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Protein

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3

Gene

Gng3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.

GO - Molecular functioni

  1. GTPase activity Source: MGI
  2. signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  1. G-protein coupled receptor signaling pathway Source: MGI
  2. metabolic process Source: GOC
  3. positive regulation of cytosolic calcium ion concentration Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Enzyme and pathway databases

ReactomeiREACT_272374. Adrenaline,noradrenaline inhibits insulin secretion.
REACT_286837. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_297430. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_308732. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
REACT_339334. Activation of G protein gated Potassium channels.
REACT_339920. Glucagon-type ligand receptors.
REACT_345203. Glucagon signaling in metabolic regulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3
Gene namesi
Name:Gng3
Synonyms:Gngt3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:102704. Gng3.

Subcellular locationi

  1. Cell membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated

GO - Cellular componenti

  1. heterotrimeric G-protein complex Source: MGI
  2. neuronal postsynaptic density Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7272Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3PRO_0000012619Add
BLAST
Propeptidei73 – 753Removed in mature formBy similarityPRO_0000012620

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei72 – 721Cysteine methyl esterBy similarity
Lipidationi72 – 721S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiP63216.
PaxDbiP63216.
PRIDEiP63216.

PTM databases

PhosphoSiteiP63216.

Expressioni

Tissue specificityi

Abundantly expressed in brain. Low levels in testis.

Gene expression databases

BgeeiP63216.
GenevestigatoriP63216.

Interactioni

Subunit structurei

G proteins are composed of 3 units, alpha, beta and gamma.

Protein-protein interaction databases

IntActiP63216. 1 interaction.
STRINGi10090.ENSMUSP00000093978.

Structurei

3D structure databases

ProteinModelPortaliP63216.
SMRiP63216. Positions 12-71.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the G protein gamma family.Curated

Phylogenomic databases

eggNOGiNOG279844.
GeneTreeiENSGT00760000119218.
HOVERGENiHBG014983.
InParanoidiP63216.
KOiK04540.
OMAiEASMCRI.
OrthoDBiEOG7H1JP7.
PhylomeDBiP63216.
TreeFamiTF319909.

Family and domain databases

Gene3Di4.10.260.10. 1 hit.
InterProiIPR015898. G-protein_gamma-like_dom.
IPR001770. Gprotein-gamma.
[Graphical view]
PANTHERiPTHR13809. PTHR13809. 1 hit.
PfamiPF00631. G-gamma. 1 hit.
[Graphical view]
PRINTSiPR00321. GPROTEING.
SMARTiSM00224. GGL. 1 hit.
[Graphical view]
SUPFAMiSSF48670. SSF48670. 1 hit.
PROSITEiPS50058. G_PROTEIN_GAMMA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P63216-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGETPVNST MSIGQARKMV EQLKIEASLC RIKVSKAAAD LMTYCDAHAC
60 70
EDPLITPVPT SENPFREKKF FCALL
Length:75
Mass (Da):8,305
Last modified:September 27, 2004 - v1
Checksum:i35CC03965FE69A9D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF069953 Genomic DNA. Translation: AAC83941.1.
AK004459 mRNA. Translation: BAB23313.1.
AK032646 mRNA. Translation: BAC27969.1.
BC029680 mRNA. Translation: AAH29680.1.
U38497 mRNA. Translation: AAB01728.1.
CCDSiCCDS29550.1.
PIRiJC4340.
RefSeqiNP_034446.1. NM_010316.3.
UniGeneiMm.329700.

Genome annotation databases

EnsembliENSMUST00000096259; ENSMUSP00000093978; ENSMUSG00000071658.
GeneIDi14704.
KEGGimmu:14704.
UCSCiuc008gnh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF069953 Genomic DNA. Translation: AAC83941.1.
AK004459 mRNA. Translation: BAB23313.1.
AK032646 mRNA. Translation: BAC27969.1.
BC029680 mRNA. Translation: AAH29680.1.
U38497 mRNA. Translation: AAB01728.1.
CCDSiCCDS29550.1.
PIRiJC4340.
RefSeqiNP_034446.1. NM_010316.3.
UniGeneiMm.329700.

3D structure databases

ProteinModelPortaliP63216.
SMRiP63216. Positions 12-71.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP63216. 1 interaction.
STRINGi10090.ENSMUSP00000093978.

PTM databases

PhosphoSiteiP63216.

Proteomic databases

MaxQBiP63216.
PaxDbiP63216.
PRIDEiP63216.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000096259; ENSMUSP00000093978; ENSMUSG00000071658.
GeneIDi14704.
KEGGimmu:14704.
UCSCiuc008gnh.1. mouse.

Organism-specific databases

CTDi2785.
MGIiMGI:102704. Gng3.

Phylogenomic databases

eggNOGiNOG279844.
GeneTreeiENSGT00760000119218.
HOVERGENiHBG014983.
InParanoidiP63216.
KOiK04540.
OMAiEASMCRI.
OrthoDBiEOG7H1JP7.
PhylomeDBiP63216.
TreeFamiTF319909.

Enzyme and pathway databases

ReactomeiREACT_272374. Adrenaline,noradrenaline inhibits insulin secretion.
REACT_286837. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_297430. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_308732. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
REACT_339334. Activation of G protein gated Potassium channels.
REACT_339920. Glucagon-type ligand receptors.
REACT_345203. Glucagon signaling in metabolic regulation.

Miscellaneous databases

NextBioi286679.
PROiP63216.
SOURCEiSearch...

Gene expression databases

BgeeiP63216.
GenevestigatoriP63216.

Family and domain databases

Gene3Di4.10.260.10. 1 hit.
InterProiIPR015898. G-protein_gamma-like_dom.
IPR001770. Gprotein-gamma.
[Graphical view]
PANTHERiPTHR13809. PTHR13809. 1 hit.
PfamiPF00631. G-gamma. 1 hit.
[Graphical view]
PRINTSiPR00321. GPROTEING.
SMARTiSM00224. GGL. 1 hit.
[Graphical view]
SUPFAMiSSF48670. SSF48670. 1 hit.
PROSITEiPS50058. G_PROTEIN_GAMMA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: Brain.
  2. "Structure and mapping of the G protein gamma3 subunit gene and a divergently transcribed novel gene, Gng3lg."
    Downes G.B., Copeland N.G., Jenkins N.A., Gautam N.
    Genomics 53:220-230(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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.
    , 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: Cerebellum.
  4. "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].
    Tissue: Eye.
  5. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-17 AND 25-31, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  6. "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 13-68.
    Strain: CF-1 / Harlan.
  7. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.

Entry informationi

Entry nameiGBG3_MOUSE
AccessioniPrimary (citable) accession number: P63216
Secondary accession number(s): P29798, Q61014
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: April 1, 2015
This is version 101 of the entry and version 1 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.