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Q9DC51 (GNAI3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanine nucleotide-binding protein G(k) subunit alpha
Alternative name(s):
G(i) alpha-3
Gene names
Name:Gnai3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. G(k) is the stimulatory G protein 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.

Subunit structure

G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts with GPSM1. Interacts with RGS12. Interacts (via active GTP- or inactive GDP-bound form) with RGS14 By similarity. Ref.6

Subcellular location

Cytoplasm By similarity. Cell membrane By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Note: Localizes in the centrosomes of interphase and mitotic cells. Detected at the cleavage furrow and/or the midbody By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processCell cycle
Cell division
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionTransducer
   PTMLipoprotein
Myristate
Palmitate
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Traceable author statement PubMed 2508088. Source: MGI

adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from sequence or structural similarity. Source: UniProtKB

vesicle fusion

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 8192889. Source: MGI

centrosome

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 8192889. Source: MGI

extrinsic component of cytoplasmic side of plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

heterotrimeric G-protein complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

membrane raft

Inferred from electronic annotation. Source: Ensembl

midbody

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

zymogen granule

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionG-protein beta/gamma-subunit complex binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

G-protein coupled serotonin receptor binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

GTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

signal transducer activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NclP094054EBI-641852,EBI-641864

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 354353Guanine nucleotide-binding protein G(k) subunit alpha
PRO_0000203693

Regions

Nucleotide binding40 – 478GTP By similarity
Nucleotide binding175 – 1817GTP By similarity
Nucleotide binding200 – 2045GTP By similarity
Nucleotide binding269 – 2724GTP By similarity

Sites

Metal binding471Magnesium By similarity
Metal binding1811Magnesium By similarity
Binding site3261GTP; via amide nitrogen By similarity

Amino acid modifications

Lipidation21N-myristoyl glycine By similarity
Lipidation31S-palmitoyl cysteine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9DC51 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A03C83CE5488C777

FASTA35440,538
        10         20         30         40         50         60 
MGCTLSAEDK AAVERSKMID RNLREDGEKA AKEVKLLLLG AGESGKSTIV KQMKIIHEDG 

        70         80         90        100        110        120 
YSEDECKQYK VVVYSNTIQS IIAIIRAMGR LKIDFGESAR ADDARQLFVL AGSAEEGVMT 

       130        140        150        160        170        180 
SELAGVIKRL WRDGGVQACF SRSREYQLND SASYYLNDLD RISQTNYIPT QQDVLRTRVK 

       190        200        210        220        230        240 
TTGIVETHFT FKELYFKMFD VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM 

       250        260        270        280        290        300 
NRMHESMKLF DSICNNKWFT DTSIILFLNK KDLFEEKIKR SPLTICYPEY TGSNTYEEAA 

       310        320        330        340        350 
AYIQCQFEDL NRRKDTKEVY THFTCATDTK NVQFVFDAVT DVIIKNNLKE CGLY 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Heart, Kidney and Lung.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
[4]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 36-46; 55-67; 181-192; 198-205 AND 249-257, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[5]"G protein gene expression during mouse oocyte growth and maturation, and preimplantation embryo development."
Williams C.J., Schultz R.M., Kopf G.S.
Mol. Reprod. Dev. 44:315-323(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 248-322.
Strain: CF-1 / Harlan.
[6]"G protein betagamma subunits and AGS3 control spindle orientation and asymmetric cell fate of cerebral cortical progenitors."
Sanada K., Tsai L.-H.
Cell 122:119-131(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GPSM1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK004566 mRNA. Translation: BAB23377.1.
AK077490 mRNA. Translation: BAC36828.1.
AK133749 mRNA. Translation: BAE21821.1.
AK168578 mRNA. Translation: BAE40447.1.
AK169067 mRNA. Translation: BAE40854.1.
AK169285 mRNA. Translation: BAE41043.1.
AL671854 Genomic DNA. Translation: CAM27256.1.
BC041107 mRNA. Translation: AAH41107.1.
U38502 mRNA. Translation: AAB01733.1.
RefSeqNP_034436.1. NM_010306.3.
UniGeneMm.271703.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3AB3X-ray2.40A/C1-28[»]
ProteinModelPortalQ9DC51.
SMRQ9DC51. Positions 5-348.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199968. 1 interaction.
DIPDIP-49479N.
IntActQ9DC51. 3 interactions.
MINTMINT-1718603.

PTM databases

PhosphoSiteQ9DC51.

Proteomic databases

PaxDbQ9DC51.
PRIDEQ9DC51.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000000001; ENSMUSP00000000001; ENSMUSG00000000001.
GeneID14679.
KEGGmmu:14679.
UCSCuc008qyd.1. mouse.

Organism-specific databases

CTD2773.
MGIMGI:95773. Gnai3.

Phylogenomic databases

eggNOGNOG322962.
GeneTreeENSGT00690000101958.
HOGENOMHOG000038730.
HOVERGENHBG063184.
InParanoidA2AE36.
KOK04630.
OMAGEAARAX.
OrthoDBEOG72C50B.
PhylomeDBQ9DC51.
TreeFamTF300673.

Gene expression databases

BgeeQ9DC51.
GenevestigatorQ9DC51.

Family and domain databases

Gene3D1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR001408. Gprotein_alpha_I.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR10218. PTHR10218. 1 hit.
PfamPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSPR00318. GPROTEINA.
PR00441. GPROTEINAI.
SMARTSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNetSearch...

Other

NextBio286582.
PROQ9DC51.
SOURCESearch...

Entry information

Entry nameGNAI3_MOUSE
AccessionPrimary (citable) accession number: Q9DC51
Secondary accession number(s): A2AE36, Q3TGV1, Q61019
Entry history
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot