDAVT DIIIANNLRG CGLY
