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Protein

Regulator of G-protein signaling 17

Gene

Rgs17

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity2 Publications

GO - Molecular functioni

  • GTPase activator activity Source: MGI

GO - Biological processi

  • G-protein coupled receptor signaling pathway Source: MGI
  • negative regulation of signal transduction Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation, Signal transduction inhibitor

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of G-protein signaling 17
Short name:
RGS17
Alternative name(s):
Regulator of Gz-selective protein signaling 2
Gene namesi
Name:Rgs17
Synonyms:Rgsz21 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1927469. Rgs17.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Membrane, Nucleus, Synapse, Synaptosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 210210Regulator of G-protein signaling 17PRO_0000204225Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei137 – 1371PhosphotyrosineCombined sources

Post-translational modificationi

N- and O-glycosylated in synapsomal membranes.1 Publication
Serine phosphorylated in synapsomal membranes.1 Publication
Sumoylated with SUMO1 and SUM02 in synaptosomes. The sumoylated forms act as a scaffold for sequestering mu-opioid receptor-activated G(alpha) subunits.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9QZB0.
MaxQBiQ9QZB0.
PaxDbiQ9QZB0.
PRIDEiQ9QZB0.

PTM databases

iPTMnetiQ9QZB0.
PhosphoSiteiQ9QZB0.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiQ9QZB0.
CleanExiMM_RGS17.
ExpressionAtlasiQ9QZB0. baseline and differential.
GenevisibleiQ9QZB0. MM.

Interactioni

Subunit structurei

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).By similarity2 Publications

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000065825.

Structurei

3D structure databases

ProteinModelPortaliQ9QZB0.
SMRiQ9QZB0. Positions 69-203.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini84 – 200117RGSPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi28 – 4013Poly-CysAdd
BLAST

Sequence similaritiesi

Contains 1 RGS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3589. Eukaryota.
ENOG410YMJD. LUCA.
GeneTreeiENSGT00760000118903.
HOGENOMiHOG000233513.
HOVERGENiHBG013233.
InParanoidiQ9QZB0.
KOiK16449.
OrthoDBiEOG7SN8DQ.
PhylomeDBiQ9QZB0.
TreeFamiTF315837.

Family and domain databases

Gene3Di1.10.196.10. 1 hit.
InterProiIPR016137. RGS.
IPR024066. RGS_subdom1.
[Graphical view]
PfamiPF00615. RGS. 1 hit.
[Graphical view]
PRINTSiPR01301. RGSPROTEIN.
SMARTiSM00315. RGS. 1 hit.
[Graphical view]
SUPFAMiSSF48097. SSF48097. 1 hit.
PROSITEiPS50132. RGS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9QZB0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKRQQSQNE GTQAVSQAPG NQRPNNTCCF CWCCCCSCSC LTVRNEERGD
60 70 80 90 100
SSGRSPHTTK MESIQVLEEC QNPTADEVLS WSQNFDKMMK TPAGRNLFRE
110 120 130 140 150
FLRTEYSEEN LLFWLACEDL KKEQNKKAVE EKARMIYEDY ISILSPKEVS
160 170 180 190 200
LDSRVREVIN RSLLDPSPHM YEDAQLQIYT LMHRDSFPRF LNSQIYKAFV
210
ESTTSCTSES
Length:210
Mass (Da):24,345
Last modified:May 1, 2000 - v1
Checksum:i451B868679E5B9B0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191555 mRNA. Translation: AAF05758.1.
AK018279 mRNA. Translation: BAB31145.1.
AK030492 mRNA. Translation: BAC26989.1.
AK046009 mRNA. Translation: BAC32571.1.
AK163188 mRNA. Translation: BAE37226.1.
CCDSiCCDS56685.1.
RefSeqiNP_001155294.1. NM_001161822.1.
NP_064342.1. NM_019958.4.
XP_006512520.1. XM_006512457.2.
UniGeneiMm.44606.

