RGS17_MOUSE
ID RGS17_MOUSE Reviewed; 210 AA.
AC Q9QZB0; Q543T9;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Regulator of G-protein signaling 17;
DE Short=RGS17;
DE AltName: Full=Regulator of Gz-selective protein signaling 2;
GN Name=Rgs17; Synonyms=Rgsz2 {ECO:0000303|Ref.1};
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].
RC STRAIN=BALB/cJ;
RA Barker S.A., Ross E.M.;
RT "RGSZ2, a new member of the Gz-selective GAP family.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Corpora quadrigemina, Olfactory bulb, and Pituitary;
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 INTERACTION WITH OPRM1; GNAZ AND GNAI2, GLYCOSYLATION, TISSUE SPECIFICITY,
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [4]
RP SUMOYLATION, PHOSPHORYLATION, SUBCELLULAR LOCATION, FUNCTION, INTERACTION
RP WITH GNAZ AND GNAI2, AND TISSUE SPECIFICITY.
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).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-137, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [6]
RP INTERACTION WITH HINT1, AND DESUMOYLATION.
RX PubMed=31088288; DOI=10.1089/ars.2019.7724;
RA Cortes-Montero E., Rodriguez-Munoz M., Sanchez-Blazquez P., Garzon J.;
RT "The Axonal Motor Neuropathy-Related HINT1 Protein Is a Zinc- and
RT Calmodulin-Regulated Cysteine SUMO Protease.";
RL Antioxid. Redox Signal. 31:503-520(2019).
CC -!- FUNCTION: Regulates G protein-coupled receptor signaling cascades,
CC including signaling via muscarinic acetylcholine receptor CHRM2 and
CC dopamine receptor DRD2 (By similarity). Inhibits signal transduction by
CC increasing the GTPase activity of G protein alpha subunits, thereby
CC driving them into their inactive GDP-bound form. Binds selectively to
CC GNAZ and GNAI2 subunits, accelerates their GTPase activity and
CC regulates their signaling activities. Negatively regulates mu-opioid
CC receptor-mediated activation of the G-proteins.
CC {ECO:0000250|UniProtKB:Q9UGC6, ECO:0000269|PubMed:15827571,
CC ECO:0000269|PubMed:16900103}.
CC -!- SUBUNIT: Interacts with GNAI1 and GNAQ (By similarity). Interacts with
CC GNAZ and GNAI2 (PubMed:15827571, PubMed:16900103). Interacts with OPRM1
CC (PubMed:15827571). Forms a complex with mu-opioid receptors and
CC G(alpha)z/i2 subunits, including GNAZ and GNAI2; the formation of this
CC complex results in mu-opioid receptor desensitization
CC (PubMed:15827571). Interacts with HINT1 (PubMed:31088288).
CC {ECO:0000250|UniProtKB:Q9UGC6, ECO:0000269|PubMed:15827571,
CC ECO:0000269|PubMed:16900103, ECO:0000269|PubMed:31088288}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15827571,
CC ECO:0000269|PubMed:16900103}. Synapse, synaptosome
CC {ECO:0000269|PubMed:15827571, ECO:0000269|PubMed:16900103}. Nucleus
CC {ECO:0000269|PubMed:16900103}. Cytoplasm {ECO:0000269|PubMed:16900103}.
CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level)
CC (PubMed:15827571, PubMed:16900103). Highly expressed in the
CC hypothalamus, periaqueductal gray matter, and pons-medulla. Lower
CC levels in the thalamus, cortex and spinal cord. Weak expression in the
CC striatum and cerebellum. {ECO:0000269|PubMed:15827571,
CC ECO:0000269|PubMed:16900103}.
CC -!- PTM: N- and O-glycosylated in synapsomal membranes.
CC {ECO:0000269|PubMed:15827571}.
CC -!- PTM: Serine phosphorylated in synapsomal membranes.
CC {ECO:0000269|PubMed:16900103}.
CC -!- PTM: Sumoylated with SUMO1 and SUM02 in synaptosomes. The sumoylated
CC forms act as a scaffold for sequestering mu-opioid receptor-activated
CC G(alpha) subunits (PubMed:16900103). Desumoylated by HINT1
CC (PubMed:31088288). {ECO:0000269|PubMed:16900103,
CC ECO:0000269|PubMed:31088288}.
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DR EMBL; AF191555; AAF05758.1; -; mRNA.
DR EMBL; AK018279; BAB31145.1; -; mRNA.
DR EMBL; AK030492; BAC26989.1; -; mRNA.
DR EMBL; AK046009; BAC32571.1; -; mRNA.
DR EMBL; AK163188; BAE37226.1; -; mRNA.
DR CCDS; CCDS56685.1; -.
DR RefSeq; NP_001155294.1; NM_001161822.1.
DR RefSeq; NP_064342.1; NM_019958.4.
DR RefSeq; XP_006512520.1; XM_006512457.3.
DR AlphaFoldDB; Q9QZB0; -.
DR SMR; Q9QZB0; -.
DR IntAct; Q9QZB0; 1.
DR MINT; Q9QZB0; -.
DR STRING; 10090.ENSMUSP00000116291; -.
DR iPTMnet; Q9QZB0; -.
DR PhosphoSitePlus; Q9QZB0; -.
DR MaxQB; Q9QZB0; -.
DR PaxDb; Q9QZB0; -.
DR PRIDE; Q9QZB0; -.
DR ProteomicsDB; 253262; -.
DR Antibodypedia; 33390; 180 antibodies from 30 providers.
DR DNASU; 56533; -.
DR Ensembl; ENSMUST00000117676; ENSMUSP00000113519; ENSMUSG00000019775.
DR Ensembl; ENSMUST00000131996; ENSMUSP00000116291; ENSMUSG00000019775.
DR GeneID; 56533; -.
DR KEGG; mmu:56533; -.
DR UCSC; uc007egg.2; mouse.
DR CTD; 26575; -.
DR MGI; MGI:1927469; Rgs17.
DR VEuPathDB; HostDB:ENSMUSG00000019775; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000155393; -.
DR InParanoid; Q9QZB0; -.
DR OMA; NAHMYED; -.
DR OrthoDB; 1409647at2759; -.
DR PhylomeDB; Q9QZB0; -.
DR TreeFam; TF315837; -.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-418597; G alpha (z) signalling events.
DR BioGRID-ORCS; 56533; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Rgs17; mouse.
DR PRO; PR:Q9QZB0; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9QZB0; protein.
DR Bgee; ENSMUSG00000019775; Expressed in superior colliculus and 148 other tissues.
DR ExpressionAtlas; Q9QZB0; baseline and differential.
DR Genevisible; Q9QZB0; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
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; GTPase activation; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Signal transduction inhibitor; Synapse;
KW Synaptosome; Ubl conjugation.
FT CHAIN 1..210
FT /note="Regulator of G-protein signaling 17"
FT /id="PRO_0000204225"
FT DOMAIN 84..200
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 137
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
SQ SEQUENCE 210 AA; 24345 MW; 451B868679E5B9B0 CRC64;
MRKRQQSQNE GTQAVSQAPG NQRPNNTCCF CWCCCCSCSC LTVRNEERGD SSGRSPHTTK
MESIQVLEEC QNPTADEVLS WSQNFDKMMK TPAGRNLFRE FLRTEYSEEN LLFWLACEDL
KKEQNKKAVE EKARMIYEDY ISILSPKEVS LDSRVREVIN RSLLDPSPHM YEDAQLQIYT
LMHRDSFPRF LNSQIYKAFV ESTTSCTSES
