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RGS4_MACFA
ID   RGS4_MACFA              Reviewed;         205 AA.
AC   Q4R525; Q5ISP0;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Regulator of G-protein signaling 4;
DE            Short=RGS4;
GN   Name=RGS4; ORFNames=QflA-11075;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Frontal cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 50-191.
RX   PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
RA   Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
RA   Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
RT   "Accelerated evolution of nervous system genes in the origin of Homo
RT   sapiens.";
RL   Cell 119:1027-1040(2004).
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. Activity on G(z)-alpha is inhibited by
CC       phosphorylation of the G-protein. Activity on G(z)-alpha and G(i)-
CC       alpha-1 is inhibited by palmitoylation of the G-protein (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: Palmitoylated on Cys-2 and/or Cys-12. {ECO:0000250}.
CC   -!- PTM: Phosphorylated by cyclic GMP-dependent protein kinase.
CC       {ECO:0000250}.
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DR   EMBL; AB169719; BAE01800.1; -; mRNA.
DR   EMBL; AY650340; AAV67372.1; -; mRNA.
DR   AlphaFoldDB; Q4R525; -.
DR   BMRB; Q4R525; -.
DR   SMR; Q4R525; -.
DR   STRING; 9541.XP_005539883.1; -.
DR   eggNOG; KOG3589; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd08714; RGS_RGS4; 1.
DR   Gene3D; 1.10.167.10; -; 1.
DR   Gene3D; 1.10.196.10; -; 1.
DR   InterPro; IPR016137; RGS.
DR   InterPro; IPR034952; RGS4.
DR   InterPro; IPR034953; RGS_RGS4.
DR   InterPro; IPR036305; RGS_sf.
DR   InterPro; IPR024066; RGS_subdom1/3.
DR   InterPro; IPR044926; RGS_subdomain_2.
DR   PANTHER; PTHR10845:SF184; PTHR10845:SF184; 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   2: Evidence at transcript level;
KW   Lipoprotein; Palmitate; Phosphoprotein; Reference proteome;
KW   Signal transduction inhibitor.
FT   CHAIN           1..205
FT                   /note="Regulator of G-protein signaling 4"
FT                   /id="PRO_0000261130"
FT   DOMAIN          62..178
FT                   /note="RGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT   LIPID           2
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           12
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           95
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   205 AA;  23256 MW;  7713F1F7496A698B CRC64;
     MCKGLAGLPA SCLRSAKDMK HRLGFLLQKS DSCEHNSSHN KKDKVVICQR VSQEEVKKWA
     ESLENLISHE CGLAAFKAFL KSEYSEENID FWISCEEYKK IKSPSKLSPK AKKIYNEFIS
     VQATKEVNLD SCTREETSRN MLEPTITCFD EAQKKIFNLM EKDSYRRFLK SRFYLDLVNP
     SSCGAEKQKG AKSSADCASL VPQCA
 
 
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