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Protein

Guanine nucleotide-binding protein G(T) subunit gamma-T1

Gene

Gngt1

Organism
Mus musculus (Mouse)
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 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. cardiac muscle cell apoptotic process Source: MGI
  2. cellular response to hypoxia Source: MGI
  3. eye photoreceptor cell development Source: MGI
  4. G-protein coupled receptor signaling pathway Source: MGI
  5. metabolic process Source: GOC
  6. phototransduction Source: MGI
  7. protein localization Source: MGI
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_311545. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_325400. Olfactory Signaling Pathway.
REACT_326042. Activation of the phototransduction cascade.
REACT_339334. Activation of G protein gated Potassium channels.
REACT_339920. Glucagon-type ligand receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein G(T) subunit gamma-T1
Alternative name(s):
Transducin gamma chain
Gene namesi
Name:Gngt1
Synonyms:Gng1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:109165. Gngt1.

Subcellular locationi

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

GO - Cellular componenti

  1. heterotrimeric G-protein complex Source: MGI
  2. photoreceptor inner segment Source: Ensembl
  3. photoreceptor outer segment Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 7170Guanine nucleotide-binding protein G(T) subunit gamma-T1PRO_0000012607Add
BLAST
Propeptidei72 – 743Removed in mature formBy similarityPRO_0000012608

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei71 – 711Cysteine methyl ester1 Publication
Lipidationi71 – 711S-farnesyl cysteine1 Publication

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiQ61012.
PRIDEiQ61012.

PTM databases

PhosphoSiteiQ61012.

Expressioni

Tissue specificityi

Retinal rod outer segment.

Gene expression databases

BgeeiQ61012.
GenevestigatoriQ61012.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiQ61012. 1 interaction.
STRINGi10090.ENSMUSP00000031673.

Structurei

3D structure databases

ProteinModelPortaliQ61012.
SMRiQ61012. Positions 1-68.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the G protein gamma family.Curated

Phylogenomic databases

eggNOGiNOG291971.
GeneTreeiENSGT00530000063397.
HOVERGENiHBG014983.
InParanoidiQ61012.
KOiK04548.
OMAiKGGCVIC.
OrthoDBiEOG7H1JP7.
PhylomeDBiQ61012.
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.

Q61012-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVINIEDLT EKDKLKMEVD QLKKEVTLER MMVSKCCEEV RDYIEERSGE
60 70
DPLVKGIPED KNPFKELKGG CVIS
Length:74
Mass (Da):8,528
Last modified:January 23, 2007 - v3
Checksum:i3ABB43EF45CE02F4
GO

Mass spectrometryi

Molecular mass is 8314.5±0.1 Da from positions 2 - 71. Determined by ESI. Includes farnesylation and methylation.1 Publication
Molecular mass is 695.5±0.1 Da from positions 67 - 71. Determined by MALDI. Includes farnesylation and methylation.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK020863 mRNA. Translation: BAB32232.1.
AK020903 mRNA. Translation: BAB32247.1.
BC025929 mRNA. Translation: AAH25929.1.
U38495 mRNA. Translation: AAB01726.1.
CCDSiCCDS39418.1.
RefSeqiNP_034444.1. NM_010314.2.
XP_006505047.1. XM_006504984.1.
XP_006505048.1. XM_006504985.2.
XP_006505049.1. XM_006504986.1.
UniGeneiMm.95398.

Genome annotation databases

EnsembliENSMUST00000031673; ENSMUSP00000031673; ENSMUSG00000029663.
GeneIDi14699.
KEGGimmu:14699.
UCSCiuc009avi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK020863 mRNA. Translation: BAB32232.1.
AK020903 mRNA. Translation: BAB32247.1.
BC025929 mRNA. Translation: AAH25929.1.
U38495 mRNA. Translation: AAB01726.1.
CCDSiCCDS39418.1.
RefSeqiNP_034444.1. NM_010314.2.
XP_006505047.1. XM_006504984.1.
XP_006505048.1. XM_006504985.2.
XP_006505049.1. XM_006504986.1.
UniGeneiMm.95398.

3D structure databases

ProteinModelPortaliQ61012.
SMRiQ61012. Positions 1-68.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ61012. 1 interaction.
STRINGi10090.ENSMUSP00000031673.

PTM databases

PhosphoSiteiQ61012.

Proteomic databases

MaxQBiQ61012.
PRIDEiQ61012.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031673; ENSMUSP00000031673; ENSMUSG00000029663.
GeneIDi14699.
KEGGimmu:14699.
UCSCiuc009avi.1. mouse.

Organism-specific databases

CTDi2792.
MGIiMGI:109165. Gngt1.

Phylogenomic databases

eggNOGiNOG291971.
GeneTreeiENSGT00530000063397.
HOVERGENiHBG014983.
InParanoidiQ61012.
KOiK04548.
OMAiKGGCVIC.
OrthoDBiEOG7H1JP7.
PhylomeDBiQ61012.
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_311545. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_325400. Olfactory Signaling Pathway.
REACT_326042. Activation of the phototransduction cascade.
REACT_339334. Activation of G protein gated Potassium channels.
REACT_339920. Glucagon-type ligand receptors.

Miscellaneous databases

ChiTaRSiGngt1. mouse.
NextBioi286659.
PROiQ61012.
SOURCEiSearch...

Gene expression databases

BgeeiQ61012.
GenevestigatoriQ61012.

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. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Retina.
  2. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Eye.
  3. "Top-down analysis of protein isoprenylation by electrospray ionization hybrid quadrupole time-of-flight tandem mass spectrometry; the mouse Tgamma protein."
    Kassai H., Satomi Y., Fukada Y., Takao T.
    Rapid Commun. Mass Spectrom. 19:269-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-71, ISOPRENYLATION AT CYS-71, METHYLATION AT CYS-71, MASS SPECTROMETRY.
  4. "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(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-66.
    Strain: CF-1 / Harlan.
    Tissue: Retina.

Entry informationi

Entry nameiGBG1_MOUSE
AccessioniPrimary (citable) accession number: Q61012
Secondary accession number(s): Q9CR01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 123 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. 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.