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Protein

Guanine nucleotide-binding protein G(o) subunit alpha

Gene

Gnao1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(o) protein function is not clear. Stimulated by RGS14 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471MagnesiumBy similarity
Metal bindingi182 – 1821MagnesiumBy similarity
Binding sitei326 – 3261GTP; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi40 – 478GTPBy similarity
Nucleotide bindingi176 – 1827GTPBy similarity
Nucleotide bindingi201 – 2055GTPBy similarity
Nucleotide bindingi270 – 2734GTPBy similarity

GO - Molecular functioni

  • corticotropin-releasing hormone receptor 1 binding Source: RGD
  • GDP binding Source: RGD
  • G-protein coupled serotonin receptor binding Source: RGD
  • GTPase activating protein binding Source: RGD
  • GTPase activity Source: RGD
  • GTP binding Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • mu-type opioid receptor binding Source: RGD
  • protein complex binding Source: RGD
  • signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  • adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: InterPro
  • aging Source: RGD
  • dopamine receptor signaling pathway Source: Ensembl
  • forebrain development Source: RGD
  • G-protein coupled receptor signaling pathway Source: RGD
  • locomotory behavior Source: Ensembl
  • negative regulation of calcium ion transport Source: RGD
  • neuron projection development Source: RGD
  • positive regulation of GTPase activity Source: RGD
  • regulation of heart contraction Source: Ensembl
  • response to cytokine Source: RGD
  • response to drug Source: RGD
  • response to hydrogen peroxide Source: RGD
  • response to morphine Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to organonitrogen compound Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Keywords - Ligandi

GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-112043. PLC beta mediated events.
R-RNO-202040. G-protein activation.
R-RNO-4086398. Ca2+ pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein G(o) subunit alpha
Gene namesi
Name:Gnao1
Synonyms:Gna0, Gnao
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi628732. Gnao1.

Subcellular locationi

  • Cell membrane By similarity
  • Membrane By similarity; Lipid-anchor By similarity

GO - Cellular componenti

  • cell body Source: Ensembl
  • dendrite Source: Ensembl
  • membrane Source: RGD
  • myelin sheath Source: UniProtKB
  • neuron projection Source: RGD
  • plasma membrane Source: UniProtKB-SubCell
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 354353Guanine nucleotide-binding protein G(o) subunit alphaPRO_0000203706Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Lipidationi3 – 31S-palmitoyl cysteine1 Publication
Modified residuei346 – 3461Deamidated asparagine; in form Alpha-31 Publication

Post-translational modificationi

Deamidation of Asn-346 converts alpha-1 to alpha-3.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei351 – 3511Not S-palmitoylated

Keywords - PTMi

Lipoprotein, Myristate, Palmitate

Proteomic databases

PaxDbiP59215.
PRIDEiP59215.

PTM databases

iPTMnetiP59215.
PhosphoSiteiP59215.
SwissPalmiP59215.

Expressioni

Gene expression databases

GenevisibleiP59215. RN.

Interactioni

Subunit structurei

Interacts with RGS14 (By similarity). G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site.By similarity

GO - Molecular functioni

  • corticotropin-releasing hormone receptor 1 binding Source: RGD
  • G-protein coupled serotonin receptor binding Source: RGD
  • GTPase activating protein binding Source: RGD
  • mu-type opioid receptor binding Source: RGD
  • protein complex binding Source: RGD

Protein-protein interaction databases

BioGridi248412. 3 interactions.
DIPiDIP-59090N.
IntActiP59215. 4 interactions.
MINTiMINT-5028451.
STRINGi10116.ENSRNOP00000026373.

Structurei

3D structure databases

ProteinModelPortaliP59215.
SMRiP59215. Positions 5-353.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the G-alpha family. G(i/o/t/z) subfamily.Curated

Phylogenomic databases

eggNOGiKOG0082. Eukaryota.
ENOG410XNVQ. LUCA.
GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038730.
HOVERGENiHBG063184.
InParanoidiP59215.
KOiK04534.
OrthoDBiEOG72C50B.
PhylomeDBiP59215.
TreeFamiTF300673.

Family and domain databases

Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR001408. Gprotein_alpha_I.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10218. PTHR10218. 1 hit.
PfamiPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSiPR00318. GPROTEINA.
PR00441. GPROTEINAI.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Alpha-1 (identifier: P59215-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGCTLSAEER AALERSKAIE KNLKEDGISA AKDVKLLLLG AGESGKSTIV
60 70 80 90 100
KQMKIIHEDG FSGEDVKQYK PVVYSNTIQS LAAIVRAMDT LGVEYGDKER
110 120 130 140 150
KADSKMVCDV VSRMEDTEPF SAELLSAMMR LWGDSGIQEC FNRSREYQLN
160 170 180 190 200
DSAKYYLDSL DRIGAADYQP TEQDILRTRV KTTGIVETHF TFKNLHFRLF
210 220 230 240 250
DVGGQRSERK KWIHCFEDVT AIIFCVALSG YDQVLHEDET TNRMHESLML
260 270 280 290 300
FDSICNNKFF IDTSIILFLN KKDLFGEKIK KSPLTICFPE YPGSNTYEDA
310 320 330 340 350
AAYIQTQFES KNRSPNKEIY CHMTCATDTN NIQVVFDAVT DIIIANNLRG

