RGS9_TAMST
ID RGS9_TAMST Reviewed; 484 AA.
AC Q80ZD1;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Regulator of G-protein signaling 9;
DE Short=RGS9;
OS Tamias striatus (Eastern chipmunk).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Tamias.
OX NCBI_TaxID=45474;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH GBB5.
RC TISSUE=Retina;
RX PubMed=12598617; DOI=10.1523/jneurosci.23-04-01287.2003;
RA Zhang X., Wensel T.G., Kraft T.W.;
RT "GTPase regulators and photoresponses in cones of the eastern chipmunk.";
RL J. Neurosci. 23:1287-1297(2003).
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. Binds to G(t)-alpha. Involved in
CC phototransduction; key element in the recovery phase of visual
CC transduction (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with Gbeta5. Interacts with RGS7BP, leading to
CC regulate the subcellular location of the heterodimer formed with
CC Gbeta5. Component of the RGS9-1-Gbeta5 complex composed of RGS9 (RGS9-
CC 1), Gbeta5 (GNB5) and RGS9BP (Probable). {ECO:0000305|PubMed:12598617}.
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC Note=Targeted to the membrane via its interaction with RGS9BP.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation is decreased by light exposition. {ECO:0000250}.
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DR EMBL; AF480879; AAO49275.1; -; mRNA.
DR AlphaFoldDB; Q80ZD1; -.
DR SMR; Q80ZD1; -.
DR PRIDE; Q80ZD1; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd00068; GGL; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 4.10.260.10; -; 1.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR015898; G-protein_gamma-like_dom.
DR InterPro; IPR036284; GGL_sf.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR040759; RGS_DHEX.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF00631; G-gamma; 1.
DR Pfam; PF00615; RGS; 1.
DR Pfam; PF18148; RGS_DHEX; 1.
DR PRINTS; PR01301; RGSPROTEIN.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00224; GGL; 1.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF48670; SSF48670; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW Membrane; Sensory transduction; Signal transduction inhibitor; Vision.
FT CHAIN 1..484
FT /note="Regulator of G-protein signaling 9"
FT /id="PRO_0000204206"
FT DOMAIN 30..105
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 219..280
FT /note="G protein gamma"
FT DOMAIN 299..414
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
SQ SEQUENCE 484 AA; 56670 MW; FC2FF63230588C09 CRC64;
MTIRHQGQQY RPRMAFLQKI EALVKDMQNP DTGVKTQSQR VLVTSVPHAM TGGDVLQWII
QRLWISSLEA QNLGNFIVKY GYIYPLQDPK NLILKPDSSL YRFQTPYFWP TQQWPAEDTD
YAIYLAKRNI KKKGILEEYE KENYNFLNKK INYKWDFVIM QAKEQYRAGK ERNKADRYAL
DCQEKAYWLV HRCPPGMNDV LDYGLDRVTN PNEVKKQTIT AVKKEIMYYQ QALMRSTVKS
SVSLGGIVKY SEQFSSNDAI MSGCLPSNPW ITDDTQFWDL NAKLVEIPTK MRVERWAFNF
SELIRDPKGR QSFQYFLRKE FSGENLGFWE ACEDLKYGDQ SKVKEKAEEI YKLFLAPGAR
RWINIDGKTM DITVKGLKHP HRYVLDAAQT HIYMLMKKDS YARYLKSPIY KEMLAKAIEP
QETTKKSSTL PFIRRHLRSS PSPVILRQLE EEAKAREAAN TVDITQVMSK LDRRSLLKKE
LPPK