GNAO_RAT
ID GNAO_RAT Reviewed; 354 AA.
AC P59215; P04900; P30033;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Guanine nucleotide-binding protein G(o) subunit alpha;
GN Name=Gnao1; Synonyms=Gna0, Gnao;
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] (ISOFORM ALPHA-1).
RX PubMed=2820999; DOI=10.1016/s0021-9258(18)47929-x;
RA Jones D.T., Reed R.R.;
RT "Molecular cloning of five GTP-binding protein cDNA species from rat
RT olfactory neuroepithelium.";
RL J. Biol. Chem. 262:14241-14249(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-2).
RX PubMed=1901650; DOI=10.1073/pnas.88.8.2974;
RA Tsukamoto T., Toyama R., Itoh H., Kozasa T., Matsuoka M., Kaziro Y.;
RT "Structure of the human gene and two rat cDNAs encoding the alpha chain of
RT GTP-binding regulatory protein Go: two different mRNAs are generated by
RT alternative splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:2974-2978(1991).
RN [3]
RP PROTEIN SEQUENCE OF 22-32; 36-46; 68-86; 87-100; 114-130; 163-177; 182-193;
RP 199-206 AND 244-272, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 45-354 (ISOFORM ALPHA-1).
RX PubMed=3086867; DOI=10.1073/pnas.83.11.3776;
RA Itoh H., Kozasa T., Nagata S., Nakamura S., Katada T., Ui M., Iwai S.,
RA Ohtsuka E., Kawasaki H., Suzuki K., Kaziro Y.;
RT "Molecular cloning and sequence determination of cDNAs for alpha subunits
RT of the guanine nucleotide-binding proteins Gs, Gi, and Go from rat brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:3776-3780(1986).
RN [5]
RP PROTEIN SEQUENCE OF 55-67; 114-129 AND 163-176.
RX PubMed=2158629; DOI=10.1038/344836a0;
RA Strittmatter S.M., Valenzuela D., Kennedy T.E., Neer E.J., Fishman M.C.;
RT "G0 is a major growth cone protein subject to regulation by GAP-43.";
RL Nature 344:836-841(1990).
RN [6]
RP MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-3, AND LACK OF
RP PALMITOYLATION AT CYS-351.
RX PubMed=8484716; DOI=10.1042/bj2910349;
RA Parenti M., Vigano M.A., Newman C.M.H., Milligan G., Magee A.I.;
RT "A novel N-terminal motif for palmitoylation of G-protein alpha subunits.";
RL Biochem. J. 291:349-353(1993).
RN [7]
RP DEAMIDATION AT ASN-346.
RX PubMed=9990023; DOI=10.1073/pnas.96.4.1327;
RA Exner T., Jensen O.N., Mann M., Kleuss C., Nurnberg B.;
RT "Posttranslational modification of Galphao1 generates Galphao3, an abundant
RT G protein in brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:1327-1332(1999).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. The G(o) protein function is not clear. Stimulated by RGS14
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RGS14 (By similarity). G proteins are composed
CC of 3 units; alpha, beta and gamma. The alpha chain contains the guanine
CC nucleotide binding site. {ECO:0000250|UniProtKB:P18872}.
CC -!- INTERACTION:
CC P59215; P17612: PRKACA; Xeno; NbExp=4; IntAct=EBI-8071125, EBI-476586;
CC P59215; Q9NS28: RGS18; Xeno; NbExp=2; IntAct=EBI-8071125, EBI-15933052;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P18872}.
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=P59215-1; Sequence=Displayed;
CC Name=Alpha-2;
CC IsoId=P59215-2, P30033-1;
CC Sequence=VSP_031252;
CC -!- PTM: Deamidation of Asn-346 converts alpha-1 to alpha-3.
CC {ECO:0000269|PubMed:9990023}.
CC -!- PTM: Histaminylated at Gln-205 residues by TGM2.
CC {ECO:0000250|UniProtKB:P18872}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC {ECO:0000305}.
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DR EMBL; M17526; AAA40826.1; -; mRNA.
DR EMBL; M12671; AAA41262.1; -; mRNA.
DR PIR; C40436; RGRTO1.
DR PIR; D40436; RGRTO2.
DR RefSeq; NP_059023.1; NM_017327.1. [P59215-1]
DR AlphaFoldDB; P59215; -.
DR SMR; P59215; -.
DR BioGRID; 248412; 7.
DR CORUM; P59215; -.
DR DIP; DIP-59090N; -.
DR IntAct; P59215; 22.
DR MINT; P59215; -.
DR STRING; 10116.ENSRNOP00000026373; -.
