GNAO_CRILO
ID GNAO_CRILO Reviewed; 354 AA.
AC P59216; P04900; P17806;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Guanine nucleotide-binding protein G(o) subunit alpha;
GN Name=GNAO1; Synonyms=GNA0, GNAO;
OS Cricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10030;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-1 AND ALPHA-2).
RX PubMed=2113531; DOI=10.1016/s0021-9258(19)38579-5;
RA Hsu W.H., Rudolph U., Sanford J., Bertrand P., Olate J., Nelson C.,
RA Moss L.G., Boyd A.E. III, Codina J., Birnbaumer L.;
RT "Molecular cloning of a novel splice variant of the alpha subunit of the
RT mammalian Go protein.";
RL J. Biol. Chem. 265:11220-11226(1990).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Alpha-1;
CC IsoId=P59216-1; Sequence=Displayed;
CC Name=Alpha-2;
CC IsoId=P59216-2, P17806-1;
CC Sequence=VSP_031249;
CC -!- PTM: Deamidation of Asn-346 converts alpha-1 to alpha-3.
CC {ECO:0000250|UniProtKB:P59215}.
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; M33661; AAA36987.1; -; mRNA.
DR EMBL; M33662; AAA36988.1; -; mRNA.
DR AlphaFoldDB; P59216; -.
DR SMR; P59216; -.
DR PRIDE; P59216; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IEA:InterPro.
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 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; GTP-binding; Lipoprotein; Magnesium;
KW Membrane; Metal-binding; Myristate; Nucleotide-binding; Palmitate;
KW 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_0000203700"
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 MOD_RES 346
FT /note="Deamidated asparagine; in form Alpha-3"
FT /evidence="ECO:0000250"
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 LFDSICNNKWFTDTSIILFLNKKDIFEEKITRSPLTICFPEYTGPSAFTEAVAHIQGQY
FT ESKNKSAHKEIYTHFTCATDTNNIQFVFDAVTDVIIAKNLRGCGLY (in isoform
FT Alpha-2)"
FT /evidence="ECO:0000303|PubMed:2113531"
FT /id="VSP_031249"
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