Genome annotation databases

EnsembliENSMUST00000117676; ENSMUSP00000113519; ENSMUSG00000019775.
ENSMUST00000131996; ENSMUSP00000116291; ENSMUSG00000019775.
GeneIDi56533.
KEGGimmu:56533.
UCSCiuc007egg.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191555 mRNA. Translation: AAF05758.1.
AK018279 mRNA. Translation: BAB31145.1.
AK030492 mRNA. Translation: BAC26989.1.
AK046009 mRNA. Translation: BAC32571.1.
AK163188 mRNA. Translation: BAE37226.1.
CCDSiCCDS56685.1.
RefSeqiNP_001155294.1. NM_001161822.1.
NP_064342.1. NM_019958.4.
XP_006512520.1. XM_006512457.2.
UniGeneiMm.44606.

3D structure databases

ProteinModelPortaliQ9QZB0.
SMRiQ9QZB0. Positions 69-203.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000065825.

PTM databases

iPTMnetiQ9QZB0.
PhosphoSiteiQ9QZB0.

Proteomic databases

EPDiQ9QZB0.
MaxQBiQ9QZB0.
PaxDbiQ9QZB0.
PRIDEiQ9QZB0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000117676; ENSMUSP00000113519; ENSMUSG00000019775.
ENSMUST00000131996; ENSMUSP00000116291; ENSMUSG00000019775.
GeneIDi56533.
KEGGimmu:56533.
UCSCiuc007egg.2. mouse.

Organism-specific databases

CTDi26575.
MGIiMGI:1927469. Rgs17.

Phylogenomic databases

eggNOGiKOG3589. Eukaryota.
ENOG410YMJD. LUCA.
GeneTreeiENSGT00760000118903.
HOGENOMiHOG000233513.
HOVERGENiHBG013233.
InParanoidiQ9QZB0.
KOiK16449.
OrthoDBiEOG7SN8DQ.
PhylomeDBiQ9QZB0.
TreeFamiTF315837.

Miscellaneous databases

PROiQ9QZB0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QZB0.
CleanExiMM_RGS17.
ExpressionAtlasiQ9QZB0. baseline and differential.
GenevisibleiQ9QZB0. MM.

Family and domain databases

Gene3Di1.10.196.10. 1 hit.
InterProiIPR016137. RGS.
IPR024066. RGS_subdom1.
[Graphical view]
PfamiPF00615. RGS. 1 hit.
[Graphical view]
PRINTSiPR01301. RGSPROTEIN.
SMARTiSM00315. RGS. 1 hit.
[Graphical view]
SUPFAMiSSF48097. SSF48097. 1 hit.
PROSITEiPS50132. RGS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "RGSZ2, a new member of the Gz-selective GAP family."
    Barker S.A., Ross E.M.
    Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
  2. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum, Corpora quadrigemina, Olfactory bulb and Pituitary.
  3. "The RGSZ2 protein exists in a complex with mu-opioid receptors and regulates the desensitizing capacity of Gz proteins."
    Garzan J., Rodriguez-Munoz M., Lopez-Fando A., Sanchez-Blazquez P.
    Neuropsychopharmacology 30:1632-1648(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH OPRM1; GNAZ AND GNAI2, GLYCOSYLATION, TISSUE SPECIFICITY, FUNCTION, SUBCELLULAR LOCATION.
  4. "Sumoylated RGS-Rz proteins act as scaffolds for mu-opioid receptors and G-protein complexes in mouse brain."
    Rodriguez-Munoz M., Bermudez D., Sanchez-Blazquez P., Garzon J.
    Neuropsychopharmacology 32:842-850(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION, PHOSPHORYLATION, SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH GNAZ AND GNAI2, TISSUE SPECIFICITY.
  5. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiRGS17_MOUSE
AccessioniPrimary (citable) accession number: Q9QZB0
Secondary accession number(s): Q543T9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.