RGS12_RAT
ID RGS12_RAT Reviewed; 1387 AA.
AC O08774; O88383;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Regulator of G-protein signaling 12;
DE Short=RGS12;
GN Name=Rgs12;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9168931; DOI=10.1006/bbrc.1997.6537;
RA Snow B.E., Antonio L., Suggs S., Gutstein H.B., Siderovski D.P.;
RT "Molecular cloning and expression analysis of rat Rgs12 and Rgs14.";
RL Biochem. Biophys. Res. Commun. 233:770-777(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=9651375; DOI=10.1074/jbc.273.28.17749;
RA Snow B.E., Hall R.A., Krumins A.M., Brothers G.M., Bouchard D.,
RA Brothers C.A., Chung S., Mangion J., Gilman A.G., Lefkowitz R.J.,
RA Siderovski D.P.;
RT "GTPase activating specificity of RGS12 and binding specificity of an
RT alternatively spliced PDZ (PSD-95/Dlg/ZO-1) domain.";
RL J. Biol. Chem. 273:17749-17755(1998).
RN [3]
RP FUNCTION, AND INTERACTION WITH GNAI1; GNAI2 AND GNAI3.
RX PubMed=11387333; DOI=10.1074/jbc.m103208200;
RA Kimple R.J., De Vries L., Tronchere H., Behe C.I., Morris R.A.,
RA Gist Farquhar M., Siderovski D.P.;
RT "RGS12 and RGS14 GoLoco motifs are G alpha(i) interaction sites with
RT guanine nucleotide dissociation inhibitor activity.";
RL J. Biol. Chem. 276:29275-29281(2001).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16819986; DOI=10.1111/j.1460-9568.2006.04838.x;
RA Lopez-Aranda M.F., Acevedo M.J., Carballo F.J., Gutierrez A., Khan Z.U.;
RT "Localization of the GoLoco motif carrier regulator of G-protein signalling
RT 12 and 14 proteins in monkey and rat brain.";
RL Eur. J. Neurosci. 23:2971-2982(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171; SER-661; SER-671 AND
RP SER-879, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:0000269|PubMed:11387333, ECO:0000269|PubMed:9651375}.
CC -!- SUBUNIT: Interacts with GNAI1, GNAI2 and GNAI3; the interactions are
CC GDP-dependent. {ECO:0000269|PubMed:11387333}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16819986}. Cytoplasm
CC {ECO:0000269|PubMed:16819986}. Cell projection, dendrite
CC {ECO:0000269|PubMed:16819986}. Synapse {ECO:0000269|PubMed:16819986}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=O08774-1; Sequence=Displayed;
CC Name=2; Synonyms=PDZ-less;
CC IsoId=O08774-2; Sequence=VSP_005688, VSP_005689;
CC -!- TISSUE SPECIFICITY: Detected in brain cortex GABAergic neurons, in
CC striatum and substantia nigra, and in the Purkinje cell layer in the
CC cerebellum and hippocampus (at protein level) (PubMed:16819986).
CC Expressed at high levels in brain and lung and lower levels in testis,
CC heart, and spleen (PubMed:9168931). {ECO:0000269|PubMed:16819986,
CC ECO:0000269|PubMed:9168931}.
CC -!- DOMAIN: The GoLoco domain is necessary for interaction with GNAI1,
CC GNAI2 and GNAI3.
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DR EMBL; U92280; AAC53176.1; -; mRNA.
DR EMBL; AF035151; AAC40154.1; -; mRNA.
DR PIR; JC5502; JC5502.
DR RefSeq; NP_062212.1; NM_019339.1. [O08774-1]
DR AlphaFoldDB; O08774; -.
DR SMR; O08774; -.
DR BioGRID; 248512; 10.
DR IntAct; O08774; 3.
DR MINT; O08774; -.
DR STRING; 10116.ENSRNOP00000045065; -.
DR iPTMnet; O08774; -.
DR PhosphoSitePlus; O08774; -.
DR PaxDb; O08774; -.
DR PRIDE; O08774; -.
DR GeneID; 54292; -.
DR KEGG; rno:54292; -.
DR CTD; 6002; -.
DR RGD; 3564; Rgs12.
DR eggNOG; KOG3589; Eukaryota.
DR InParanoid; O08774; -.
DR PhylomeDB; O08774; -.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:O08774; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097440; C:apical dendrite; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:RGD.
DR GO; GO:0005096; F:GTPase activator activity; IDA:RGD.
