ID   RGS9_RAT                Reviewed;         677 AA.
AC   P49805;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 3.
DT   24-JAN-2024, entry version 167.
DE   RecName: Full=Regulator of G-protein signaling 9;
DE            Short=RGS9;
GN   Name=Rgs9;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=Sprague-Dawley; TISSUE=Hypothalamus;
RX   PubMed=9765512;
RA   Granneman J.G., Zhai Y., Zhu Z., Bannon M.J., Burchett S.A., Schmidt C.J.,
RA   Andrade R., Cooper J.;
RT   "Molecular characterization of human and rat RGS9L, a novel splice variant
RT   enriched in dopamine target regions, and chromosomal localization of the
RT   RGS9 gene.";
RL   Mol. Pharmacol. 54:687-694(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RGS9L).
RC   TISSUE=Brain;
RA   Zhou J., Moroi K., Homma S., Usui H., Nishiyama M., Kimura S.;
RT   "A long form of rat regulator of G-protein signaling 9 (RGS9).";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 234-677 (ISOFORM RGS9L).
RC   STRAIN=Sprague-Dawley;
RC   TISSUE=Cerebellum, Corpus striatum, and Hippocampus;
RX   PubMed=9556034;
RX   DOI=10.1002/(sici)1097-4547(19980401)52:1<118::aid-jnr11>3.0.co;2-6;
RA   Thomas E.A., Danielson P.E., Sutcliffe J.G.;
RT   "RGS9: a regulator of G-protein signalling with specific expression in rat
RT   and mouse striatum.";
RL   J. Neurosci. Res. 52:118-124(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 330-395.
RC   TISSUE=Brain;
RX   PubMed=8548815; DOI=10.1016/s0092-8674(00)80998-8;
RA   Koelle M.R., Horvitz H.R.;
RT   "EGL-10 regulates G protein signaling in the C. elegans nervous system and
RT   shares a conserved domain with many mammalian proteins.";
RL   Cell 84:115-125(1996).
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 GNAT1. Involved in phototransduction;
CC       key element in the recovery phase of visual transduction (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer with GNB5. Interacts with RGS7BP, leading to
CC       regulate the subcellular location of the heterodimer formed with GNB5.
CC       Component of the RGS9-1-Gbeta5 complex composed of RGS9 (RGS9-1),
CC       Gbeta5 (GNB5) and RGS9BP. Interacts with PDE6G and GNAT1.
CC       {ECO:0000250|UniProtKB:O46469}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC       Note=Targeted to the membrane via its interaction with RGS9BP.
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=RGS9L;
CC         IsoId=P49805-1; Sequence=Displayed;
CC       Name=RGS9S;
CC         IsoId=P49805-2; Sequence=VSP_005680;
CC   -!- TISSUE SPECIFICITY: Expressed in the central nervous system. Isoform
CC       RGS9L is found in striatum, hypothalamus and nucleus accumbens while
CC       isoform RGS9S is expressed in retina and pineal gland.
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DR   EMBL; AF071475; AAC64039.1; -; mRNA.
DR   EMBL; AB019145; BAA34051.1; -; mRNA.
DR   EMBL; AF038006; AAC01959.1; -; mRNA.
DR   EMBL; U32433; AAC52370.1; -; mRNA.
DR   RefSeq; NP_062097.1; NM_019224.2. [P49805-1]
DR   AlphaFoldDB; P49805; -.
DR   SMR; P49805; -.
DR   STRING; 10116.ENSRNOP00000005076; -.
DR   CarbonylDB; P49805; -.
DR   PhosphoSitePlus; P49805; -.
DR   PaxDb; 10116-ENSRNOP00000005076; -.
DR   Ensembl; ENSRNOT00000005076.7; ENSRNOP00000005076.6; ENSRNOG00000003800.7. [P49805-1]
DR   Ensembl; ENSRNOT00055054679; ENSRNOP00055045196; ENSRNOG00055031554. [P49805-1]
DR   Ensembl; ENSRNOT00060024734; ENSRNOP00060019701; ENSRNOG00060014467. [P49805-1]
DR   GeneID; 29481; -.
DR   KEGG; rno:29481; -.
DR   AGR; RGD:3572; -.
DR   CTD; 8787; -.
DR   RGD; 3572; Rgs9.
DR   eggNOG; KOG3589; Eukaryota.
DR   GeneTree; ENSGT00940000156505; -.
