P27600 (GNA12_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Guanine nucleotide-binding protein subunit alpha-12
Short name=G alpha-12
Short name=G-protein subunit alpha-12

Gene names

Name:	Gna12
Synonyms:	Gna-12

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	379 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
Subunit structure	G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts with UBXD5 By similarity.
Subcellular location	Membrane; Lipid-anchor.
Post-translational modification	Myristoylation of mutated N-terminus in place of original palmitoylation restores the transformation activity. Ref.3
Sequence similarities	Belongs to the G-alpha family. G(12) subfamily.

Ontologies

Keywords
Cellular component	Membrane
Ligand	GTP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Transducer
PTM	Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Rho protein signal transduction Inferred from direct assay PubMed 10037795. Source: MGI adenylate cyclase-modulating G-protein coupled receptor signaling pathway Inferred from Biological aspect of Ancestor. Source: RefGenome cell differentiation Inferred from direct assay PubMed 9305907. Source: MGI embryonic digit morphogenesis Inferred from genetic interaction PubMed 12077299. Source: MGI in utero embryonic development Inferred from genetic interaction PubMed 12077299. Source: MGI intracellular protein kinase cascade Inferred from direct assay PubMed 10037795. Source: MGI regulation of cell shape Inferred from direct assay PubMed 10037795. Source: MGI response to drug Inferred from electronic annotation. Source: Compara
Cellular_component	brush border membrane Inferred from Biological aspect of Ancestor. Source: RefGenome heterotrimeric G-protein complex Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	D5 dopamine receptor binding Inferred from Biological aspect of Ancestor. Source: RefGenome G-protein beta/gamma-subunit complex binding Inferred from Biological aspect of Ancestor. Source: RefGenome GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from sequence alignment Ref.2. Source: MGI metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW signal transducer activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 379

379

Guanine nucleotide-binding protein subunit alpha-12

PRO_0000203771

Regions

Nucleotide binding

62 – 69

8

GTP By similarity

Nucleotide binding

200 – 206

7

GTP By similarity

Nucleotide binding

225 – 229

5

GTP By similarity

Nucleotide binding

294 – 297

4

GTP By similarity

Sites

Metal binding

69

1

Magnesium By similarity

Metal binding

206

1

Magnesium By similarity

Binding site

351

1

GTP; via amide nitrogen By similarity

Amino acid modifications

Modified residue

38

1

Phosphoserine Ref.4

Lipidation

11

1

S-palmitoyl cysteine Ref.3

Experimental info

Mutagenesis

2

1

S → G: Results in myristoylation of G-2, which restores the transformation activity; when associated with S-6. Ref.3

Mutagenesis

6

1

R → S: Results in myristoylation of G-2, which restores the transformation activity; when associated with G-2. Ref.3

Mutagenesis

11

1

C → S: Abolishes palmitoylation and transformation activity. Ref.3

Secondary structure

1

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379

Helix Strand Turn

Details...

