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P27600 (GNA12_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length379 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. May play a role in the control of cell migration through the TOR signaling cascade. Ref.4

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. Interacts (when active) with PPP5C (via TPR repeats); activates PPP5C phosphatase activity and translocates PPP5C to the cell membrane By similarity. Interacts with RGS22 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 componentMembrane
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionTransducer
   PTMLipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from sequence alignment Ref.2. Source: MGI

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 signal transduction

Inferred from direct assay PubMed 10037795. Source: MGI

regulation of TOR signaling

Inferred from mutant phenotype Ref.4. Source: UniProtKB

regulation of cell shape

Inferred from direct assay PubMed 10037795. Source: MGI

regulation of fibroblast migration

Inferred from mutant phenotype Ref.4. Source: UniProtKB

regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.4. Source: UniProtKB

response to drug

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentbrush border membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

extrinsic component of cytoplasmic side of plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

heterotrimeric G-protein complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionD5 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 379379Guanine nucleotide-binding protein subunit alpha-12
PRO_0000203771

Regions

Nucleotide binding62 – 698GTP By similarity
Nucleotide binding200 – 2067GTP By similarity
Nucleotide binding225 – 2295GTP By similarity
Nucleotide binding294 – 2974GTP By similarity

Sites

Metal binding691Magnesium By similarity
Metal binding2061Magnesium By similarity
Binding site3511GTP; via amide nitrogen By similarity

Amino acid modifications

Lipidation111S-palmitoyl cysteine Ref.3

Experimental info

Mutagenesis21S → G: Results in myristoylation of G-2, which restores the transformation activity; when associated with S-6. Ref.3
Mutagenesis61R → S: Results in myristoylation of G-2, which restores the transformation activity; when associated with G-2. Ref.3
Mutagenesis111C → S: Abolishes palmitoylation and transformation activity. Ref.3

Secondary structure

................................................ 379
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27600 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 647C524AD7A0B5E2

FASTA37944,095
        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 

« Hide

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]"PRR5L degradation promotes mTORC2-mediated PKC-delta phosphorylation and cell migration downstream of Galpha12."
Gan X., Wang J., Wang C., Sommer E., Kozasa T., Srinivasula S., Alessi D., Offermanns S., Simon M.I., Wu D.
Nat. Cell Biol. 14:686-696(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TOR SIGNALING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M63659 mRNA. Translation: AAA37648.1.
M57618 mRNA. Translation: AAA63302.1.
CCDSCCDS19825.1.
PIRA41095.
C33833.
RefSeqNP_034432.1. NM_010302.2.
UniGeneMm.370185.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZCAX-ray2.90A/B48-379[»]
ProteinModelPortalP27600.
SMRP27600. Positions 54-371.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP27600. 2 interactions.
MINTMINT-4096224.
STRING10090.ENSMUSP00000000153.

PTM databases

PhosphoSiteP27600.

Proteomic databases

PaxDbP27600.
PRIDEP27600.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000000153; ENSMUSP00000000153; ENSMUSG00000000149.
GeneID14673.
KEGGmmu:14673.
UCSCuc009aih.1. mouse.

Organism-specific databases

CTD2768.
MGIMGI:95767. Gna12.

Phylogenomic databases

eggNOGNOG279688.
GeneTreeENSGT00690000101672.
HOGENOMHOG000038729.
HOVERGENHBG063184.
InParanoidP27600.
KOK04346.
OMAWQHSENE.
OrthoDBEOG7HF1JF.
PhylomeDBP27600.
TreeFamTF300673.

Gene expression databases

ArrayExpressP27600.
BgeeP27600.
CleanExMM_GNA12.
GenevestigatorP27600.

Family and domain databases

Gene3D1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR000469. Gprotein_alpha_12.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR10218. PTHR10218. 1 hit.
PfamPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSPR00318. GPROTEINA.
PR00440. GPROTEINA12.
SMARTSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNetSearch...

Other

EvolutionaryTraceP27600.
NextBio286558.
PROP27600.
SOURCESearch...

Entry information

Entry nameGNA12_MOUSE
AccessionPrimary (citable) accession number: P27600
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot