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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
 
 
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