Beta strand

56 – 67

12

Helix

68 – 79

12

Helix

85 – 112

28

Helix

120 – 122

3

Helix

123 – 130

8

Helix

142 – 157

16

Helix

159 – 166

8

Helix

168 – 170

3

Helix

176 – 182

7

Helix

184 – 187

4

Helix

196 – 201

6

Beta strand

208 – 216

9

Beta strand

219 – 226

8

Helix

230 – 233

4

Helix

234 – 238

5

Turn

239 – 242

4

Beta strand

244 – 251

8

Beta strand

260 – 266

7

Helix

267 – 279

13

Helix

282 – 284

3

Beta strand

287 – 294

8

Helix

296 – 305

10

Turn

309 – 311

3

Helix

322 – 335

14

Beta strand

346 – 348

3

Helix

354 – 370

17

Sequences

	Sequence		Length	Mass (Da)
	P27600 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 647C524AD7A0B5E2	FASTA	379	44,095
	10 20 30 40 50 60 MSGVVRTLSR CLLPAEAGAR ERRAGAARDA EREARRRSRD IDALLARERR AVRRLVKILL 70 80 90 100 110 120 LGAGESGKST FLKQMRIIHG REFDQKALLE FRDTIFDNIL KGSRVLVDAR DKLGIPWQHS 130 140 150 160 170 180 ENEKHGMFLM AFENKAGLPV EPATFQLYVP ALSALWRDSG IREAFSRRSE FQLGESVKYF 190 200 210 220 230 240 LDNLDRIGQL NYFPSKQDIL LARKATKGIV EHDFVIKKIP FKMVDVGGQR SQRQKWFQCF 250 260 270 280 290 300 DGITSILFMV SSSEYDQVLM EDRRTNRLVE SMNIFETIVN NKLFFNVSII LFLNKMDLLV 310 320 330 340 350 360 EKVKSVSIKK HFPDFKGDPH RLEDVQRYLV QCFDRKRRNR SKPLFHHFTT AIDTENIRFV 370 FHAVKDTILQ ENLKDIMLQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"G alpha 12 and G alpha 13 subunits define a fourth class of G protein alpha subunits." Strathmann M.P., Simon M.I. Proc. Natl. Acad. Sci. U.S.A. 88:5582-5586(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Diversity of the G-protein family: sequences from five additional alpha subunits in the mouse." Strathmann M., Wilkie T.M., Simon M.I. Proc. Natl. Acad. Sci. U.S.A. 86:7407-7409(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 232-292.
[3]	"Galpha12 requires acylation for its transforming activity." Jones T.L., Gutkind J.S. Biochemistry 37:3196-3202(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PALMITOYLATION AT CYS-11, MUTAGENESIS OF SER-2; ARG-6 AND CYS-11.
[4]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M63659 mRNA. Translation: AAA37648.1.
M57618 mRNA. Translation: AAA63302.1.

IPI

IPI00230191.

PIR

A41095.
C33833.

RefSeq

NP_034432.1. NM_010302.2.

UniGene

Mm.370185.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZCA	X-ray	2.90	A/B	48-379	[»]

ProteinModelPortal

P27600.

SMR

P27600. Positions 54-371.

ModBase

Search...

Protein-protein interaction databases

STRING

10090.ENSMUSP00000000153.

PTM databases

PhosphoSite

P27600.

Proteomic databases

PaxDb

P27600.

PRIDE

P27600.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000000153; ENSMUSP00000000153; ENSMUSG00000000149.

GeneID

14673.

KEGG

mmu:14673.

UCSC

uc009aih.1. mouse.

Organism-specific databases

CTD

2768.

MGI

MGI:95767. Gna12.

Phylogenomic databases

eggNOG

NOG279688.

GeneTree

ENSGT00690000101672.

HOGENOM

HOG000038729.

HOVERGEN

HBG063184.

InParanoid

P27600.

KO

K04346.

OMA

RDTIYEN.

OrthoDB

EOG4XPQG7.

Gene expression databases

ArrayExpress

P27600.

Bgee

P27600.

CleanEx

MM_GNA12.

Genevestigator

P27600.

GermOnline

ENSMUSG00000000149. Mus musculus.

Family and domain databases

Gene3D

1.10.400.10. 1 hit.

InterPro

IPR000469. Gprotein_alpha_12.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
[Graphical view]

PANTHER

PTHR10218. PTHR10218. 1 hit.

Pfam

PF00503. G-alpha. 1 hit.
[Graphical view]

PRINTS

PR00318. GPROTEINA.
PR00440. GPROTEINA12.

SMART

SM00275. G_alpha. 1 hit.
[Graphical view]

SUPFAM

SSF47895. Transducn_insert. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P27600.

NextBio

286558.

SOURCE

Search...

Entry information

Entry name

GNA12_MOUSE

Accession

Primary (citable) accession number: P27600

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 122 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program