(data stored in ACNUC17492 zone)

SWISSPROT: RGS2_PIG

ID   RGS2_PIG                Reviewed;         212 AA.
AC   Q3S853; Q2V8V0;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   08-MAY-2019, entry version 89.
DE   RecName: Full=Regulator of G-protein signaling 2;
DE            Short=RGS2;
GN   Name=RGS2;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Yao W., Yang Z.;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Yao W.;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulates G protein-coupled receptor signaling cascades.
CC       Inhibits signal transduction by increasing the GTPase activity of
CC       G protein alpha subunits, thereby driving them into their inactive
CC       GDP-bound form (By similarity). It is involved in the negative
CC       regulation of the angiotensin-activated signaling pathway (By
CC       similarity). Plays a role in the regulation of blood pressure in
CC       response to signaling via G protein-coupled receptors and GNAQ.
CC       Plays a role in regulating the constriction and relaxation of
CC       vascular smooth muscle (By similarity). Binds EIF2B5 and blocks
CC       its activity, thereby inhibiting the translation of mRNA into
CC       protein (By similarity). {ECO:0000250|UniProtKB:O08849,
CC       ECO:0000250|UniProtKB:P41220}.
CC   -!- SUBUNIT: Interacts with GNAQ. Does not interact with GNAI1 and
CC       GNAI3. Interacts with EIF2B5. Interacts with PRKG1 (isoform
CC       alpha). {ECO:0000250|UniProtKB:P41220}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:P41220}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P41220}. Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:P41220}.
CC   -!- PTM: Phosphorylated by protein kinase C. Phosphorylation by PRKG1
CC       leads to activation of RGS2 activity.
CC       {ECO:0000250|UniProtKB:P41220}.
DR   EMBL; DQ285660; ABB89038.1; -; Genomic_DNA.
DR   EMBL; DQ150111; AAZ94412.2; -; mRNA.
DR   RefSeq; NP_001038065.1; NM_001044600.1.
DR   SMR; Q3S853; -.
DR   STRING; 9823.ENSSSCP00000011519; -.
DR   PaxDb; Q3S853; -.
DR   PRIDE; Q3S853; -.
DR   Ensembl; ENSSSCT00000042452; ENSSSCP00000037031; ENSSSCG00000037241.
DR   GeneID; 733670; -.
DR   KEGG; ssc:733670; -.
DR   CTD; 5997; -.
DR   eggNOG; KOG3589; Eukaryota.
DR   eggNOG; ENOG410YMJD; LUCA.
DR   GeneTree; ENSGT00940000157937; -.
DR   HOGENOM; HOG000233512; -.
DR   InParanoid; Q3S853; -.
DR   KO; K18154; -.
DR   OMA; TIIKDWK; -.
DR   OrthoDB; 1246872at2759; -.
DR   TreeFam; TF315837; -.
DR   Reactome; R-SSC-416476; G alpha (q) signalling events.
DR   Proteomes; UP000008227; Chromosome 10.
DR   Bgee; ENSSSCG00000010806; Expressed in 5 organ(s), highest expression level in lung.
DR   ExpressionAtlas; Q3S853; differential.
DR   Genevisible; Q3S853; SS.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0001965; F:G-protein alpha-subunit binding; IEA:Ensembl.
DR   GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR   GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0140194; P:negative regulation of adenylate cyclase-inhibiting adrenergic receptor signaling pathway involved in heart process; IEA:Ensembl.
DR   GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; IEA:Ensembl.
DR   GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; IEA:Ensembl.
DR   GO; GO:0043407; P:negative regulation of MAP kinase activity; IEA:Ensembl.
DR   GO; GO:0010519; P:negative regulation of phospholipase activity; IEA:Ensembl.
DR   GO; GO:0060452; P:positive regulation of cardiac muscle contraction; IEA:Ensembl.
DR   GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0055119; P:relaxation of cardiac muscle; IEA:Ensembl.
DR   GO; GO:0060087; P:relaxation of vascular smooth muscle; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR   Gene3D; 1.10.196.10; -; 2.
DR   InterPro; IPR016137; RGS.
DR   InterPro; IPR034947; RGS2.
DR   InterPro; IPR036305; RGS_sf.
DR   InterPro; IPR024066; RGS_subdom1/3.
DR   PANTHER; PTHR10845:SF43; PTHR10845:SF43; 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;
DR   PRODOM; Q3S853.
DR   SWISS-2DPAGE; Q3S853.
KW   Cell cycle; Cell membrane; Complete proteome; Cytoplasm;
KW   GTPase activation; Membrane; Nucleus; Phosphoprotein;
KW   Reference proteome; Signal transduction inhibitor;
KW   Translation regulation.
FT   CHAIN         1    212       Regulator of G-protein signaling 2.
FT                                /FTId=PRO_0000204180.
FT   DOMAIN       83    199       RGS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00171}.
FT   REGION       32     66       Necessary for membrane association.
FT                                {ECO:0000250|UniProtKB:P41220}.
FT   REGION       79    116       Necessary to inhibit protein synthesis.
FT                                {ECO:0000250|UniProtKB:P41220}.
FT   CONFLICT    152    152       F -> S (in Ref. 1; ABB89038).
FT                                {ECO:0000305}.
SQ   SEQUENCE   212 AA;  24390 MW;  2B720A0FEC0FE41E CRC64;
     MQSAMFLTVH HDCGPMDKSA GTGPKSEEKR EKMKRTLLKD WKTRLSYFLQ NSSSPGKPKT
     GKKSKPQTFI KPSPEEAQLW AEAFDELLAS KYGLAAFRAF LKSEFCEENI EFWLACEDFK
     KTKSPQKLSS KARKIYTDFI EKEAPKEINI DFQTKTLIAQ NIQEATSGCF TTAQKRVYSL
     MENNSYPRFL ESEFYQDLCR KPPQITTEPH AT
//

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