DR   HOGENOM; CLU_025092_5_0_1; -.
DR   InParanoid; P49805; -.
DR   OrthoDB; 22856at2759; -.
DR   PhylomeDB; P49805; -.
DR   Reactome; R-RNO-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR   Reactome; R-RNO-418594; G alpha (i) signalling events.
DR   Reactome; R-RNO-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   PRO; PR:P49805; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000003800; Expressed in frontal cortex and 10 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098839; C:postsynaptic density membrane; ISO:RGD.
DR   GO; GO:0042734; C:presynaptic membrane; ISO:RGD.
DR   GO; GO:0005096; F:GTPase activator activity; IDA:RGD.
DR   GO; GO:1990603; P:dark adaptation; ISO:RGD.
DR   GO; GO:0007212; P:dopamine receptor signaling pathway; IMP:RGD.
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:0036367; P:light adaption; ISO:RGD.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEP:RGD.
DR   GO; GO:1905912; P:regulation of calcium ion export across plasma membrane; IDA:RGD.
DR   GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IDA:RGD.
DR   GO; GO:0001975; P:response to amphetamine; IEP:RGD.
DR   GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   CDD; cd04450; DEP_RGS7-like; 1.
DR   CDD; cd00068; GGL; 1.
DR   CDD; cd08739; RGS_RGS9; 1.
DR   Gene3D; 1.10.1240.60; -; 1.
DR   Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR   Gene3D; 4.10.260.10; Transducin (heterotrimeric G protein), gamma chain; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; IPR047016; RGS6/7/9/11.
DR   InterPro; IPR047017; RGS6/7/9/11_DHEX_sf.
DR   InterPro; IPR047077; RGS9_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   PANTHER; PTHR45746; LP21163P; 1.
DR   PANTHER; PTHR45746:SF1; REGULATOR OF G-PROTEIN SIGNALING 9; 1.
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; SM01224; G_gamma; 1.
DR   SMART; SM00224; GGL; 1.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR   SUPFAM; SSF48670; Transducin (heterotrimeric G protein), gamma chain; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50186; DEP; 1.
DR   PROSITE; PS50132; RGS; 1.
DR   Genevisible; P49805; RN.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Membrane; Reference proteome; Sensory transduction;
KW   Signal transduction inhibitor; Vision.
FT   CHAIN           1..677
FT                   /note="Regulator of G-protein signaling 9"
FT                   /id="PRO_0000204205"
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          295..416
FT                   /note="RGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT   REGION          530..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          639..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         467..677
FT                   /note="Missing (in isoform RGS9S)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_005680"
SQ   SEQUENCE   677 AA;  77131 MW;  39F403E3D3C37A67 CRC64;
     MTIRHQGQQY RPRMAFLQKI EALVKDMQNP ETGVRMQNQR VLVTSVPHAM TGGDVLQWII
     QRLWISNLEA QNLGNFIVKY GYIYPLQDPK NLVLKPDSSL YRFQTPYFWP TQQWPAEDTD
     YAIYLAKRNI KKKGILEEYE KENYDFLNKK INYKWDFVIM QAKEQYRTGK ERNKADRYAL
     DCQEKAYWLV HRSPPGMNNV LDYGLDRVTN PNEVKKQTVT AVRKEIMYYQ QALMRSTVKS
     SVSLGGIVKY SEQFSSNDAI MSGCLPSNPW ITDDTQFWDL NAKLVEVPTK MRVERWAFNF
     SELIRDPKGR QSFQYFLKKE FSGENLGFWE ACEDLKYGDQ SKVKEKAEEI YKLFLAPGAR
     RWINIDGKTM DITVKGLRHP HRYVLDAAQT HIYMLMKKDS YARYLKSPIY KEMLAKAIEP
     QETTKRSSTL PFMRRHLRSS PSPVILRQLE EEERAREAAN TVDITQPGQH LAPSPHLAVY
     TGTCVPPSPS SPFSPSCRSP RKPFPSPSRF IRRPSIAICP SPIRVALEGS SGLEGKGEAS
     WSGANPGPPV TESIETSVDR SRPHSQPRAP LKARAALSLG RFLRRGCLAS PVFARLSPKC
     PSVSHGKVQP LGDMGQQLPR LKPKKVANFF QIKMEMPTDS GPCLMDSDDP GAGESGDQTT
     EKEVICPWES LAEGKAG
//