ID   GNA12_MOUSE             Reviewed;         379 AA.
AC   P27600;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-SEP-2015, entry version 143.
DE   RecName: Full=Guanine nucleotide-binding protein subunit alpha-12;
DE            Short=G alpha-12;
DE            Short=G-protein subunit alpha-12;
GN   Name=Gna12; Synonyms=Gna-12;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=1905812; DOI=10.1073/pnas.88.13.5582;
RA   Strathmann M.P., Simon M.I.;
RT   "G alpha 12 and G alpha 13 subunits define a fourth class of G protein
RT   alpha subunits.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:5582-5586(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 232-292.
RX   PubMed=2508088; DOI=10.1073/pnas.86.19.7407;
RA   Strathmann M., Wilkie T.M., Simon M.I.;
RT   "Diversity of the G-protein family: sequences from five additional
RT   alpha subunits in the mouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:7407-7409(1989).
RN   [3]
RP   PALMITOYLATION AT CYS-11, AND MUTAGENESIS OF SER-2; ARG-6 AND CYS-11.
RX   PubMed=9485474; DOI=10.1021/bi972253j;
RA   Jones T.L., Gutkind J.S.;
RT   "Galpha12 requires acylation for its transforming activity.";
RL   Biochemistry 37:3196-3202(1998).
RN   [4]
RP   FUNCTION IN TOR SIGNALING.
RX   PubMed=22609986; DOI=10.1038/ncb2507;
RA   Gan X., Wang J., Wang C., Sommer E., Kozasa T., Srinivasula S.,
RA   Alessi D., Offermanns S., Simon M.I., Wu D.;
RT   "PRR5L degradation promotes mTORC2-mediated PKC-delta phosphorylation
RT   and cell migration downstream of Galpha12.";
RL   Nat. Cell Biol. 14:686-696(2012).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC       involved as modulators or transducers in various transmembrane
CC       signaling systems. May play a role in the control of cell
CC       migration through the TOR signaling cascade.
CC       {ECO:0000269|PubMed:22609986}.
CC   -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and
CC       gamma. The alpha chain contains the guanine nucleotide binding
CC       site. Interacts with UBXD5. Interacts (when active) with PPP5C
CC       (via TPR repeats); activates PPP5C phosphatase activity and
CC       translocates PPP5C to the cell membrane (By similarity). Interacts
CC       with RGS22 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
CC   -!- PTM: Myristoylation of mutated N-terminus in place of original
CC       palmitoylation restores the transformation activity.
CC       {ECO:0000269|PubMed:9485474}.
CC   -!- SIMILARITY: Belongs to the G-alpha family. G(12) subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M63659; AAA37648.1; -; mRNA.
DR   EMBL; M57618; AAA63302.1; -; mRNA.
DR   CCDS; CCDS19825.1; -.
DR   PIR; A41095; A41095.
DR   PIR; C33833; C33833.
DR   RefSeq; NP_034432.1; NM_010302.2.
DR   UniGene; Mm.370185; -.
DR   PDB; 1ZCA; X-ray; 2.90 A; A/B=48-379.
DR   PDBsum; 1ZCA; -.
DR   ProteinModelPortal; P27600; -.
DR   SMR; P27600; 54-371.
DR   IntAct; P27600; 3.
DR   MINT; MINT-4096224; -.
DR   STRING; 10090.ENSMUSP00000000153; -.
DR   PhosphoSite; P27600; -.
DR   MaxQB; P27600; -.
DR   PaxDb; P27600; -.
DR   PRIDE; P27600; -.
DR   Ensembl; ENSMUST00000000153; ENSMUSP00000000153; ENSMUSG00000000149.
DR   GeneID; 14673; -.
DR   KEGG; mmu:14673; -.
DR   UCSC; uc009aih.1; mouse.
DR   CTD; 2768; -.
DR   MGI; MGI:95767; Gna12.
DR   eggNOG; NOG279688; -.
DR   GeneTree; ENSGT00770000120503; -.
DR   HOGENOM; HOG000038729; -.
DR   HOVERGEN; HBG063184; -.
DR   InParanoid; P27600; -.
DR   KO; K04346; -.
DR   OMA; GISEHIF; -.
DR   OrthoDB; EOG7HF1JF; -.
DR   PhylomeDB; P27600; -.
DR   TreeFam; TF300673; -.
DR   Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR   Reactome; R-MMU-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR   EvolutionaryTrace; P27600; -.
DR   NextBio; 286558; -.
DR   PRO; PR:P27600; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   Bgee; P27600; -.
DR   CleanEx; MM_GNA12; -.
DR   Genevisible; P27600; MM.
DR   GO; GO:0031526; C:brush border membrane; IBA:GO_Central.
DR   GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; TAS:MGI.
DR   GO; GO:0031752; F:D5 dopamine receptor binding; IBA:GO_Central.
DR   GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; ISA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004871; F:signal transducer activity; IBA:GO_Central.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IDA:MGI.
DR   GO; GO:0042733; P:embryonic digit morphogenesis; IGI:MGI.
DR   GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISA:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR   GO; GO:0035556; P:intracellular signal transduction; IDA:MGI.
DR   GO; GO:0008360; P:regulation of cell shape; IDA:MGI.
DR   GO; GO:0010762; P:regulation of fibroblast migration; IMP:UniProtKB.
