GNAO_XENLA
ID GNAO_XENLA Reviewed; 354 AA.
AC P10825;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Guanine nucleotide-binding protein G(o) subunit alpha;
GN Name=gna0;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oocyte;
RX PubMed=2494063; DOI=10.1016/0014-5793(89)81190-1;
RA Olate J., Jorquera H., Purcell P., Codina J., Birnbaumer L., Allende J.E.;
RT "Molecular cloning and sequence determination of a cDNA coding for the
RT alpha-subunit of a Go-type protein of Xenopus laevis oocytes.";
RL FEBS Lett. 244:188-192(1989).
RN [2]
RP ERRATUM OF PUBMED:2494063, AND SEQUENCE REVISION.
RA Olate J., Jorquera H., Purcell P., Codina J., Birnbaumer L., Allende J.E.;
RL FEBS Lett. 267:316-316(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.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC {ECO:0000305}.
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DR EMBL; X14636; CAA32784.1; -; mRNA.
DR PIR; S02785; RGXLOA.
DR RefSeq; NP_001081529.1; NM_001088060.1.
DR AlphaFoldDB; P10825; -.
DR SMR; P10825; -.
DR PRIDE; P10825; -.
DR GeneID; 397896; -.
DR KEGG; xla:397896; -.
DR CTD; 397896; -.
DR Xenbase; XB-GENE-17340914; gnao1.S.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 397896; Expressed in brain and 19 other tissues.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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 GTP-binding; Lipoprotein; Magnesium; Metal-binding; Myristate;
KW Nucleotide-binding; Palmitate; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..354
FT /note="Guanine nucleotide-binding protein G(o) subunit
FT alpha"
FT /id="PRO_0000203708"
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 LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 354 AA; 40464 MW; 4B03687E10532133 CRC64;
MGCTLSAEER AALERSKQIE KNLKEDGVTA AKDVKLLLLG AGESGKSTIV KQMKIIHEDG
FSGEDVKQYK PVVYSNTIQS LAAIVRAMDT LGIEYGDKER RADAKMVCDV VSRMEDTEPY
SPELLSAMVR LWADSGIQEC FNRSREYQLN DSAKYYLDSL DRIGAPDYQP TEQDILRTRV
KTTGIVETHF TFKNLHFRLF DVGGQRSERK KWWHCFEDVT AIIFCVALTG YDQVLHEDET
TNRMHESLKL FDSICNNKWF TDTSIILFLN KKDIFQEKIK SSPLTICFPE YTGPNSFTEA
VAHTQHQYES RNKSENKEIY THITCATDTQ NIQFVFDAVT DVIIAYNLRG CGLY
