GNAO_BOVIN
ID GNAO_BOVIN Reviewed; 354 AA.
AC P08239; A5PJS0;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 4.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Guanine nucleotide-binding protein G(o) subunit alpha;
DE AltName: Full=GTP-binding protein G39;
GN Name=GNAO1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3106961; DOI=10.1073/pnas.84.10.3107;
RA van Meurs K.P., Angus C.W., Lavu S., Kung H.-F., Czarnecki S.K., Moss J.,
RA Vaughan M.;
RT "Deduced amino acid sequence of bovine retinal Go alpha: similarities to
RT other guanine nucleotide-binding proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:3107-3111(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Cerebellum;
RA Ovchinnikov Y.A., Slepak V.Z., Pronin A.N., Shlenskii A.B., Levina N.B.,
RA Voeikov V.L., Bystrov N.S., Severtsova I.V., Lipkin V.M.;
RT "G39, GTP-binding protein from bovine cerebellum. Amino acid sequence and
RT nucleotide sequence of the corresponding cDNA.";
RL Dokl. Biochem. 297:404-406(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Cerebellum;
RX PubMed=3121394; DOI=10.1016/0014-5793(87)80557-4;
RA Ovchinnikov Y.A., Slepak V.Z., Pronin A.N., Shlensky A.B., Levina N.B.,
RA Voeikov V.L., Lipkin V.M.;
RT "Primary structure of bovine cerebellum GTP-binding protein G39 and its
RT effect on the adenylate cyclase system.";
RL FEBS Lett. 226:91-95(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 146-206.
RX PubMed=3090546; DOI=10.1073/pnas.83.16.5813;
RA Angus C.W., van Meurs K.P., Tsai S.-C., Adamik R., Miedel M.C.,
RA Pan Y.-C.E., Kung H.-F., Moss J., Vaughan M.;
RT "Identification of the probable site of choleragen-catalyzed ADP-
RT ribosylation in a Go alpha-like protein based on cDNA sequence.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:5813-5816(1986).
RN [6]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=3113429; DOI=10.1016/0006-291x(87)90780-7;
RA Schultz A.M., Tsai S.C., Kung H.F., Oroszlan S., Moss J., Vaughan M.;
RT "Hydroxylamine-stable covalent linkage of myristic acid in G0 alpha, a
RT guanine nucleotide-binding protein of bovine brain.";
RL Biochem. Biophys. Res. Commun. 146:1234-1239(1987).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P18872}.
CC Membrane {ECO:0000250|UniProtKB:P09471}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P09471}.
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; M16116; AAA30530.1; -; mRNA.
DR EMBL; X12924; CAA31391.1; -; mRNA.
DR EMBL; BC142217; AAI42218.1; -; mRNA.
DR EMBL; M14489; AAA30551.1; -; mRNA.
DR PIR; S00213; RGBOO1.
DR RefSeq; NP_776750.1; NM_174325.1.
DR AlphaFoldDB; P08239; -.
DR SMR; P08239; -.
DR BioGRID; 159106; 1.
DR STRING; 9913.ENSBTAP00000033570; -.
DR iPTMnet; P08239; -.
DR SwissPalm; P08239; -.
DR PaxDb; P08239; -.
DR PRIDE; P08239; -.
DR Ensembl; ENSBTAT00000033660; ENSBTAP00000033570; ENSBTAG00000003794.
DR GeneID; 281792; -.
DR KEGG; bta:281792; -.
DR CTD; 2775; -.
DR VEuPathDB; HostDB:ENSBTAG00000003794; -.
DR VGNC; VGNC:57047; GNAO1.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000155883; -.
DR HOGENOM; CLU_014184_7_0_1; -.
DR InParanoid; P08239; -.
DR OMA; QVIWADA; -.
DR OrthoDB; 754573at2759; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000003794; Expressed in prefrontal cortex and 102 other tissues.
DR ExpressionAtlas; P08239; baseline and differential.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0051430; F:corticotropin-releasing hormone receptor 1 binding; IBA:GO_Central.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0031821; F:G protein-coupled serotonin 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; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031852; F:mu-type opioid receptor binding; IBA:GO_Central.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; IBA:GO_Central.
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 Cell membrane; Direct protein sequencing; GTP-binding; Lipoprotein;
KW Magnesium; Membrane; Metal-binding; Myristate; Nucleotide-binding;
KW Palmitate; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3113429"
FT CHAIN 2..354
FT /note="Guanine nucleotide-binding protein G(o) subunit
FT alpha"
FT /id="PRO_0000203699"
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:0000250|UniProtKB:P18872"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:3113429"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 253
FT /note="S -> F (in Ref. 2; CAA31391)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="T -> I (in Ref. 1; AAA30530)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 40067 MW; 052FB75F456A89A3 CRC64;
MGCTLSAEER AALERSKAIE KNLKEDGISA AKDVKLLLLG AGESGKSTIV KQMKIIHEDG
FSGEDVKQYK PVVYSNTIQS LAAIVRAMDT LGIEYGDKER KADAKMVCDV VSRMEDTEPF
SPELLSAMMR LWGDSGIQEC FNRSREYQLN DSAKYYLDSL DRIGAADYQP TEQDILRTRV
KTTGIVETHF TFKNLHFRLF DVGGQRSERK KWIHCFEDVT AIIFCVALSG YDQVLHEDET
TNRMHESLML FDSICNNKFF IDTSIILFLN KKDLFGEKIK KSPLTICFPE YTGSNTYEDA
AAYIQAQFES KNRSPNKEIY CHMTCATDTN NIQVVFDAVT DIIIANNLRG CGLY
