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(T) subunit gamma-T1

Gene

GNGT1

Organism
Bos taurus (Bovine)
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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transducer

Enzyme and pathway databases

ReactomeiR-BTA-1296041. Activation of G protein gated Potassium channels.
R-BTA-2485179. Activation of the phototransduction cascade.
R-BTA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
R-BTA-381676. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
R-BTA-381753. Olfactory Signaling Pathway.
R-BTA-400042. Adrenaline,noradrenaline inhibits insulin secretion.
R-BTA-420092. Glucagon-type ligand receptors.
R-BTA-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-BTA-997272. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 4

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 7170Guanine nucleotide-binding protein G(T) subunit gamma-T1PRO_0000012601Add
BLAST
Propeptidei72 – 743Removed in mature formPRO_0000012602

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei71 – 711Cysteine methyl ester1 Publication
Lipidationi71 – 711S-farnesyl cysteine3 Publications

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

PaxDbiP02698.
PRIDEiP02698.

Expressioni

Tissue specificityi

Retinal rod outer segment.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-29228N.
IntActiP02698. 1 interaction.
MINTiMINT-94580.
STRINGi9913.ENSBTAP00000003465.

Structurei

Secondary structure

1
74
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Helixi6 – 83Combined sources
Helixi11 – 2515Combined sources
Helixi33 – 4715Combined sources
Helixi48 – 503Combined sources
Helixi52 – 554Combined sources
Helixi59 – 613Combined sources
Helixi62 – 709Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0RX-ray2.80G2-66[»]
1B9XX-ray3.00B1-68[»]
1B9YX-ray3.00B1-68[»]
1GOTX-ray2.00G2-66[»]
1MF6NMR-A60-71[»]
1TBGX-ray2.10E/F/G/H2-68[»]
2TRCX-ray2.40G1-68[»]
ProteinModelPortaliP02698.
SMRiP02698. Positions 1-68.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02698.

Family & Domainsi

Sequence similaritiesi

Belongs to the G protein gamma family.Curated

Phylogenomic databases

eggNOGiKOG4119. Eukaryota.
ENOG41122JF. LUCA.
GeneTreeiENSGT00530000063397.
HOGENOMiHOG000231034.
HOVERGENiHBG014983.
InParanoidiP02698.
KOiK04548.
OMAiKGGCVIC.
OrthoDBiEOG7H1JP7.
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.

P02698-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVINIEDLT EKDKLKMEVD QLKKEVTLER MLVSKCCEEF RDYVEERSGE
60 70
DPLVKGIPED KNPFKELKGG CVIS
Length:74
Mass (Da):8,544
Last modified:January 23, 2007 - v2
Checksum:iB12B580FABDB1C05
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03255 mRNA. Translation: AAA30794.1.
K02199 mRNA. Translation: AAA30793.1.
S62031, S62029 Genomic DNA. Translation: AAB26895.1.
K02436 mRNA. Translation: AAA30788.1.
PIRiI46939. RGBOGT.
RefSeqiNP_776752.1. NM_174327.2.
XP_010802284.1. XM_010803982.2.
XP_010802285.1. XM_010803983.2.
UniGeneiBt.473.

Genome annotation databases

EnsembliENSBTAT00000003465; ENSBTAP00000003465; ENSBTAG00000002674.
GeneIDi281796.
KEGGibta:281796.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03255 mRNA. Translation: AAA30794.1.
K02199 mRNA. Translation: AAA30793.1.
S62031, S62029 Genomic DNA. Translation: AAB26895.1.
K02436 mRNA. Translation: AAA30788.1.
PIRiI46939. RGBOGT.
RefSeqiNP_776752.1. NM_174327.2.
XP_010802284.1. XM_010803982.2.
XP_010802285.1. XM_010803983.2.
UniGeneiBt.473.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0RX-ray2.80G2-66[»]
1B9XX-ray3.00B1-68[»]
1B9YX-ray3.00B1-68[»]
1GOTX-ray2.00G2-66[»]
1MF6NMR-A60-71[»]
1TBGX-ray2.10E/F/G/H2-68[»]
2TRCX-ray2.40G1-68[»]
ProteinModelPortaliP02698.
SMRiP02698. Positions 1-68.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29228N.
IntActiP02698. 1 interaction.
MINTiMINT-94580.
STRINGi9913.ENSBTAP00000003465.

