RGS12_MOUSE
ID RGS12_MOUSE Reviewed; 1381 AA.
AC Q8CGE9; E9PXX2;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Regulator of G-protein signaling 12;
DE Short=RGS12;
GN Name=Rgs12;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=15525537; DOI=10.1016/j.devcel.2004.10.004;
RA Martin-McCaffrey L., Willard F.S., Oliveira-dos-Santos A.J., Natale D.R.,
RA Snow B.E., Kimple R.J., Pajak A., Watson A.J., Dagnino L., Penninger J.M.,
RA Siderovski D.P., D'Souza S.J.;
RT "RGS14 is a mitotic spindle protein essential from the first division of
RT the mammalian zygote.";
RL Dev. Cell 7:763-769(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171; SER-194; SER-661;
RP SER-671; SER-850; SER-879 AND SER-943, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-633, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Regulates G protein-coupled receptor signaling cascades.
CC Inhibits signal transduction by increasing the GTPase activity of G
CC protein alpha subunits, thereby driving them into their inactive GDP-
CC bound form. {ECO:0000250|UniProtKB:O08774}.
CC -!- SUBUNIT: Interacts with GNAI1, GNAI2 and GNAI3; the interactions are
CC GDP-dependent. {ECO:0000250|UniProtKB:O08774}.
CC -!- INTERACTION:
CC Q8CGE9; Q63932: Map2k2; NbExp=3; IntAct=EBI-7340552, EBI-397724;
CC Q8CGE9; P15056: BRAF; Xeno; NbExp=2; IntAct=EBI-7340552, EBI-365980;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O08774}. Cytoplasm
CC {ECO:0000250|UniProtKB:O08774}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:O08774}. Synapse {ECO:0000250|UniProtKB:O08774}.
CC -!- TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:15525537}.
CC -!- DEVELOPMENTAL STAGE: Expressed in germinal vesicle oocyte, metaphase II
CC oocyte and blastocyst (at protein level). Expressed in oocyte.
CC {ECO:0000269|PubMed:15525537}.
CC -!- DOMAIN: The GoLoco domain is necessary for interaction with GNAI1,
CC GNAI2 and GNAI3. {ECO:0000250}.
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DR EMBL; AC126447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC133204; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040396; AAH40396.1; -; mRNA.
DR CCDS; CCDS19222.1; -.
DR RefSeq; NP_775578.2; NM_173402.2.
DR AlphaFoldDB; Q8CGE9; -.
DR SMR; Q8CGE9; -.
DR BioGRID; 214886; 2.
DR IntAct; Q8CGE9; 6.
DR MINT; Q8CGE9; -.
DR STRING; 10090.ENSMUSP00000030984; -.
DR iPTMnet; Q8CGE9; -.
DR PhosphoSitePlus; Q8CGE9; -.
DR EPD; Q8CGE9; -.
DR jPOST; Q8CGE9; -.
DR MaxQB; Q8CGE9; -.
DR PaxDb; Q8CGE9; -.
DR PRIDE; Q8CGE9; -.
DR ProteomicsDB; 253261; -.
DR Antibodypedia; 22482; 98 antibodies from 21 providers.
DR DNASU; 71729; -.
DR Ensembl; ENSMUST00000030984; ENSMUSP00000030984; ENSMUSG00000029101.
DR GeneID; 71729; -.
DR KEGG; mmu:71729; -.
DR UCSC; uc008xdg.2; mouse.
DR CTD; 6002; -.
DR MGI; MGI:1918979; Rgs12.
DR VEuPathDB; HostDB:ENSMUSG00000029101; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000159741; -.
DR HOGENOM; CLU_002190_0_0_1; -.
DR InParanoid; Q8CGE9; -.
DR OMA; HKSEWSK; -.
DR TreeFam; TF328814; -.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 71729; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Rgs12; mouse.
DR PRO; PR:Q8CGE9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8CGE9; protein.
DR Bgee; ENSMUSG00000029101; Expressed in spermatocyte and 200 other tissues.
DR ExpressionAtlas; Q8CGE9; baseline and differential.
DR Genevisible; Q8CGE9; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097440; C:apical dendrite; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0030695; F:GTPase regulator activity; ISO:MGI.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0038032; P:termination of G protein-coupled receptor signaling pathway; ISO:MGI.
DR CDD; cd08742; RGS_RGS12; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.10.196.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR003109; GoLoco_motif.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR003116; RBD_dom.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR037880; RGS12_RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR024066; RGS_subdom1/3.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF02188; GoLoco; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF02196; RBD; 2.
DR Pfam; PF00615; RGS; 1.
