Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Guanine nucleotide-binding protein G(k) subunit alpha

Gene

Gnai3

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

Functioni

Heterotrimeric guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (PubMed:2159473). Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins. Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels. Stimulates the activity of receptor-regulated K+ channels. The active GTP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471MagnesiumBy similarity
Metal bindingi181 – 1811MagnesiumBy similarity
Binding sitei326 – 3261GTP; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi43 – 486GTPBy similarity
Nucleotide bindingi150 – 1512GTPBy similarity
Nucleotide bindingi175 – 1817GTPBy similarity
Nucleotide bindingi200 – 2045GTPBy similarity
Nucleotide bindingi269 – 2724GTPBy similarity

GO - Molecular functioni

  • GDP binding Source: UniProtKB
  • 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: UniProtKB
  • GTP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • protein domain specific binding Source: RGD
  • signal transducer activity Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transducer

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiR-RNO-112043. PLC beta mediated events.
R-RNO-170670. Adenylate cyclase inhibitory pathway.
R-RNO-202040. G-protein activation.
R-RNO-392170. ADP signalling through P2Y purinoceptor 12.
R-RNO-418594. G alpha (i) signalling events.
SABIO-RKP08753.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein G(k) subunit alpha
Alternative name(s):
G(i) alpha-3
Gene namesi
Name:Gnai3
Synonyms:Gnai-3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi2714. Gnai3.

Subcellular locationi

  • Cytoplasm By similarity
  • Cell membrane By similarity
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity
  • Membrane By similarity; Lipid-anchor By similarity

  • Note: Localizes in the centrosomes of interphase and mitotic cells. Detected at the cleavage furrow and/or the midbody.By similarity

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: Ensembl
  • Golgi membrane Source: UniProtKB
  • heterotrimeric G-protein complex Source: GO_Central
  • lysosomal membrane Source: Ensembl
  • membrane Source: RGD
  • membrane raft Source: RGD
  • midbody Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • zymogen granule Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 354353Guanine nucleotide-binding protein G(k) subunit alphaPRO_0000203694Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Lipidationi3 – 31S-palmitoyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Myristate, Palmitate

Proteomic databases

PaxDbiP08753.
PRIDEiP08753.

PTM databases

iPTMnetiP08753.
PhosphoSiteiP08753.
SwissPalmiP08753.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

GenevisibleiP08753. RN.

Interactioni

Subunit structurei

Heterotrimeric G proteins are composed of 3 units; alpha, beta and gamma. The alpha subunit contains the guanine nucleotide binding site (PubMed:2159473). GTP binding causes dissociation of the heterotrimer, liberating the individual subunits so that they can interact with downstream effector proteins. Interacts with GPSM1 (PubMed:11121039). Interacts (GDP-bound form) with GPSM2 (via GoLoco domains). Does not interact with RGS2. Interacts with RGS8 and RGS10; this strongly enhances the intrinsic GTPase activity (By similarity). Interacts with RGS12 (PubMed:11387333). Interacts with RGS16; this strongly enhances the intrinsic GTPase activity (By similarity). Interacts (via active GTP- or inactive GDP-bound form) with RGS14 (PubMed:11387333, PubMed:16870394).By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RGS19P497954EBI-874897,EBI-874907From a different organism.
Wasf1Q5BJU72EBI-874897,EBI-7269229

GO - Molecular functioni

  • G-protein beta/gamma-subunit complex binding Source: GO_Central
  • G-protein coupled serotonin receptor binding Source: RGD
  • GTPase activating protein binding Source: RGD
  • protein domain specific binding Source: RGD

Protein-protein interaction databases

DIPiDIP-608N.
IntActiP08753. 2 interactions.
MINTiMINT-1795694.
STRINGi10116.ENSRNOP00000026710.

Structurei

3D structure databases

ProteinModelPortaliP08753.
SMRiP08753. Positions 5-348.
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.
HOVERGENiHBG063184.
InParanoidiP08753.
KOiK04630.
OMAiISQINYI.
OrthoDBiEOG72C50B.
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.

Sequencei

Sequence statusi: Complete.

