RGS18_RAT
ID RGS18_RAT Reviewed; 235 AA.
AC Q4L0E8;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Regulator of G-protein signaling 18;
DE Short=RGS18;
GN Name=Rgs18;
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].
RC STRAIN=Fischer 344;
RX PubMed=15946253; DOI=10.1111/j.1365-2567.2005.02174.x;
RA Kveberg L., Ryan J.C., Rolstad B., Inngjerdingen M.;
RT "Expression of regulator of G protein signalling proteins in natural killer
RT cells, and their modulation by Ly49A and Ly49D.";
RL Immunology 115:358-365(2005).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION BY
RP 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: Inhibits signal transduction by increasing the GTPase
CC activity of G protein alpha subunits thereby driving them into their
CC inactive GDP-bound form. Binds to G(i) alpha-1, G(i) alpha-2, G(i)
CC alpha-3 and G(q) alpha (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR EMBL; AY651776; AAV85503.1; -; mRNA.
DR RefSeq; NP_001040549.1; NM_001047084.1.
DR AlphaFoldDB; Q4L0E8; -.
DR SMR; Q4L0E8; -.
DR STRING; 10116.ENSRNOP00000005324; -.
DR iPTMnet; Q4L0E8; -.
DR PhosphoSitePlus; Q4L0E8; -.
DR PaxDb; Q4L0E8; -.
DR GeneID; 289076; -.
DR KEGG; rno:289076; -.
DR UCSC; RGD:1306522; rat.
DR CTD; 64407; -.
DR RGD; 1306522; Rgs18.
DR eggNOG; KOG3589; Eukaryota.
DR InParanoid; Q4L0E8; -.
DR OrthoDB; 1193829at2759; -.
DR PhylomeDB; Q4L0E8; -.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:Q4L0E8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005096; F:GTPase activator activity; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISO:RGD.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.10.196.10; -; 1.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR034950; RGS18.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR024066; RGS_subdom1/3.
DR InterPro; IPR044926; RGS_subdomain_2.
DR PANTHER; PTHR10845:SF155; PTHR10845:SF155; 1.
DR Pfam; PF00615; RGS; 1.
DR PRINTS; PR01301; RGSPROTEIN.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome;
KW Signal transduction inhibitor.
FT CHAIN 1..235
FT /note="Regulator of G-protein signaling 18"
FT /id="PRO_0000342605"
FT DOMAIN 86..202
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NS28"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99PG4"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 235 AA; 27645 MW; 12BB334292AB6D67 CRC64;
MDMSLVFFSH LNMCESKEKT FFKLMHGSGK EETNIEAKIR AKEKRNRLSL LLQRPDFHGE
THTSRSALLA KETRVSSEEA LKWAESFDKL LSHRDGVDAF TRFLKTEFSE ENIEFWVACE
DFKKCTEPQQ LILKAKSIYE KFIKNDAPKE VNLDFHTKEV ITKSIAQPTL HSFDAAQSRV
CQLMEHDSYK RFLKSEIYLH LIEGRPQRPT NLRRRSRSFT YNEFQDVKSD VAIWL