DR BindingDB; P59215; -.
DR ChEMBL; CHEMBL4295785; -.
DR iPTMnet; P59215; -.
DR PhosphoSitePlus; P59215; -.
DR SwissPalm; P59215; -.
DR jPOST; P59215; -.
DR PaxDb; P59215; -.
DR PRIDE; P59215; -.
DR Ensembl; ENSRNOT00000026373; ENSRNOP00000026373; ENSRNOG00000019482. [P59215-1]
DR GeneID; 50664; -.
DR KEGG; rno:50664; -.
DR UCSC; RGD:628732; rat. [P59215-1]
DR CTD; 2775; -.
DR RGD; 628732; Gnao1.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000155883; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P59215; -.
DR OMA; QVIWADA; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; P59215; -.
DR TreeFam; TF300673; -.
DR Reactome; R-RNO-4086398; Ca2+ pathway.
DR SABIO-RK; P59215; -.
DR PRO; PR:P59215; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000019482; Expressed in frontal cortex and 17 other tissues.
DR Genevisible; P59215; RN.
DR GO; GO:0044297; C:cell body; ISO:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0051430; F:corticotropin-releasing hormone receptor 1 binding; IPI:RGD.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0031821; F:G protein-coupled serotonin receptor binding; IPI:RGD.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0019003; F:GDP binding; TAS:RGD.
DR GO; GO:0005525; F:GTP binding; IDA:RGD.
DR GO; GO:0032794; F:GTPase activating protein binding; IPI:RGD.
DR GO; GO:0003924; F:GTPase activity; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031852; F:mu-type opioid receptor binding; IPI:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007568; P:aging; IDA:RGD.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; ISO:RGD.
DR GO; GO:0030900; P:forebrain development; IEP:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0051926; P:negative regulation of calcium ion transport; IMP:RGD.
DR GO; GO:0031175; P:neuron projection development; IEP:RGD.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEP:RGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:RGD.
DR GO; GO:0008016; P:regulation of heart contraction; ISO:RGD.
DR GO; GO:0034097; P:response to cytokine; IEP:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0043278; P:response to morphine; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IDA:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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 Alternative splicing; Cell membrane; Direct protein sequencing;
KW GTP-binding; Lipoprotein; Magnesium; Membrane; Metal-binding; Myristate;
KW Nucleotide-binding; Palmitate; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8484716"
FT CHAIN 2..354
FT /note="Guanine nucleotide-binding protein G(o) subunit
FT alpha"
FT /id="PRO_0000203706"
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 SITE 351
FT /note="Not S-palmitoylated"
FT /evidence="ECO:0000269|PubMed:8484716"
FT MOD_RES 205
FT /note="5-glutamyl histamine"
FT /evidence="ECO:0000250|UniProtKB:P18872"
FT MOD_RES 346
FT /note="Deamidated asparagine; in form Alpha-3"
FT /evidence="ECO:0000269|PubMed:9990023"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:8484716"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:8484716"
FT VAR_SEQ 247..354
FT /note="SLMLFDSICNNKFFIDTSIILFLNKKDLFGEKIKKSPLTICFPEYPGSNTYE
FT DAAAYIQTQFESKNRSPNKEIYCHMTCATDTNNIQVVFDAVTDIIIANNLRGCGLY ->
FT FLKLFDSICNNKWFTDTSIILFLNKKDIFEEKIKKSPLTICFPEYTGPSAFTEAVAHIQ
FT GQYESKNKSAHKEVYSHVTCATDTNNIQFVFDAVTDVIIAKNLRGCGLY (in
FT isoform Alpha-2)"
FT /evidence="ECO:0000303|PubMed:1901650"
FT /id="VSP_031252"
SQ SEQUENCE 354 AA; 40069 MW; 577024F61B179C89 CRC64;
MGCTLSAEER AALERSKAIE KNLKEDGISA AKDVKLLLLG AGESGKSTIV KQMKIIHEDG
FSGEDVKQYK PVVYSNTIQS LAAIVRAMDT LGVEYGDKER KADSKMVCDV VSRMEDTEPF
SAELLSAMMR LWGDSGIQEC FNRSREYQLN DSAKYYLDSL DRIGAADYQP TEQDILRTRV
KTTGIVETHF TFKNLHFRLF DVGGQRSERK KWIHCFEDVT AIIFCVALSG YDQVLHEDET
TNRMHESLML FDSICNNKFF IDTSIILFLN KKDLFGEKIK KSPLTICFPE YPGSNTYEDA
AAYIQTQFES KNRSPNKEIY CHMTCATDTN NIQVVFDAVT DIIIANNLRG CGLY