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

P08753-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGCTLSAEDK AAVERSKMID RNLREDGEKA AKEVKLLLLG AGESGKSTIV
60 70 80 90 100
KQMKIIHEDG YSEDECKQYK VVVYSNTIQS IIAIIRAMGR LKIDFGEAAR
110 120 130 140 150
ADDARQLFVL AGSAEEGVMT SELAGVIKRL WRDGGVQACF SRSREYQLND
160 170 180 190 200
SASYYLNDLD RISQTNYIPT QQDVLRTRVK TTGIVETHFT FKELYFKMFD
210 220 230 240 250
VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM NRMHESMKLF
260 270 280 290 300
DSICNNKWFT DTSIILFLNK KDLFEEKIKR SPLTICYPEY TGSNTYEEAA
310 320 330 340 350
AYIQCQFEDL NRRKDTKEVY THFTCATDTK NVQFVFDAVT DVIIKNNLKE

CGLY
Length:354
Mass (Da):40,522
Last modified:January 23, 2007 - v3
Checksum:iA65D63CE5A32C777
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03219 mRNA. Translation: AAA41224.1.
M20713 mRNA. Translation: AAA40823.1.
PIRiE27423. RGRTI3.
RefSeqiNP_037238.1. NM_013106.1.
UniGeneiRn.4368.

Genome annotation databases

EnsembliENSRNOT00000026710; ENSRNOP00000026710; ENSRNOG00000019465.
GeneIDi25643.
KEGGirno:25643.
UCSCiRGD:2714. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03219 mRNA. Translation: AAA41224.1.
M20713 mRNA. Translation: AAA40823.1.
PIRiE27423. RGRTI3.
RefSeqiNP_037238.1. NM_013106.1.
UniGeneiRn.4368.

3D structure databases

ProteinModelPortaliP08753.
SMRiP08753. Positions 5-348.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-608N.
IntActiP08753. 2 interactions.
MINTiMINT-1795694.
STRINGi10116.ENSRNOP00000026710.

PTM databases

iPTMnetiP08753.
PhosphoSiteiP08753.
SwissPalmiP08753.

Proteomic databases

PaxDbiP08753.
PRIDEiP08753.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000026710; ENSRNOP00000026710; ENSRNOG00000019465.
GeneIDi25643.
KEGGirno:25643.
UCSCiRGD:2714. rat.

Organism-specific databases

CTDi2773.
RGDi2714. Gnai3.

Phylogenomic databases

eggNOGiKOG0082. Eukaryota.
ENOG410XNVQ. LUCA.
GeneTreeiENSGT00760000118851.
HOVERGENiHBG063184.
InParanoidiP08753.
KOiK04630.
OMAiISQINYI.
OrthoDBiEOG72C50B.
TreeFamiTF300673.

Enzyme and pathway databases

ReactomeiR-RNO-112043. PLC beta mediated events.
R-RNO-170670. Adenylate cyclase inhibitory pathway.
R-RNO-202040. G-protein activation.
R-RNO-392170. ADP signalling through P2Y purinoceptor 12.
R-RNO-418594. G alpha (i) signalling events.
SABIO-RKP08753.

Miscellaneous databases

PROiP08753.

Gene expression databases

GenevisibleiP08753. 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. "Presence of three distinct molecular species of Gi protein alpha subunit. Structure of rat cDNAs and human genomic DNAs."
    Itoh H., Toyama R., Kozasa T., Tsukamoto T., Matsuoka M., Kaziro Y.
    J. Biol. Chem. 263:6656-6664(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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], TISSUE SPECIFICITY.
  3. "Purification and characterization of Go alpha and three types of Gi alpha after expression in Escherichia coli."
    Linder M.E., Ewald D.A., Miller R.J., Gilman A.G.
    J. Biol. Chem. 265:8243-8251(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 111-125, FUNCTION, SUBUNIT.
  4. "Activator of G protein signaling 3 is a guanine dissociation inhibitor for Galpha i subunits."
    de Vries L., Fischer T., Tronchere H., Brothers G.M., Strockbine B., Siderovski D.P., Farquhar M.G.
    Proc. Natl. Acad. Sci. U.S.A. 97:14364-14369(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GPSM1.
  5. "RGS12 and RGS14 GoLoco motifs are G alpha(i) interaction sites with guanine nucleotide dissociation inhibitor activity."
    Kimple R.J., De Vries L., Tronchere H., Behe C.I., Morris R.A., Gist Farquhar M., Siderovski D.P.
    J. Biol. Chem. 276:29275-29281(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RGS12 AND RGS14.
  6. "Selective interactions between Gi alpha1 and Gi alpha3 and the GoLoco/GPR domain of RGS14 influence its dynamic subcellular localization."
    Shu F.J., Ramineni S., Amyot W., Hepler J.R.
    Cell. Signal. 19:163-176(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RGS14.

Entry informationi

Entry nameiGNAI3_RAT
AccessioniPrimary (citable) accession number: P08753
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 152 of the entry and version 3 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.