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Regulator of G-protein signaling 17 (RGS17) (Regulator of Gz-selective protein signaling 2)

 RGS17_MOUSE             Reviewed;         210 AA.
Q9QZB0; Q543T9;
14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
17-JUN-2020, entry version 139.
RecName: Full=Regulator of G-protein signaling 17;
Short=RGS17;
AltName: Full=Regulator of Gz-selective protein signaling 2;
Name=Rgs17; Synonyms=Rgsz2 {ECO:0000303|Ref.1};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
Barker S.A., Ross E.M.;
"RGSZ2, a new member of the Gz-selective GAP family.";
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Cerebellum, Corpora quadrigemina, Olfactory bulb, and Pituitary;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
INTERACTION WITH OPRM1; GNAZ AND GNAI2, GLYCOSYLATION, TISSUE SPECIFICITY,
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15827571; DOI=10.1038/sj.npp.1300726;
Garzan J., Rodriguez-Munoz M., Lopez-Fando A., Sanchez-Blazquez P.;
"The RGSZ2 protein exists in a complex with mu-opioid receptors and
regulates the desensitizing capacity of Gz proteins.";
Neuropsychopharmacology 30:1632-1648(2005).
[4]
SUMOYLATION, PHOSPHORYLATION, SUBCELLULAR LOCATION, FUNCTION, INTERACTION
WITH GNAZ AND GNAI2, AND TISSUE SPECIFICITY.
PubMed=16900103; DOI=10.1038/sj.npp.1301184;
Rodriguez-Munoz M., Bermudez D., Sanchez-Blazquez P., Garzon J.;
"Sumoylated RGS-Rz proteins act as scaffolds for mu-opioid receptors and G-
protein complexes in mouse brain.";
Neuropsychopharmacology 32:842-850(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-137, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
-!- FUNCTION: Regulates G protein-coupled receptor signaling cascades,
including signaling via muscarinic acetylcholine receptor CHRM2 and
dopamine receptor DRD2 (By similarity). Inhibits signal transduction by
increasing the GTPase activity of G protein alpha subunits, thereby
driving them into their inactive GDP-bound form. Binds selectively to
GNAZ and GNAI2 subunits, accelerates their GTPase activity and
regulates their signaling activities. Negatively regulates mu-opioid
receptor-mediated activation of the G-proteins.
{ECO:0000250|UniProtKB:Q9UGC6, ECO:0000269|PubMed:15827571,
ECO:0000269|PubMed:16900103}.
-!- SUBUNIT: Interacts with GNAI1 and GNAQ (By similarity). Interacts with
GNAZ and GNAI2 (PubMed:15827571, PubMed:16900103). Interacts with OPRM1
(PubMed:15827571). Forms a complex with mu-opioid receptors and
G(alpha)z/i2 subunits, including GNAZ and GNAI2; the formation of this
complex results in mu-opioid receptor desensitization
(PubMed:15827571). {ECO:0000250|UniProtKB:Q9UGC6,
ECO:0000269|PubMed:15827571, ECO:0000269|PubMed:16900103}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15827571,
ECO:0000269|PubMed:16900103}. Cell junction, synapse, synaptosome
{ECO:0000269|PubMed:15827571, ECO:0000269|PubMed:16900103}. Nucleus
{ECO:0000269|PubMed:16900103}. Cytoplasm {ECO:0000269|PubMed:16900103}.
-!- TISSUE SPECIFICITY: Detected in brain (at protein level)
(PubMed:15827571, PubMed:16900103). Highly expressed in the
hypothalamus, periaqueductal gray matter, and pons-medulla. Lower
levels in the thalamus, cortex and spinal cord. Weak expression in the
striatum and cerebellum. {ECO:0000269|PubMed:15827571,
ECO:0000269|PubMed:16900103}.
-!- PTM: N- and O-glycosylated in synapsomal membranes.
{ECO:0000269|PubMed:15827571}.
-!- PTM: Serine phosphorylated in synapsomal membranes.
{ECO:0000269|PubMed:16900103}.
-!- PTM: Sumoylated with SUMO1 and SUM02 in synaptosomes. The sumoylated
forms act as a scaffold for sequestering mu-opioid receptor-activated
G(alpha) subunits. {ECO:0000269|PubMed:16900103}.
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EMBL; AF191555; AAF05758.1; -; mRNA.
EMBL; AK018279; BAB31145.1; -; mRNA.
EMBL; AK030492; BAC26989.1; -; mRNA.
EMBL; AK046009; BAC32571.1; -; mRNA.
EMBL; AK163188; BAE37226.1; -; mRNA.
CCDS; CCDS56685.1; -.
RefSeq; NP_001155294.1; NM_001161822.1.
RefSeq; NP_064342.1; NM_019958.4.
RefSeq; XP_006512520.1; XM_006512457.3.
SMR; Q9QZB0; -.
STRING; 10090.ENSMUSP00000116291; -.
iPTMnet; Q9QZB0; -.
PhosphoSitePlus; Q9QZB0; -.
MaxQB; Q9QZB0; -.
PaxDb; Q9QZB0; -.
PRIDE; Q9QZB0; -.
Antibodypedia; 33390; 146 antibodies.
Ensembl; ENSMUST00000117676; ENSMUSP00000113519; ENSMUSG00000019775.
Ensembl; ENSMUST00000131996; ENSMUSP00000116291; ENSMUSG00000019775.
GeneID; 56533; -.
KEGG; mmu:56533; -.
UCSC; uc007egg.2; mouse.
CTD; 26575; -.
MGI; MGI:1927469; Rgs17.
eggNOG; KOG3589; Eukaryota.
eggNOG; ENOG410YMJD; LUCA.
GeneTree; ENSGT00940000155393; -.
InParanoid; Q9QZB0; -.
KO; K16449; -.
OMA; QSFDKMM; -.
OrthoDB; 1409647at2759; -.
PhylomeDB; Q9QZB0; -.
TreeFam; TF315837; -.
Reactome; R-MMU-416476; G alpha (q) signalling events.
Reactome; R-MMU-418594; G alpha (i) signalling events.
Reactome; R-MMU-418597; G alpha (z) signalling events.
BioGRID-ORCS; 56533; 1 hit in 12 CRISPR screens.
ChiTaRS; Rgs17; mouse.
PRO; PR:Q9QZB0; -.
Proteomes; UP000000589; Chromosome 10.
RNAct; Q9QZB0; protein.
Bgee; ENSMUSG00000019775; Expressed in secondary oocyte and 170 other tissues.
Genevisible; Q9QZB0; MM.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
GO; GO:0005096; F:GTPase activator activity; TAS:MGI.
GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:MGI.
GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
InterPro; IPR016137; RGS.
InterPro; IPR036305; RGS_sf.
Pfam; PF00615; RGS; 1.
PRINTS; PR01301; RGSPROTEIN.
SMART; SM00315; RGS; 1.
SUPFAM; SSF48097; SSF48097; 1.
PROSITE; PS50132; RGS; 1.
1: Evidence at protein level;
Cell junction; Cytoplasm; Glycoprotein; GTPase activation; Membrane;
Nucleus; Phosphoprotein; Reference proteome; Signal transduction inhibitor;
Synapse; Synaptosome; Ubl conjugation.
CHAIN 1..210
/note="Regulator of G-protein signaling 17"
/id="PRO_0000204225"
DOMAIN 84..200
/note="RGS"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
COMPBIAS 28..40
/note="Poly-Cys"
MOD_RES 137
/note="Phosphotyrosine"
/evidence="ECO:0000244|PubMed:18034455"
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


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WP1049: G Protein Signaling Pathways
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WP232: G Protein Signaling Pathways
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WP211: BMP signaling pathway
WP1689: Porphyrin and chlorophyll metabolism
WP813: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP931: G Protein Signaling Pathways
WP2032: TSH signaling pathway
WP2292: Chemokine signaling pathway
WP35: G Protein Signaling Pathways
WP1150: IL-3 Signaling Pathway
WP235: Wnt Signaling
WP1289: Type II interferon signaling (IFNG)
WP363: Wnt Signaling Pathway
WP1370: TGF Beta Signaling Pathway
WP510: MAPK Signaling Pathway
WP1657: Glycerolipid metabolism
WP747: IL-2 Signaling Pathway
WP1868: Netrin-1 signaling
WP10: IL-9 Signaling Pathway
WP818: IL-4 signaling Pathway

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Bibliography :