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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.
16-OCT-2019, entry version 135.
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; -.
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; -.
HOGENOM; HOG000233513; -.
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.
ChiTaRS; Rgs17; mouse.
PRO; PR:Q9QZB0; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000019775; Expressed in 171 organ(s), highest expression level in secondary oocyte.
ExpressionAtlas; Q9QZB0; baseline and differential.
Genevisible; Q9QZB0; MM.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
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; Complete proteome; Cytoplasm; Glycoprotein;
GTPase activation; Membrane; Nucleus; Phosphoprotein;
Reference proteome; Signal transduction inhibitor; Synapse;
Synaptosome; Ubl conjugation.
CHAIN 1 210 Regulator of G-protein signaling 17.
/FTId=PRO_0000204225.
DOMAIN 84 200 RGS. {ECO:0000255|PROSITE-
ProRule:PRU00171}.
COMPBIAS 28 40 Poly-Cys.
MOD_RES 137 137 Phosphotyrosine.
{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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WP211: BMP signaling pathway
WP1689: Porphyrin and chlorophyll metabolism
WP813: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
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WP2292: Chemokine signaling pathway
WP2032: TSH signaling pathway
WP35: G Protein Signaling Pathways
WP1370: TGF Beta Signaling Pathway
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WP510: MAPK Signaling Pathway
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WP747: IL-2 Signaling Pathway
WP10: IL-9 Signaling Pathway
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WP1098: Wnt Signaling Pathway
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[Rgs7bp D13Bwg1146e R7bp] Regulator of G-protein signaling 7-binding protein (R7 family-binding protein)
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[OPRM1] Mu-type opioid receptor (M-OR-1) (MOR-1) (Fragment)
[Sh2b1 Sh2-b Sh2bpsm1] SH2B adapter protein 1 (FceRI gamma-chain-interacting protein SH2-B) (SH2 domain-containing protein 1B) (SH2-B PH domain-containing signaling mediator 1)
[GPSM2 LGN] G-protein-signaling modulator 2 (Mosaic protein LGN)
[OPRM1 MOR1] Mu-type opioid receptor (M-OR-1) (MOR-1)
[OPRM1] Mu-type opioid receptor (M-OR-1) (MOR-1)
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