RGS17_HUMAN
ID RGS17_HUMAN Reviewed; 210 AA.
AC Q9UGC6; Q5TF49; Q8TD61; Q9UJS8;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Regulator of G-protein signaling 17;
DE Short=RGS17;
GN Name=RGS17; Synonyms=RGSZ2 {ECO:0000303|PubMed:15096504};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Ghahremani M.H., Daigle M., Albert P.R.;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 61-210.
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15096504; DOI=10.1074/jbc.m401800200;
RA Mao H., Zhao Q., Daigle M., Ghahremani M.H., Chidiac P., Albert P.R.;
RT "RGS17/RGSZ2, a novel regulator of Gi/o, Gz, and Gq signaling.";
RL J. Biol. Chem. 279:26314-26322(2004).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 72-206, AND INTERACTION WITH
RP GNAI1 AND GNAQ.
RX PubMed=18434541; DOI=10.1073/pnas.0801508105;
RA Soundararajan M., Willard F.S., Kimple A.J., Turnbull A.P., Ball L.J.,
RA Schoch G.A., Gileadi C., Fedorov O.Y., Dowler E.F., Higman V.A.,
RA Hutsell S.Q., Sundstroem M., Doyle D.A., Siderovski D.P.;
RT "Structural diversity in the RGS domain and its interaction with
RT heterotrimeric G protein alpha-subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:6457-6462(2008).
CC -!- FUNCTION: Regulates G protein-coupled receptor signaling cascades,
CC including signaling via muscarinic acetylcholine receptor CHRM2 and
CC dopamine receptor DRD2. Inhibits signal transduction by increasing the
CC GTPase activity of G protein alpha subunits, thereby driving them into
CC their inactive GDP-bound form (PubMed:15096504). 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 (By similarity).
CC {ECO:0000250|UniProtKB:Q9QZB0, ECO:0000269|PubMed:15096504}.
CC -!- SUBUNIT: Interacts with GNAI1 and GNAQ (PubMed:18434541). Interacts
CC with GNAZ and GNAI2. Interacts with OPRM1. Forms a complex with mu-
CC opioid receptors and G(alpha)z/i2 subunits, including GNAZ and GNAI2;
CC the formation of this complex results in mu-opioid receptor
CC desensitization (By similarity). Interacts with HINT1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9QZB0, ECO:0000269|PubMed:18434541}.
CC -!- INTERACTION:
CC Q9UGC6; P29972: AQP1; NbExp=6; IntAct=EBI-3918154, EBI-745213;
CC Q9UGC6; A0A087WZT3: BOLA2B; NbExp=3; IntAct=EBI-3918154, EBI-12006120;
CC Q9UGC6; Q9H2X0: CHRD; NbExp=3; IntAct=EBI-3918154, EBI-947551;
CC Q9UGC6; Q9UGL9: CRCT1; NbExp=3; IntAct=EBI-3918154, EBI-713677;
CC Q9UGC6; Q02930-3: CREB5; NbExp=3; IntAct=EBI-3918154, EBI-10192698;
CC Q9UGC6; G5E9A7: DMWD; NbExp=3; IntAct=EBI-3918154, EBI-10976677;
CC Q9UGC6; Q53GS7: GLE1; NbExp=3; IntAct=EBI-3918154, EBI-1955541;
CC Q9UGC6; P63096: GNAI1; NbExp=3; IntAct=EBI-3918154, EBI-618639;
CC Q9UGC6; P08754: GNAI3; NbExp=3; IntAct=EBI-3918154, EBI-357563;
CC Q9UGC6; P49639: HOXA1; NbExp=6; IntAct=EBI-3918154, EBI-740785;
CC Q9UGC6; Q9H2F3: HSD3B7; NbExp=3; IntAct=EBI-3918154, EBI-3918847;
CC Q9UGC6; O14901: KLF11; NbExp=3; IntAct=EBI-3918154, EBI-948266;
CC Q9UGC6; Q9BYQ6: KRTAP4-11; NbExp=3; IntAct=EBI-3918154, EBI-10302392;
CC Q9UGC6; Q6L8G4: KRTAP5-11; NbExp=5; IntAct=EBI-3918154, EBI-11993296;
CC Q9UGC6; Q6L8H2: KRTAP5-3; NbExp=3; IntAct=EBI-3918154, EBI-11974251;