DR   GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR   GO; GO:0032006; P:regulation of TOR signaling; IMP:UniProtKB.
DR   GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR   GO; GO:0007266; P:Rho protein signal transduction; IDA:MGI.
DR   Gene3D; 1.10.400.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR000469; Gprotein_alpha_12.
DR   InterPro; IPR001019; Gprotein_alpha_su.
DR   InterPro; IPR011025; GproteinA_insert.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10218; PTHR10218; 1.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR00440; GPROTEINA12.
DR   SMART; SM00275; G_alpha; 1.
DR   SUPFAM; SSF47895; SSF47895; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; GTP-binding; Lipoprotein; Magnesium;
KW   Membrane; Metal-binding; Nucleotide-binding; Palmitate;
KW   Reference proteome; Transducer.
FT   CHAIN         1    379       Guanine nucleotide-binding protein
FT                                subunit alpha-12.
FT                                /FTId=PRO_0000203771.
FT   NP_BIND      62     69       GTP. {ECO:0000250}.
FT   NP_BIND     200    206       GTP. {ECO:0000250}.
FT   NP_BIND     225    229       GTP. {ECO:0000250}.
FT   NP_BIND     294    297       GTP. {ECO:0000250}.
FT   METAL        69     69       Magnesium. {ECO:0000250}.
FT   METAL       206    206       Magnesium. {ECO:0000250}.
FT   BINDING     351    351       GTP; via amide nitrogen. {ECO:0000250}.
FT   LIPID        11     11       S-palmitoyl cysteine.
FT                                {ECO:0000269|PubMed:9485474}.
FT   MUTAGEN       2      2       S->G: Results in myristoylation of G-2,
FT                                which restores the transformation
FT                                activity; when associated with S-6.
FT                                {ECO:0000269|PubMed:9485474}.
FT   MUTAGEN       6      6       R->S: Results in myristoylation of G-2,
FT                                which restores the transformation
FT                                activity; when associated with G-2.
FT                                {ECO:0000269|PubMed:9485474}.
FT   MUTAGEN      11     11       C->S: Abolishes palmitoylation and
FT                                transformation activity.
FT                                {ECO:0000269|PubMed:9485474}.
FT   STRAND       56     67       {ECO:0000244|PDB:1ZCA}.
FT   HELIX        68     79       {ECO:0000244|PDB:1ZCA}.
FT   HELIX        85    112       {ECO:0000244|PDB:1ZCA}.
FT   HELIX       120    122       {ECO:0000244|PDB:1ZCA}.
FT   HELIX       123    130       {ECO:0000244|PDB:1ZCA}.
FT   HELIX       142    157       {ECO:0000244|PDB:1ZCA}.
FT   HELIX       159    166       {ECO:0000244|PDB:1ZCA}.
FT   HELIX       168    170       {ECO:0000244|PDB:1ZCA}.
FT   HELIX       176    182       {ECO:0000244|PDB:1ZCA}.
FT   HELIX       184    187       {ECO:0000244|PDB:1ZCA}.
FT   HELIX       196    201       {ECO:0000244|PDB:1ZCA}.
FT   STRAND      208    216       {ECO:0000244|PDB:1ZCA}.
FT   STRAND      219    226       {ECO:0000244|PDB:1ZCA}.
FT   HELIX       230    233       {ECO:0000244|PDB:1ZCA}.
FT   HELIX       234    238       {ECO:0000244|PDB:1ZCA}.
FT   TURN        239    242       {ECO:0000244|PDB:1ZCA}.
FT   STRAND      244    251       {ECO:0000244|PDB:1ZCA}.
FT   STRAND      260    266       {ECO:0000244|PDB:1ZCA}.
FT   HELIX       267    279       {ECO:0000244|PDB:1ZCA}.
FT   HELIX       282    284       {ECO:0000244|PDB:1ZCA}.
FT   STRAND      287    294       {ECO:0000244|PDB:1ZCA}.
FT   HELIX       296    305       {ECO:0000244|PDB:1ZCA}.
FT   TURN        309    311       {ECO:0000244|PDB:1ZCA}.
FT   HELIX       322    335       {ECO:0000244|PDB:1ZCA}.
FT   STRAND      346    348       {ECO:0000244|PDB:1ZCA}.
FT   HELIX       354    370       {ECO:0000244|PDB:1ZCA}.
SQ   SEQUENCE   379 AA;  44095 MW;  647C524AD7A0B5E2 CRC64;
     MSGVVRTLSR CLLPAEAGAR ERRAGAARDA EREARRRSRD IDALLARERR AVRRLVKILL
     LGAGESGKST FLKQMRIIHG REFDQKALLE FRDTIFDNIL KGSRVLVDAR DKLGIPWQHS
     ENEKHGMFLM AFENKAGLPV EPATFQLYVP ALSALWRDSG IREAFSRRSE FQLGESVKYF
     LDNLDRIGQL NYFPSKQDIL LARKATKGIV EHDFVIKKIP FKMVDVGGQR SQRQKWFQCF
     DGITSILFMV SSSEYDQVLM EDRRTNRLVE SMNIFETIVN NKLFFNVSII LFLNKMDLLV
     EKVKSVSIKK HFPDFKGDPH RLEDVQRYLV QCFDRKRRNR SKPLFHHFTT AIDTENIRFV
     FHAVKDTILQ ENLKDIMLQ
//