CGLY
Length:354
Mass (Da):40,069
Last modified:January 23, 2007 - v2
Checksum:i577024F61B179C89
GO
Isoform Alpha-2 (identifier: P59215-2) [UniParc] [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     247-354: SLMLFDSICN...ANNLRGCGLY → FLKLFDSICN...AKNLRGCGLY

Show »
Length:354
Mass (Da):40,081
Checksum:i1C9D8AB39DC03CE3
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei247 – 354108SLMLF…GCGLY → FLKLFDSICNNKWFTDTSII LFLNKKDIFEEKIKKSPLTI CFPEYTGPSAFTEAVAHIQG QYESKNKSAHKEVYSHVTCA TDTNNIQFVFDAVTDVIIAK NLRGCGLY in isoform Alpha-2. 1 PublicationVSP_031252Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17526 mRNA. Translation: AAA40826.1.
M12671 mRNA. Translation: AAA41262.1.
PIRiC40436. RGRTO1.
D40436. RGRTO2.
RefSeqiNP_059023.1. NM_017327.1. [P59215-1]
XP_008770542.1. XM_008772320.1. [P59215-1]
UniGeneiRn.90161.

Genome annotation databases

EnsembliENSRNOT00000026373; ENSRNOP00000026373; ENSRNOG00000019482. [P59215-1]
GeneIDi50664.
KEGGirno:50664.
UCSCiRGD:628732. rat. [P59215-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17526 mRNA. Translation: AAA40826.1.
M12671 mRNA. Translation: AAA41262.1.
PIRiC40436. RGRTO1.
D40436. RGRTO2.
RefSeqiNP_059023.1. NM_017327.1. [P59215-1]
XP_008770542.1. XM_008772320.1. [P59215-1]
UniGeneiRn.90161.

3D structure databases

ProteinModelPortaliP59215.
SMRiP59215. Positions 5-353.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248412. 3 interactions.
DIPiDIP-59090N.
IntActiP59215. 4 interactions.
MINTiMINT-5028451.
STRINGi10116.ENSRNOP00000026373.

PTM databases

iPTMnetiP59215.
PhosphoSiteiP59215.
SwissPalmiP59215.

Proteomic databases

PaxDbiP59215.
PRIDEiP59215.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000026373; ENSRNOP00000026373; ENSRNOG00000019482. [P59215-1]
GeneIDi50664.
KEGGirno:50664.
UCSCiRGD:628732. rat. [P59215-1]

Organism-specific databases

CTDi2775.
RGDi628732. Gnao1.

Phylogenomic databases

eggNOGiKOG0082. Eukaryota.
ENOG410XNVQ. LUCA.
GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038730.
HOVERGENiHBG063184.
InParanoidiP59215.
KOiK04534.
OrthoDBiEOG72C50B.
PhylomeDBiP59215.
TreeFamiTF300673.

Enzyme and pathway databases

ReactomeiR-RNO-112043. PLC beta mediated events.
R-RNO-202040. G-protein activation.
R-RNO-4086398. Ca2+ pathway.

Miscellaneous databases

NextBioi610486.
PROiP59215.

Gene expression databases

GenevisibleiP59215. RN.

Family and domain databases

Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR001408. Gprotein_alpha_I.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10218. PTHR10218. 1 hit.
PfamiPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSiPR00318. GPROTEINA.
PR00441. GPROTEINAI.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning of five GTP-binding protein cDNA species from rat olfactory neuroepithelium."
    Jones D.T., Reed R.R.
    J. Biol. Chem. 262:14241-14249(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1).
  2. "Structure of the human gene and two rat cDNAs encoding the alpha chain of GTP-binding regulatory protein Go: two different mRNAs are generated by alternative splicing."
    Tsukamoto T., Toyama R., Itoh H., Kozasa T., Matsuoka M., Kaziro Y.
    Proc. Natl. Acad. Sci. U.S.A. 88:2974-2978(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-2).
  3. Lubec G., Chen W.-Q.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 22-32; 36-46; 68-86; 87-100; 114-130; 163-177; 182-193; 199-206 AND 244-272, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.
  4. "Molecular cloning and sequence determination of cDNAs for alpha subunits of the guanine nucleotide-binding proteins Gs, Gi, and Go from rat brain."
    Itoh H., Kozasa T., Nagata S., Nakamura S., Katada T., Ui M., Iwai S., Ohtsuka E., Kawasaki H., Suzuki K., Kaziro Y.
    Proc. Natl. Acad. Sci. U.S.A. 83:3776-3780(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 45-354 (ISOFORM ALPHA-1).
  5. "G0 is a major growth cone protein subject to regulation by GAP-43."
    Strittmatter S.M., Valenzuela D., Kennedy T.E., Neer E.J., Fishman M.C.
    Nature 344:836-841(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 55-67; 114-129 AND 163-176.
  6. "A novel N-terminal motif for palmitoylation of G-protein alpha subunits."
    Parenti M., Vigano M.A., Newman C.M.H., Milligan G., Magee A.I.
    Biochem. J. 291:349-353(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-3, ABSENCE OF PALMITOYLATION AT CYS-351.
  7. "Posttranslational modification of Galphao1 generates Galphao3, an abundant G protein in brain."
    Exner T., Jensen O.N., Mann M., Kleuss C., Nurnberg B.
    Proc. Natl. Acad. Sci. U.S.A. 96:1327-1332(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEAMIDATION AT ASN-346.

Entry informationi

Entry nameiGNAO_RAT
AccessioniPrimary (citable) accession number: P59215
Secondary accession number(s): P04900, P30033
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.