RGS20_MOUSE
ID RGS20_MOUSE Reviewed; 239 AA.
AC Q9QZB1; Q14A97; Q3TY63; Q9CUV8; Q9QZB2;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Regulator of G-protein signaling 20;
DE Short=RGS20;
DE AltName: Full=Regulator of G-protein signaling Z1;
GN Name=Rgs20; Synonyms=Rgsz1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-32.
RC STRAIN=129/B6, and BALB/cJ;
RA Barker S.A., Wang J., Ross E.M.;
RT "A mouse ortholog of RGSZ1.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hippocampus, and Visual cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND GLYCOSYLATION.
RX PubMed=14997173; DOI=10.1038/sj.npp.1300408;
RA Garzan J., Rodriguez-Munoz M., Lopez-Fando A., Garcia-Espana A.,
RA Sanchez-Blazquez P.;
RT "RGSZ1 and GAIP regulate mu- but not delta-opioid receptors in mouse CNS:
RT role in tachyphylaxis and acute tolerance.";
RL Neuropsychopharmacology 29:1091-1104(2004).
RN [5]
RP INTERACTION WITH OPRM1, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=15827571; DOI=10.1038/sj.npp.1300726;
RA Garzan J., Rodriguez-Munoz M., Lopez-Fando A., Sanchez-Blazquez P.;
RT "The RGSZ2 protein exists in a complex with mu-opioid receptors and
RT regulates the desensitizing capacity of Gz proteins.";
RL Neuropsychopharmacology 30:1632-1648(2005).
RN [6]
RP SUMOYLATION, PHOSPHORYLATION, AND FUNCTION.
RX PubMed=16900103; DOI=10.1038/sj.npp.1301184;
RA Rodriguez-Munoz M., Bermudez D., Sanchez-Blazquez P., Garzon J.;
RT "Sumoylated RGS-Rz proteins act as scaffolds for mu-opioid receptors and G-
RT protein complexes in mouse brain.";
RL Neuropsychopharmacology 32:842-850(2007).
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 selectively to G(z)-alpha and G(alpha)-
CC i2 subunits, accelerates their GTPase activity and regulates their
CC signaling activities. The G(z)-alpha activity is inhibited by the
CC phosphorylation and palmitoylation of the G-protein. Negatively
CC regulates mu-opioid receptor-mediated activation of the G-proteins.
CC {ECO:0000269|PubMed:14997173, ECO:0000269|PubMed:15827571,
CC ECO:0000269|PubMed:16900103}.
CC -!- SUBUNIT: Forms a complex with G(alpha)z/i2 subunits and mu-opioid
CC receptors; the formation of this complex results in mu-opioid receptor
CC desensitization. Interacts with OPRM1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor. Nucleus. Cytoplasm.
CC Note=Shuttles between the cytoplasm/cell membrane and the nucleus
CC Anchored to the membrane through palmitoylation. {ECO:0000250}.
CC -!- PTM: Fatty acylated. Heavily palmitoylated in the cysteine string motif
CC (By similarity). {ECO:0000250}.
CC -!- PTM: N- and O-glycosylated in synapsomal membranes.
CC {ECO:0000269|PubMed:14997173}.
CC -!- PTM: Serine phosphorylated in synapsomal membranes.
CC {ECO:0000269|PubMed:16900103}.
CC -!- PTM: Sumoylated with SUMO1, SUMO2 and SUMO3. Sumoylation increases
CC binding to the G-proteins, G(alpha)-i2 and G(z), and interaction with
CC mu-opioid receptors. {ECO:0000269|PubMed:16900103}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB28987.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF191554; AAF05757.1; -; mRNA.
DR EMBL; AF191552; AAF05756.1; -; mRNA.
DR EMBL; AK013773; BAB28987.2; ALT_INIT; mRNA.
DR EMBL; AK158864; BAE34700.1; -; mRNA.
DR EMBL; BC116925; AAI16926.1; -; mRNA.
DR EMBL; BC116929; AAI16930.1; -; mRNA.
DR CCDS; CCDS14807.1; -.
DR RefSeq; NP_001277301.1; NM_001290372.1.
DR RefSeq; NP_067349.2; NM_021374.5.
DR RefSeq; XP_011236702.1; XM_011238400.1.
DR AlphaFoldDB; Q9QZB1; -.
DR SMR; Q9QZB1; -.
DR BioGRID; 208369; 4.
DR IntAct; Q9QZB1; 2.
DR MINT; Q9QZB1; -.
DR STRING; 10090.ENSMUSP00000113398; -.
DR iPTMnet; Q9QZB1; -.
DR PhosphoSitePlus; Q9QZB1; -.
DR SwissPalm; Q9QZB1; -.
DR MaxQB; Q9QZB1; -.
DR PeptideAtlas; Q9QZB1; -.
DR PRIDE; Q9QZB1; -.
DR ProteomicsDB; 253123; -.
DR Antibodypedia; 11664; 170 antibodies from 29 providers.
DR DNASU; 58175; -.
DR Ensembl; ENSMUST00000002533; ENSMUSP00000002533; ENSMUSG00000002459.
DR GeneID; 58175; -.
DR KEGG; mmu:58175; -.
DR UCSC; uc007afk.3; mouse.
DR CTD; 8601; -.
DR MGI; MGI:1929866; Rgs20.
DR VEuPathDB; HostDB:ENSMUSG00000002459; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000159123; -.
DR InParanoid; Q9QZB1; -.
DR OMA; RPMGSEC; -.
DR PhylomeDB; Q9QZB1; -.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-418597; G alpha (z) signalling events.
DR BioGRID-ORCS; 58175; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Rgs20; mouse.
DR PRO; PR:Q9QZB1; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9QZB1; protein.
DR Bgee; ENSMUSG00000002459; Expressed in caudate-putamen and 121 other tissues.
DR ExpressionAtlas; Q9QZB1; baseline and differential.
DR Genevisible; Q9QZB1; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; TAS:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; TAS:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:MGI.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR Gene3D; 1.10.167.10; -; 1.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
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 1: Evidence at protein level;
KW Cytoplasm; Glycoprotein; Lipoprotein; Membrane; Nucleus; Palmitate;
KW Phosphoprotein; Reference proteome; Signal transduction inhibitor;
KW Ubl conjugation.
FT CHAIN 1..239
FT /note="Regulator of G-protein signaling 20"
FT /id="PRO_0000204234"
FT DOMAIN 113..229
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 32
FT /note="M -> R (in strain: BALB/c)"
FT /evidence="ECO:0000269|Ref.1"
SQ SEQUENCE 239 AA; 26986 MW; F383923163A44D18 CRC64;
MRTANGGPRA RASPSASPAD PGLPEGSERT EMRMRQMCGG SETQGPAPSQ QGGRGSNACC
FCWCCCCTCS CLTVRNQEDQ RPQRASHEIR TDIPACEESP TPTLEEVCAW AQSFDNLMVT
PAGRNAFREF LRTEFSEENM LFWMACEELK REANKSTIEE KARIIYEDYI SILSPKEVSL
DSRVREVINR NMVDPSQHIF DDAQLQIYTL MHRDSYPRFM NSTVYKDLLT SLAEKTVEA
