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Protein

Guanine nucleotide-binding protein G(o) subunit alpha

Gene

Gnao1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Metal bindingi47MagnesiumBy similarity1
Metal bindingi182MagnesiumBy similarity1
Binding sitei326GTP; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi40 – 47GTPBy similarity8
Nucleotide bindingi176 – 182GTPBy similarity7
Nucleotide bindingi201 – 205GTPBy similarity5
Nucleotide bindingi270 – 273GTPBy similarity4

GO - Molecular functioni

  • corticotropin-releasing hormone receptor 1 binding Source: RGD
  • GDP binding Source: RGD
  • G-protein beta/gamma-subunit complex binding Source: GO_Central
  • 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
  • signal transducer activity Source: GO_Central

GO - Biological processi

  • adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: GO_Central
  • aging Source: RGD
  • cellular process Source: RGD
  • dopamine receptor signaling pathway Source: RGD
  • forebrain development Source: RGD
  • G-protein coupled receptor signaling pathway Source: RGD
  • locomotory behavior Source: RGD
  • 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: RGD
  • 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

Keywordsi

Molecular functionTransducer
LigandGTP-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
R-RNO-6814122 Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding
SABIO-RKiP59215

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi628732 Gnao1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002037062 – 354Guanine nucleotide-binding protein G(o) subunit alphaAdd BLAST353

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine1 Publication1
Lipidationi3S-palmitoyl cysteine1 Publication1
Modified residuei346Deamidated asparagine; in form Alpha-31 Publication1

Post-translational modificationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei351Not S-palmitoylated1 Publication1

Keywords - PTMi

Lipoprotein, Myristate, Palmitate

Proteomic databases

PaxDbiP59215
PRIDEiP59215

PTM databases

iPTMnetiP59215
PhosphoSitePlusiP59215
SwissPalmiP59215

Expressioni

Gene expression databases

BgeeiENSRNOG00000019482
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

Binary interactionsi

Show more details

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-protein interaction databases

BioGridi248412, 3 interactors
DIPiDIP-59090N
IntActiP59215, 20 interactors
MINTiP59215
STRINGi10116.ENSRNOP00000026373

Structurei

3D structure databases

ProteinModelPortaliP59215
SMRiP59215
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
OMAiVARMEDT
OrthoDBiEOG091G0VUT
PhylomeDBiP59215
TreeFamiTF300673

Family and domain databases

CDDicd00066 G-alpha, 1 hit
Gene3Di1.10.400.10, 1 hit
InterProiView protein in InterPro
IPR001408 Gprotein_alpha_I
IPR001019 Gprotein_alpha_su
IPR011025 GproteinA_insert
IPR027417 P-loop_NTPase
PANTHERiPTHR10218 PTHR10218, 1 hit
PfamiView protein in Pfam
PF00503 G-alpha, 1 hit
PRINTSiPR00318 GPROTEINA
PR00441 GPROTEINAI
SMARTiView protein in SMART
SM00275 G_alpha, 1 hit
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)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_031252247 – 354SLMLF…GCGLY → FLKLFDSICNNKWFTDTSII LFLNKKDIFEEKIKKSPLTI CFPEYTGPSAFTEAVAHIQG QYESKNKSAHKEVYSHVTCA TDTNNIQFVFDAVTDVIIAK NLRGCGLY in isoform Alpha-2. 1 PublicationAdd BLAST108

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]
UniGeneiRn.90161

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiGNAO_RAT
AccessioniPrimary (citable) accession number: P59215
Secondary accession number(s): P04900, P30033
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: April 25, 2018
This is version 149 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health