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 03-AUG-2022, entry version 103.
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; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; 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 G
CC protein alpha subunits, thereby driving them into their inactive GDP-
CC bound form (By similarity). It is involved in the negative regulation
CC of the angiotensin-activated signaling pathway (By similarity). Plays a
CC role in the regulation of blood pressure in response to signaling via G
CC protein-coupled receptors and GNAQ. Plays a role in regulating the
CC constriction and relaxation of vascular smooth muscle (By similarity).
CC Binds EIF2B5 and blocks its activity, thereby inhibiting the
CC translation of mRNA into protein (By similarity).
CC {ECO:0000250|UniProtKB:O08849, ECO:0000250|UniProtKB:P41220}.
CC -!- SUBUNIT: Interacts with GNAQ. Does not interact with GNAI1 and GNAI3.
CC Interacts with EIF2B5. Interacts with PRKG1 (isoform alpha).
CC {ECO:0000250|UniProtKB:P41220}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P41220}.
CC Cytoplasm {ECO:0000250|UniProtKB:P41220}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P41220}.
CC -!- PTM: Phosphorylated by protein kinase C. Phosphorylation by PRKG1 leads
CC to activation of RGS2 activity. {ECO:0000250|UniProtKB:P41220}.
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DR EMBL; DQ285660; ABB89038.1; -; Genomic_DNA.
DR EMBL; DQ150111; AAZ94412.2; -; mRNA.
DR RefSeq; NP_001038065.1; NM_001044600.1.
DR AlphaFoldDB; Q3S853; -.
DR SMR; Q3S853; -.
DR STRING; 9823.ENSSSCP00000011519; -.
DR PaxDb; Q3S853; -.
DR PRIDE; Q3S853; -.
DR Ensembl; ENSSSCT00000042452; ENSSSCP00000037031; ENSSSCG00000037241.
DR Ensembl; ENSSSCT00005042909; ENSSSCP00005026286; ENSSSCG00005027080.
DR Ensembl; ENSSSCT00015095830; ENSSSCP00015039364; ENSSSCG00015071331.
DR Ensembl; ENSSSCT00025025008; ENSSSCP00025010563; ENSSSCG00025018435.
DR Ensembl; ENSSSCT00030007899; ENSSSCP00030003489; ENSSSCG00030005819.
DR Ensembl; ENSSSCT00035083042; ENSSSCP00035034478; ENSSSCG00035061803.
DR Ensembl; ENSSSCT00040080391; ENSSSCP00040034807; ENSSSCG00040059147.
DR Ensembl; ENSSSCT00045042702; ENSSSCP00045029654; ENSSSCG00045025061.
DR Ensembl; ENSSSCT00050081272; ENSSSCP00050034882; ENSSSCG00050059659.
DR Ensembl; ENSSSCT00060086126; ENSSSCP00060037242; ENSSSCG00060063124.
DR Ensembl; ENSSSCT00065075089; ENSSSCP00065032700; ENSSSCG00065054828.
DR Ensembl; ENSSSCT00070023534; ENSSSCP00070019468; ENSSSCG00070012071.
DR GeneID; 733670; -.
DR KEGG; ssc:733670; -.
DR CTD; 5997; -.
DR VGNC; VGNC:96538; RGS2.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000157937; -.
DR HOGENOM; CLU_059863_3_2_1; -.
DR InParanoid; Q3S853; -.
DR OMA; GRMKRTI; -.
DR OrthoDB; 1246872at2759; -.
DR TreeFam; TF315837; -.
DR Reactome; R-SSC-416476; G alpha (q) signalling events.
DR Proteomes; UP000008227; Chromosome 10.
DR Proteomes; UP000314985; Chromosome 10.
DR Bgee; ENSSSCG00000037241; Expressed in oocyte and 43 other tissues.
DR ExpressionAtlas; Q3S853; baseline and 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:0010855; F:adenylate cyclase inhibitor activity; IEA:Ensembl.
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: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 associated smooth muscle; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.10.196.10; -; 1.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR034947; RGS2.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR024066; RGS_subdom1/3.
DR InterPro; IPR044926; RGS_subdomain_2.
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;
KW Cell cycle; Cell membrane; Cytoplasm; GTPase activation; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Signal transduction inhibitor;
KW Translation regulation.
FT CHAIN 1..212
FT /note="Regulator of G-protein signaling 2"
FT /id="PRO_0000204180"
FT DOMAIN 83..199
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT REGION 11..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 32..66
FT /note="Necessary for membrane association"
FT /evidence="ECO:0000250|UniProtKB:P41220"
FT REGION 48..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..116
FT /note="Necessary to inhibit protein synthesis"
FT /evidence="ECO:0000250|UniProtKB:P41220"
FT CONFLICT 152
FT /note="F -> S (in Ref. 1; ABB89038)"
FT /evidence="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