CC Q9UGC6; Q6L8H1: KRTAP5-4; NbExp=3; IntAct=EBI-3918154, EBI-11963072;
CC Q9UGC6; Q6L8G9: KRTAP5-6; NbExp=3; IntAct=EBI-3918154, EBI-10250562;
CC Q9UGC6; Q5T7P2: LCE1A; NbExp=3; IntAct=EBI-3918154, EBI-11962058;
CC Q9UGC6; Q5T7P3: LCE1B; NbExp=3; IntAct=EBI-3918154, EBI-10245913;
CC Q9UGC6; Q5T752: LCE1D; NbExp=5; IntAct=EBI-3918154, EBI-11741311;
CC Q9UGC6; Q5T753: LCE1E; NbExp=3; IntAct=EBI-3918154, EBI-11955335;
CC Q9UGC6; Q5TA79: LCE2A; NbExp=3; IntAct=EBI-3918154, EBI-10246607;
CC Q9UGC6; O14633: LCE2B; NbExp=3; IntAct=EBI-3918154, EBI-11478468;
CC Q9UGC6; Q5TA81: LCE2C; NbExp=3; IntAct=EBI-3918154, EBI-11973993;
CC Q9UGC6; Q5TA76: LCE3A; NbExp=3; IntAct=EBI-3918154, EBI-9394625;
CC Q9UGC6; Q5TA77: LCE3B; NbExp=5; IntAct=EBI-3918154, EBI-11974495;
CC Q9UGC6; Q5T5A8: LCE3C; NbExp=3; IntAct=EBI-3918154, EBI-10245291;
CC Q9UGC6; Q9BYE3: LCE3D; NbExp=3; IntAct=EBI-3918154, EBI-6658837;
CC Q9UGC6; Q5T5B0: LCE3E; NbExp=3; IntAct=EBI-3918154, EBI-10245456;
CC Q9UGC6; Q5TA78: LCE4A; NbExp=3; IntAct=EBI-3918154, EBI-10246358;
CC Q9UGC6; Q5TCM9: LCE5A; NbExp=5; IntAct=EBI-3918154, EBI-11955689;
CC Q9UGC6; Q7Z417: NUFIP2; NbExp=3; IntAct=EBI-3918154, EBI-1210753;
CC Q9UGC6; P32242: OTX1; NbExp=6; IntAct=EBI-3918154, EBI-740446;
CC Q9UGC6; P43115-12: PTGER3; NbExp=3; IntAct=EBI-3918154, EBI-10234038;
CC Q9UGC6; P62906: RPL10A; NbExp=6; IntAct=EBI-3918154, EBI-356860;
CC Q9UGC6; Q92504: SLC39A7; NbExp=3; IntAct=EBI-3918154, EBI-1051105;
CC Q9UGC6; P49901: SMCP; NbExp=3; IntAct=EBI-3918154, EBI-750494;
CC Q9UGC6; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-3918154, EBI-5235340;
CC Q9UGC6; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-3918154, EBI-357085;
CC Q9UGC6; Q6EMK4: VASN; NbExp=3; IntAct=EBI-3918154, EBI-10249550;
CC Q9UGC6; Q9NWL9; NbExp=3; IntAct=EBI-3918154, EBI-10315054;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9QZB0}. Synapse,
CC synaptosome {ECO:0000250|UniProtKB:Q9QZB0}. Nucleus
CC {ECO:0000250|UniProtKB:Q9QZB0}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9QZB0}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the cerebellum. Also
CC expressed in the cortex and medulla. Weakly expressed in a number of
CC peripheral tissues notably spleen, lung and leukocytes.
CC {ECO:0000269|PubMed:15096504}.
CC -!- PTM: N- and O-glycosylated in synapsomal membranes.
CC {ECO:0000250|UniProtKB:Q9QZB0}.
CC -!- PTM: Serine phosphorylated in synapsomal membranes.
CC {ECO:0000250|UniProtKB:Q9QZB0}.
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 (By similarity). Desumoylated by HINT1 (By
CC similarity). {ECO:0000250|UniProtKB:Q9QZB0}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RGS17ID47522ch6q25.html";
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DR EMBL; AF202257; AAF08978.3; -; mRNA.
DR EMBL; BT006997; AAP35643.1; -; mRNA.
DR EMBL; AL080276; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013117; AAH13117.1; -; mRNA.
DR EMBL; AF493938; AAM12652.1; -; mRNA.
DR CCDS; CCDS5244.1; -.
DR RefSeq; NP_036551.3; NM_012419.4.
DR PDB; 1ZV4; X-ray; 2.40 A; X=72-206.
DR PDB; 6AM3; X-ray; 1.53 A; A/X=72-206.
DR PDBsum; 1ZV4; -.
DR PDBsum; 6AM3; -.
