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

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P02698 (GBG1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 121. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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

Alternative name(s):
Transducin gamma chain

Gene names

Name:

GNGT1

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	74 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	G proteins are composed of 3 units, alpha, beta and gamma.
Subcellular location	Cell membrane; Lipid-anchor; Cytoplasmic side Potential.
Tissue specificity	Retinal rod outer segment.
Sequence similarities	Belongs to the G protein gamma family.
Caution	In Ref.5 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.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Molecular function	Transducer
PTM	Lipoprotein Methylation Prenylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: InterPro eye photoreceptor cell development Inferred from electronic annotation. Source: Compara phototransduction Inferred from electronic annotation. Source: Compara protein localization Inferred from electronic annotation. Source: Compara
Cellular_component	heterotrimeric G-protein complex Inferred from electronic annotation. Source: InterPro
Molecular_function	signal transducer activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.5

Chain

2 – 71

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

PRO_0000012601

Propeptide

72 – 74

Removed in mature form

PRO_0000012602

Amino acid modifications

Modified residue

Cysteine methyl ester Ref.6

Lipidation

S-farnesyl cysteine Ref.6 Ref.7 Ref.8

Secondary structure

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P02698 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: B12B580FABDB1C05
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FASTA

8,544

        10         20         30         40         50         60 
MPVINIEDLT EKDKLKMEVD QLKKEVTLER MLVSKCCEEF RDYVEERSGE DPLVKGIPED 

        70 
KNPFKELKGG CVIS

« Hide

References

[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]	"The gamma subunit of transducin is farnesylated." Lai R.K., Perez-Sala D., Canada F.J., Rando R.R. Proc. Natl. Acad. Sci. U.S.A. 87:7673-7677(1990) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

K03255 mRNA. Translation: AAA30794.1.
K02199 mRNA. Translation: AAA30793.1.
S62031, S62029 Genomic DNA. Translation: AAB26895.1.
K02436 mRNA. Translation: AAA30788.1.

IPI

IPI00695759.

PIR

RGBOGT. I46939.

RefSeq

NP_776752.1. NM_174327.2.

UniGene

Bt.473.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A0R	X-ray	2.80	G	2-66	[»]
1B9X	X-ray	3.00	B	1-67	[»]
1B9Y	X-ray	3.00	B	1-67	[»]
1GOT	X-ray	2.00	G	2-65	[»]
1MF6	NMR	-	A	60-71	[»]
1TBG	X-ray	2.10	E/F/G/H	2-68	[»]
2TRC	X-ray	2.40	G	2-67	[»]

ProteinModelPortal

P02698.

SMR

P02698. Positions 1-68.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29228N.

MINT

MINT-94580.

STRING

9913.ENSBTAP00000003465.

Proteomic databases

PRIDE

P02698.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000003465; ENSBTAP00000003465; ENSBTAG00000002674.

GeneID

281796.

KEGG

bta:281796.

Organism-specific databases

CTD

2792.

Phylogenomic databases

eggNOG

NOG291971.

GeneTree

ENSGT00530000063397.

HOGENOM

HOG000231034.

HOVERGEN

HBG014983.

InParanoid

P02698.

K04548.

OMA

EVKLERW.

OrthoDB

EOG4TMR3S.

Enzyme and pathway databases

BioCyc

CATTLE:281796-MONOMER.

Family and domain databases

Gene3D

4.10.260.10. 1 hit.

InterPro

IPR015898. G-protein_gamma-like_dom.
IPR001770. Gprotein-gamma.
[Graphical view]

PANTHER

PTHR13809. PTHR13809. 1 hit.

Pfam

PF00631. G-gamma. 1 hit.
[Graphical view]

PRINTS

PR00321. GPROTEING.

SMART

SM00224. GGL. 1 hit.
[Graphical view]

SUPFAM

SSF48670. G-protein_gamma-like. 1 hit.

PROSITE

PS50058. G_PROTEIN_GAMMA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P02698.

NextBio

20805709.

Entry information

Entry name

GBG1_BOVIN

Accession

Primary (citable) accession number: P02698

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 121 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents