P63212 (GBG2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2

Alternative name(s):
G gamma-I

Gene names

Name:

GNG2

Organism

Bos taurus (Bovine)

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	71 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. The heterodimer formed by GNB1 and GNG2 interacts with PTH1R (via C-terminus) By similarity.
Subcellular location	Cell membrane; Lipid-anchor; Cytoplasmic side Potential.
Tissue specificity	Adrenal gland and brain.
Sequence similarities	Belongs to the G protein gamma family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Molecular function	Transducer
PTM	Acetylation Lipoprotein Methylation Phosphoprotein 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 direct assay. Source: MGI
Cellular component	heterotrimeric G-protein complex Inferred from direct assay. Source: MGI
Molecular function	GTPase activity Inferred from direct assay. Source: MGI 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

1

1

Removed Ref.4 Ref.5

Chain

2 – 68

67

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2

PRO_0000012609

Propeptide

69 – 71

3

Removed in mature form

PRO_0000012610

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.4

Modified residue

52

1

Phosphothreonine By similarity

Modified residue

68

1

Cysteine methyl ester

Lipidation

68

1

S-geranylgeranyl cysteine Ref.4 Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

71

Helix Strand Turn

Details...

Helix

9 – 23

15

Helix

30 – 44

15

Helix

45 – 47

3

Turn

49 – 51

3

Turn

56 – 58

3

Sequences

	Sequence		Length	Mass (Da)
	P63212 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: EDB74E4135E7A37A	FASTA	71	7,850
	10 20 30 40 50 60 MASNNTASIA QARKLVEQLK MEANIDRIKV SKAAADLMAY CEAHAKEDPL LTPVPASENP 70 FREKKFFCAI L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Existence of two gamma subunits of the G proteins in brain." Robishaw J.D., Kalman V.K., Moomaw C.R., Slaughter C.A. J. Biol. Chem. 264:15758-15761(1989) [PubMed: 2506169] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 14-62. Tissue: Adrenal gland and Brain.
[2]	"A G protein gamma subunit shares homology with ras proteins." Gautam N., Baetscher M., Aebersold R., Simon M.I. Science 244:971-974(1989) [PubMed: 2499046] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	NIH - Mammalian Gene Collection (MGC) project Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Kidney.
[4]	"Determination of the complete covalent structure of the gamma 2 subunit of bovine brain G proteins by mass spectrometry." Wilcox M.D., Schey K.L., Busman M., Hildebrandt J.D. Biochem. Biophys. Res. Commun. 212:367-374(1995) [PubMed: 7626050] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-71, ACETYLATION AT ALA-2, ISOPRENYLATION AT CYS-68. Tissue: Brain.
[5]	"Identification of a novel gamma-subunit from bovine brain GTP binding regulatory proteins (Gi/o)." Sohma H., Hashimoto H., Hiraike N., Ohguro H., Akino T. Biochem. Biophys. Res. Commun. 190:849-856(1993) [PubMed: 8439334] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-64. Tissue: Brain.
[6]	"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: 1903391] [Abstract] Cited for: ISOPRENYLATION AT CYS-68.
[7]	"The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2." Wall M.A., Coleman D.E., Lee E., Iniguez-Lluhi J.A., Posner B.A., Gilman A.G., Sprang S.R. Cell 83:1047-1058(1995) [PubMed: 8521505] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF HETEROTRIMER.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J05071 mRNA. Translation: AAA30541.1.
M37183 mRNA. Translation: AAA30555.1.
BC112789 mRNA. Translation: AAI12790.1.

IPI

IPI00706808.

PIR

RGBOG2. B34228.

RefSeq

NP_776497.1. NM_174072.3.

UniGene

Bt.4586.
Bt.90717.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GG2	X-ray	2.40	G	1-71	[»]
1GP2	X-ray	2.30	G	1-71	[»]
1OMW	X-ray	2.50	G	1-68	[»]
1XHM	X-ray	2.70	B	1-71	[»]
2BCJ	X-ray	3.06	G	1-71	[»]
3AH8	X-ray	2.90	G	1-71	[»]
3CIK	X-ray	2.75	G	1-68	[»]
3KRW	X-ray	2.90	G	1-68	[»]
3KRX	X-ray	3.10	G	1-68	[»]
3PSC	X-ray	2.67	G	1-68	[»]
3PVU	X-ray	2.48	G	1-68	[»]
3PVW	X-ray	2.49	G	1-68	[»]
3SN6	X-ray	3.20	G	1-68	[»]

ProteinModelPortal

P63212.

SMR

P63212. Positions 8-61.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-586N.

IntAct

P63212. 1 interaction.

STRING

P63212.

Proteomic databases

PRIDE

P63212.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000003959; ENSBTAP00000003959; ENSBTAG00000003043.

GeneID

281203.

KEGG

bta:281203.

Organism-specific databases

CTD

54331.

Phylogenomic databases

eggNOG

maNOG21075.

GeneTree

ENSGT00550000074352.

HOVERGEN

HBG014983.

InParanoid

P63212.

OMA

SYCEAHA.

OrthoDB

EOG47WNQC.

PhylomeDB

P63212.

Family and domain databases

InterPro

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

Gene3D

G3DSA:4.10.260.10. G-protein_gamma_dom. 1 hit.

KO

K07826.

PANTHER

PTHR13809. Gprotein-gamma. 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...

Entry information

Entry name

GBG2_BOVIN

Accession

Primary (citable) accession number: P63212
Secondary accession number(s): P16874 , Q2KI31, Q61013, Q9TS47

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program