DR AlphaFoldDB; Q9UGC6; -.
DR SMR; Q9UGC6; -.
DR BioGRID; 117744; 45.
DR DIP; DIP-59095N; -.
DR IntAct; Q9UGC6; 45.
DR STRING; 9606.ENSP00000356194; -.
DR BindingDB; Q9UGC6; -.
DR ChEMBL; CHEMBL4295974; -.
DR GuidetoPHARMACOLOGY; 2801; -.
DR iPTMnet; Q9UGC6; -.
DR PhosphoSitePlus; Q9UGC6; -.
DR SwissPalm; Q9UGC6; -.
DR BioMuta; RGS17; -.
DR DMDM; 15214238; -.
DR jPOST; Q9UGC6; -.
DR MassIVE; Q9UGC6; -.
DR PaxDb; Q9UGC6; -.
DR PeptideAtlas; Q9UGC6; -.
DR PRIDE; Q9UGC6; -.
DR ProteomicsDB; 84206; -.
DR Antibodypedia; 33390; 180 antibodies from 30 providers.
DR DNASU; 26575; -.
DR Ensembl; ENST00000206262.2; ENSP00000206262.1; ENSG00000091844.8.
DR Ensembl; ENST00000367225.6; ENSP00000356194.1; ENSG00000091844.8.
DR GeneID; 26575; -.
DR KEGG; hsa:26575; -.
DR MANE-Select; ENST00000206262.2; ENSP00000206262.1; NM_012419.5; NP_036551.3.
DR UCSC; uc003qpm.4; human.
DR CTD; 26575; -.
DR DisGeNET; 26575; -.
DR GeneCards; RGS17; -.
DR HGNC; HGNC:14088; RGS17.
DR HPA; ENSG00000091844; Tissue enhanced (brain).
DR MIM; 607191; gene.
DR neXtProt; NX_Q9UGC6; -.
DR OpenTargets; ENSG00000091844; -.
DR PharmGKB; PA34368; -.
DR VEuPathDB; HostDB:ENSG00000091844; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000155393; -.
DR HOGENOM; CLU_059863_0_2_1; -.
DR InParanoid; Q9UGC6; -.
DR OMA; MQDNSNA; -.
DR OrthoDB; 1409647at2759; -.
DR PhylomeDB; Q9UGC6; -.
DR TreeFam; TF315837; -.
DR PathwayCommons; Q9UGC6; -.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-418597; G alpha (z) signalling events.
DR SignaLink; Q9UGC6; -.
DR BioGRID-ORCS; 26575; 5 hits in 1064 CRISPR screens.
DR ChiTaRS; RGS17; human.
DR EvolutionaryTrace; Q9UGC6; -.
DR GeneWiki; RGS17; -.
DR GenomeRNAi; 26575; -.
DR Pharos; Q9UGC6; Tchem.
DR PRO; PR:Q9UGC6; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9UGC6; protein.
DR Bgee; ENSG00000091844; Expressed in cortical plate and 162 other tissues.
DR Genevisible; Q9UGC6; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; 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:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; TAS:Reactome.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome.
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 3D-structure; Cytoplasm; Glycoprotein; GTPase activation; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Signal transduction inhibitor;
KW Synapse; Synaptosome; Ubl conjugation.
FT CHAIN 1..210
FT /note="Regulator of G-protein signaling 17"
FT /id="PRO_0000204224"
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:0000250|UniProtKB:Q9QZB0"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:6AM3"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:6AM3"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:6AM3"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:6AM3"
FT HELIX 109..120
FT /evidence="ECO:0007829|PDB:6AM3"
FT HELIX 126..140
FT /evidence="ECO:0007829|PDB:6AM3"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:6AM3"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:6AM3"
FT HELIX 172..184
FT /evidence="ECO:0007829|PDB:6AM3"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:6AM3"
FT HELIX 194..203
FT /evidence="ECO:0007829|PDB:6AM3"
SQ SEQUENCE 210 AA; 24359 MW; 0AFA22A43BF5E481 CRC64;
MRKRQQSQNE GTPAVSQAPG NQRPNNTCCF CWCCCCSCSC LTVRNEERGE NAGRPTHTTK
MESIQVLEEC QNPTAEEVLS WSQNFDKMMK APAGRNLFRE FLRTEYSEEN LLFWLACEDL
KKEQNKKVIE EKARMIYEDY ISILSPKEVS LDSRVREVIN RNLLDPNPHM YEDAQLQIYT
LMHRDSFPRF LNSQIYKSFV ESTAGSSSES