DR GO; GO:0030695; F:GTPase regulator activity; ISO:RGD.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; IEP:RGD.
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; IDA:RGD.
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 Alternative splicing; Cell projection; Cytoplasm; GTPase activation;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Signal transduction inhibitor; Synapse; Ubl conjugation.
FT CHAIN 1..1387
FT /note="Regulator of G-protein signaling 12"
FT /id="PRO_0000204214"
FT DOMAIN 21..97
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 227..339
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..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1224..1325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1349..1387
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 447..473
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..1153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1364..1378
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGE9"
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:0000250|UniProtKB:Q8CGE9"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 850
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGE9"
FT MOD_RES 879
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 943
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGE9"
FT CROSSLNK 195
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O14924"
FT VAR_SEQ 1..648
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005688"
FT VAR_SEQ 649..666
FT /note="SFGRSRRFSLTRSLDDLE -> MNLEKGLSDDSDVFIDQQ (in isoform
FT 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005689"
SQ SEQUENCE 1387 AA; 150469 MW; 958047D106B08310 CRC64;
MYRAGEPGKR QSGPAPPRVR SVEVARGRAG YGFTLSGQAP CVLSCVMRGS PADFVGLRAG
DQILAINEIN VKKASHEDVV KLIGKCSGVL RMVISEGSSH VEPSSSDEEG GLCEGKGWLR
PKLDSKALGI NRAERVVEEV QSGGIFNMIF ESPSLCASGS EPLKLKQRSL SESAALRLDV
GQDSLCTPHP SMLSKEEISK VINDDSVFTV GLDNHDDFGL DASILNVAMV VGYLGSIELP
STSSNLEHDS LQAIRGCMRR LRAEQKIHSL VTMKVMHDCV QLVTDRAGVV AEYPAEKLAF
SAVCPDDRRF FGLVTMQTND DGCLAQEDEG ALRTSCHVFM VDPDLFHHKI HQGIARRFGF
ACTADPDTSG CLEFPASSLP VLQFISVLYR DMGELIEGVR ARAFLDGDAD AHQNNSTSSN
SDSGIGNFNQ EEKSNRVLVV DLGGGSSRHG QGSSPGWESV SGRGSQPWSA PWNGTFCHDS
EAGSPLETSP NTDRFWDLTK HSGPVFHMEV PPATLRSSIP PSKRGATGSS CGFNQRWLPV
HVLQEWQCGH ASDQESYTDS TDGWSSVNCG TLPPPMSKIP ADRYRVEGSF AQAPLSTQKR
DWSRKAFGMQ NLFGPHRNVR KTKEDKKSSK LGRGVALAQT SQRTSARRSF GRSRRFSLTR
SLDDLESATV SDGELTGADL KDCISNNSLS SNASLPSVQS CRRLRERRVA SWAVSFERLL
QDPVGVRYFS DFLRKEFSEE NILFWQACEC FSHVPAHDKK ELSYRAREIF SKFLCSKATT
PVNIDSQAQL ADDILNAPHP DMFKEQQLQI FNLMKFDSYT RFLKSQLYQE CVLAEVEGRT
LPDSQQVPSS PASKHSISSD HSNVSTPKKL SGKSKSGRSL NEDVGEEDSE KKRKGAFFSW
SRSRSTGRSQ KKKDHGDHAH DALHANGGLC RRESQGSVSS AGSLDLSEAC RTSALERDKA
AKHCCVHLPD GTSCVVAVKS GFSIKEILSG LCERHGINGA AVDLFLVGGD KPLVLHQDSS
ILATRDLRLG KRTLFRLDLV PINRSVGLKA KPTKPVTEVL RPVVAKYGLD LGSLLVRLSG
EKEPLDLGAP ISSLDGQRVI LEERDPSRGK VSTEKQKGAP VKQSSAVNSS PRNHSAMGEE
RTLGKSNSIK IRGENGKSAR DPRLSKREES IAKIGKKKYQ KINLDEAEEF FELISKAQSN
RADDQRGLLR KEDLVLPEFL RLPPGSSELA LSSPPPVKGF SKRAVTSHGQ EGAVQTEESY
SDSPATSPAS AQSPCSAYSP GSAHSPGSAH SPGSAHSTPG PPGTAQPGEK PTKPSCISTV
QEGTTQAWRR LSPELEAGGI QTVEEEQVAD LTLMGEGDIS SPNSTLLPPP PLPQDTPGPT
RPGTSRF
