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Database: UniProt
Entry: P18872
LinkDB: P18872
Original site: P18872 
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   07-APR-2021, entry version 203.
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   SMR; P18872; -.
DR   BioGRID; 199970; 44.
DR   DIP; DIP-29921N; -.
DR   IntAct; P18872; 13.
DR   MINT; P18872; -.
DR   STRING; 10090.ENSMUSP00000114144; -.
DR   iPTMnet; P18872; -.
DR   PhosphoSitePlus; P18872; -.
DR   SwissPalm; P18872; -.
DR   jPOST; P18872; -.
DR   PaxDb; P18872; -.
DR   PeptideAtlas; P18872; -.
DR   PRIDE; P18872; -.
DR   ProteomicsDB; 271021; -. [P18872-1]
DR   ProteomicsDB; 271022; -. [P18872-2]
DR   Antibodypedia; 3649; 255 antibodies.
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   eggNOG; KOG0082; Eukaryota.
DR   GeneTree; ENSGT00940000155883; -.
DR   HOGENOM; CLU_014184_6_0_1; -.
DR   InParanoid; P18872; -.
DR   OMA; TYIQSQY; -.
DR   PhylomeDB; P18872; -.
DR   TreeFam; TF300673; -.
DR   Reactome; R-MMU-112043; PLC beta mediated events.
DR   Reactome; R-MMU-202040; G-protein activation.
DR   Reactome; R-MMU-4086398; Ca2+ pathway.
DR   Reactome; R-MMU-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   BioGRID-ORCS; 14681; 1 hit in 52 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 CA1 field of hippocampus and 280 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:0032991; C:protein-containing complex; ISO:MGI.
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:0044877; F:protein-containing complex 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:0009987; P:cellular process; IMP:MGI.
DR   GO; GO:0007212; P:dopamine receptor signaling pathway; IMP:MGI.
DR   GO; GO:0030900; P:forebrain development; IEA:Ensembl.
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:0031175; P:neuron projection development; IEA:Ensembl.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
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:0034097; P:response to cytokine; IEA:Ensembl.
DR   GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR   GO; GO:0043278; P:response to morphine; IEA:Ensembl.
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   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   NP_BIND         40..47
FT                   /note="GTP"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         176..182
FT                   /note="GTP"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         201..205
FT                   /note="GTP"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         270..273
FT                   /note="GTP"
FT                   /evidence="ECO:0000250"
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   METAL           47
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   METAL           182
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   BINDING         326
FT                   /note="GTP; via amide nitrogen"
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:0007744|PDB:3C7K"
FT   TURN            46..49
FT                   /evidence="ECO:0007744|PDB:3C7K"
FT   HELIX           50..52
FT                   /evidence="ECO:0007744|PDB:3C7K"
FT   HELIX           63..91
FT                   /evidence="ECO:0007744|PDB:3C7K"
FT   HELIX           100..113
FT                   /evidence="ECO:0007744|PDB:3C7K"
FT   TURN            114..116
FT                   /evidence="ECO:0007744|PDB:3C7K"
FT   HELIX           122..131
FT                   /evidence="ECO:0007744|PDB:3C7K"
FT   HELIX           135..141
FT                   /evidence="ECO:0007744|PDB:3C7K"
FT   TURN            142..145
FT                   /evidence="ECO:0007744|PDB:3C7K"
FT   HELIX           153..157
FT                   /evidence="ECO:0007744|PDB:3C7K"
FT   HELIX           160..163
FT                   /evidence="ECO:0007744|PDB:3C7K"
FT   TURN            172..176
FT                   /evidence="ECO:0007744|PDB:3C7K"
FT   STRAND          186..188
FT                   /evidence="ECO:0007744|PDB:3C7K"
FT   STRAND          199..201
FT                   /evidence="ECO:0007744|PDB:3C7K"
FT   TURN            206..208
FT                   /evidence="ECO:0007744|PDB:3C7K"
FT   HELIX           209..212
FT                   /evidence="ECO:0007744|PDB:3C7K"
FT   HELIX           214..216
FT                   /evidence="ECO:0007744|PDB:3C7K"
FT   STRAND          220..225
FT                   /evidence="ECO:0007744|PDB:3C7K"
FT   HELIX           228..232
FT                   /evidence="ECO:0007744|PDB:3C7K"
FT   STRAND          239..242
FT                   /evidence="ECO:0007744|PDB:3C7K"
FT   HELIX           243..255
FT                   /evidence="ECO:0007744|PDB:3C7K"
FT   HELIX           258..260
FT                   /evidence="ECO:0007744|PDB:3C7K"
FT   STRAND          263..268
FT                   /evidence="ECO:0007744|PDB:3C7K"
FT   HELIX           272..279
FT                   /evidence="ECO:0007744|PDB:3C7K"
FT   HELIX           284..286
FT                   /evidence="ECO:0007744|PDB:3C7K"
FT   HELIX           297..310
FT                   /evidence="ECO:0007744|PDB:3C7K"
FT   HELIX           329..344
FT                   /evidence="ECO:0007744|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
//
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