Proteomic databases

PaxDbiP02698.
PRIDEiP02698.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000003465; ENSBTAP00000003465; ENSBTAG00000002674.
GeneIDi281796.
KEGGibta:281796.

Organism-specific databases

CTDi2792.

Phylogenomic databases

eggNOGiKOG4119. Eukaryota.
ENOG41122JF. LUCA.
GeneTreeiENSGT00530000063397.
HOGENOMiHOG000231034.
HOVERGENiHBG014983.
InParanoidiP02698.
KOiK04548.
OMAiKGGCVIC.
OrthoDBiEOG7H1JP7.
TreeFamiTF319909.

Enzyme and pathway databases

ReactomeiR-BTA-1296041. Activation of G protein gated Potassium channels.
R-BTA-2485179. Activation of the phototransduction cascade.
R-BTA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
R-BTA-381676. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
R-BTA-381753. Olfactory Signaling Pathway.
R-BTA-400042. Adrenaline,noradrenaline inhibits insulin secretion.
R-BTA-420092. Glucagon-type ligand receptors.
R-BTA-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-BTA-997272. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.

Miscellaneous databases

EvolutionaryTraceiP02698.
NextBioi20805709.

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

  1. "Isolation and characterization of a cDNA clone for the gamma subunit of bovine retinal transducin."
    Hurley J.B., Fong H.K.W., Teplow D.B., Dreyer W.J., Simon M.I.
    Proc. Natl. Acad. Sci. U.S.A. 81:6948-6952(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "cDNA-derived amino acid sequence of the gamma subunit of GTPase from bovine rod outer segments."
    Yatsunami K., Pandya B.V., Oprian D.D., Khorana H.G.
    Proc. Natl. Acad. Sci. U.S.A. 82:1936-1940(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Structure of the bovine transducin gamma subunit gene and analysis of promoter function in transgenic mice."
    Tao L., Pandey S., Simon M.I., Fong H.K.
    Exp. Eye Res. 56:497-507(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Partial cDNA sequence of the gamma subunit of transducin."
    van Dop C., Medynski D.C., Sullivan K., Wu A.M., Fung B.K.-K., Bourne H.R.
    Biochem. Biophys. Res. Commun. 124:250-255(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-40.
  5. "Complete amino acid sequence of gamma-subunit of the GTP-binding protein from cattle retina."
    Ovchinnikov Y.A., Lipkin V.M., Shuvaeva T.M., Bogachuk A.P., Shemyakin V.V.
    FEBS Lett. 179:107-110(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-70.
  6. "Farnesylated gamma-subunit of photoreceptor G protein indispensable for GTP-binding."
    Fukuda Y., Takao T., Ohguro H., Yoshizawa T., Akino T., Shimonishi Y.
    Nature 346:658-660(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISOPRENYLATION AT CYS-71, METHYLATION AT CYS-71.
  7. "Gamma-subunits of G proteins, but not their alpha- or beta-subunits, are polyisoprenylated. Studies on post-translational modifications using in vitro translation with rabbit reticulocyte lysates."
    Sanford J., Codina J., Birnbaumer L.
    J. Biol. Chem. 266:9570-9579(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISOPRENYLATION AT CYS-71.
  8. Cited for: ISOPRENYLATION AT CYS-71.
  9. "Crystal structure of a G-protein beta gamma dimer at 2.1-A resolution."
    Sondek J., Bohm A., Lambright D.G., Hamm H.E., Sigler P.B.
    Nature 379:369-374(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF BETA-GAMMA DIMER.
  10. "Phosducin induces a structural change in transducin beta gamma."
    Loew A., Ho Y.K., Blundell T., Bax B.
    Structure 6:1007-1019(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH PHOSDUCIN.

Entry informationi

Entry nameiGBG1_BOVIN
AccessioniPrimary (citable) accession number: P02698
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

In PubMed:3917402 the authors propose that Cys-36 and Cys-37 are disulfide bonded because they could not be observed during peptide sequencing, but were observed after reduction by dithiothreitol and reaction with labeled iodoacetamide. The crystallographic structures do not support these cysteines being disulfide bonded. Artifactual oxidation and some other cysteine modifications might be consistent with these observations.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.