DR PRINTS; PR01301; RGSPROTEIN.
DR SMART; SM00390; GoLoco; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00455; RBD; 2.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF54236; SSF54236; 2.
DR PROSITE; PS50877; GOLOCO; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50898; RBD; 2.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasm; GTPase activation; Isopeptide bond;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat; Synapse;
KW Ubl conjugation.
FT CHAIN 1..1381
FT /note="Regulator of G-protein signaling 12"
FT /id="PRO_0000408474"
FT DOMAIN 21..98
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 223..390
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 715..832
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 962..1032
FT /note="RBD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00262"
FT DOMAIN 1034..1104
FT /note="RBD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00262"
FT DOMAIN 1187..1209
FT /note="GoLoco"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT REGION 409..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1102..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1227..1318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1347..1381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..897
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..927
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1252..1318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1374
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 524
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O14924"
FT MOD_RES 633
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 850
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 879
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 943
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 195
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O14924"
FT CONFLICT 536
FT /note="R -> K (in Ref. 2; AAH40396)"
FT /evidence="ECO:0000305"
FT CONFLICT 1135
FT /note="L -> S (in Ref. 2; AAH40396)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1381 AA; 149637 MW; 8897CD1D249B66C6 CRC64;
MYRAGEPGKR QPGPAPPRVR SVEVARGRAG YGFTLSGQAP CVLSCVMRGS PADFVGLRAG
DQILAINEIN VKKASHEDVV KLIGKCSGVL HMVIAEGTSH VESCSSDEEG GLYEGKGWLR
PKLDSKALGI NRAERVVEEV QSGGIFNMIF ESSSLCASGP EPLKLKQRSL SESAALRLDA
GQAGLCAPHP SMLSKEDISK VINDDSVFTV GLDSHDDFGL DASILNVAMV VGYLGSIELP
STSSNLEHDS LQAIRGCMRR LRAEQKIHSL VTMKVMHDCV QLVTDRAGVV AEYPAEKLAF
SAVCPDDRRF FGLVTMQTND DGGLAQEDEG ALRTSCHVFM VDPDLFHHKI HQGIARRFGF
ACTADPDTSG CLEFPASSLP VLQFISVLYR DMGELIEGVR ARAFLDGDAD AHQNNSTSSN
SDSGIGNFNQ EEKSNRVLVV DLGGGSSRHG QGSSPGWESG GGRGSQPWSA PWNGAFCHDS
EAGSPLETSP NTDRFWDLTK HSGPVSHMEV PPATLRSSIP PSKRGAAGSS CGFNQRWLPV
HVLQEWQCGH ASDQESYTDS TDGWSSVNCG TLPPPMSKIP ADRYRVEGSF AQAPLSTQKR
DWSRKAFGMQ NLFGPHRNVR KTKEDKKSSK LGRGVALAQT SQRTSARRSF GRSRRFSITR
SLDDLESATV SDGELTGADL KDCISNNSLS SNASLPSVQS CRRLRERRVA SWAVSFERLL
QDPVGVRYFS DFLRKEFSEE NILFWQACEC FSHVPAHDKK ELSYRAREIF SKFLCSKATT
PVNIDSQAQL ADDILNAPHP DMFKEQQLQI FNLMKFDSYT RFLKSQLYQE CVLAEVEGRT
LPDSQQVPSS PASKHSISSD HSNVSTPKKL SGKSKSGRSL NEDVGEEDSE KKRRGAFFSW
SRSRSTGRSQ KKKDHGDHAH DAPHANGGLC RRESQGSVSS AGSLDLSEAC RTSALEKDKA
AKHCCVHLPD GTSCVVAVKS GFSIKEILSG LCERHGINGA AVDLFLVGGD KPLVLHQDSS
ILATRDLRLE KRTLFRLDLV PINRSVGLKA KPTKPVTEVL RPVVAKYGLD LGSLLVRLSG
EKEPLDLGAP ISSLDGQRVI LEERDPSRGK VSTDKQKGAP VKQNSAVNSS PRNHLAMGEE
RTLGKSNSIK IRGENGKSAR DPRLSKREES IAKIGKKKYQ KINLDEAEEF FELISKAQSN
RADDQRGLLR KEDLVLPEFL RLPAGSSELA LSSPPPVKGY SKRAVTGHGQ EGAAQTEESY
SDSPATSPAS AQSPCSAYSP GSAHSPGSAH STPGPPGTTQ PGEKPTKPSC VSMVQEGTTQ
AWRRLSPEME AGGIQTVEDE QVADLTLMGE GDISSPNSTL LPPPPTPQDT PGPPRPGTSR
F
