ID   RGS4_PONAB              Reviewed;         205 AA.
AC   Q5R747; Q5RBG8;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Regulator of G-protein signaling 4;
DE            Short=RGS4;
GN   Name=RGS4;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR858680; CAH90892.1; -; mRNA.
DR   EMBL; CR860271; CAH92413.1; -; mRNA.
DR   RefSeq; NP_001125509.1; NM_001132037.1.
DR   AlphaFoldDB; Q5R747; -.
DR   BMRB; Q5R747; -.
DR   SMR; Q5R747; -.
DR   STRING; 9601.ENSPPYP00000000674; -.
DR   GeneID; 100172418; -.
DR   KEGG; pon:100172418; -.
DR   CTD; 5999; -.
DR   eggNOG; KOG3589; Eukaryota.
DR   HOGENOM; CLU_059863_3_0_1; -.
DR   InParanoid; Q5R747; -.
DR   Proteomes; UP000001595; 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_0000261131"
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"
FT   CONFLICT        87
FT                   /note="E -> G (in Ref. 1; CAH90892)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   205 AA;  23256 MW;  D49C4F9C8C7C81ED CRC64;
     MCKGLAGLPA SCLRSAKDMK HRLGFLLQKS DSCEHNSSHN KKDKVIICQR VSQEEVKKWA
     ESLENLISHE CGLAAFKAFL KSEYSEENID FWISCEEYKK IKSPSKLSPK AKKIYNEFIS
     VQASKEVNLD SCTREETSRN MLEPTITCFD EAQKKIFNLM EKDSYRRFLK SRFYLDLVNP
     SSCGAEKQKG AKSSADCASL VPQCA