RGS2_BOVIN
ID RGS2_BOVIN Reviewed; 211 AA.
AC Q0P5H5;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Regulator of G-protein signaling 2;
DE Short=RGS2;
GN Name=RGS2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal lung;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-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; BC120026; AAI20027.1; -; mRNA.
DR RefSeq; NP_001069064.1; NM_001075596.1.
DR AlphaFoldDB; Q0P5H5; -.
DR SMR; Q0P5H5; -.
DR PaxDb; Q0P5H5; -.
DR PRIDE; Q0P5H5; -.
DR Ensembl; ENSBTAT00000027478; ENSBTAP00000067806; ENSBTAG00000020620.
DR GeneID; 513055; -.
DR KEGG; bta:513055; -.
DR CTD; 5997; -.
DR VEuPathDB; HostDB:ENSBTAG00000020620; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000157937; -.
DR InParanoid; Q0P5H5; -.
DR OMA; THTEMAS; -.
DR OrthoDB; 1246872at2759; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000020620; Expressed in oocyte and 65 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; IEA:InterPro.
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 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..211
FT /note="Regulator of G-protein signaling 2"
FT /id="PRO_0000271374"
FT DOMAIN 83..199
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT REGION 14..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 49..71
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"
SQ SEQUENCE 211 AA; 24210 MW; D25DC20E24FE9FD6 CRC64;
MQSALFLAVQ HECGPMDKGA GTGPKNEEKR EKMKRTLLKD WKSRLSYFLQ NSSSPGKPKT
GKKSKQQTFI KPSPEEAQLW SEAFDELLAS KYGLAAFRAF LKSEFCEENI EFWLACEDFK
KTKSPQKLSS KAKKIYTDFI EKEAPKEINI DFQTKSLIAQ NIQEATSGCF TTAQKRVYSL
MENNSYPRFL ESEFYQDLCK KPQITTEPHA T