RGS17_CHICK
ID RGS17_CHICK Reviewed; 210 AA.
AC Q9PWA0;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Regulator of G-protein signaling 17;
DE Short=RGS17;
GN Name=RGS17;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spinal ganglion;
RX PubMed=10419452; DOI=10.1074/jbc.274.31.21507;
RA Jordan J.D., Carey K.D., Stork P.J.S., Iyengar R.;
RT "Modulation of rap activity by direct interaction of Galpha(o) with Rap1
RT GTPase-activating protein.";
RL J. Biol. Chem. 274:21507-21510(1999).
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q9QZB0, ECO:0000250|UniProtKB:Q9UGC6}.
CC -!- SUBUNIT: Interacts with GNAI1 and GNAQ (By similarity). Interacts with
CC GNAZ and GNAI2. 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 (By similarity).
CC {ECO:0000250|UniProtKB:Q9QZB0, ECO:0000250|UniProtKB:Q9UGC6}.
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 -!- 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. {ECO:0000250|UniProtKB:Q9QZB0}.
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DR EMBL; AF151968; AAD45948.1; -; mRNA.
DR RefSeq; NP_990172.1; NM_204841.2.
DR AlphaFoldDB; Q9PWA0; -.
DR SMR; Q9PWA0; -.
DR STRING; 9031.ENSGALP00000043022; -.
DR PaxDb; Q9PWA0; -.
DR Ensembl; ENSGALT00000043882; ENSGALP00000043022; ENSGALG00000026034.
DR GeneID; 395645; -.
DR KEGG; gga:395645; -.
DR CTD; 26575; -.
DR VEuPathDB; HostDB:geneid_395645; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000155393; -.
DR HOGENOM; CLU_059863_0_2_1; -.
DR InParanoid; Q9PWA0; -.
DR OrthoDB; 1409647at2759; -.
DR PhylomeDB; Q9PWA0; -.
DR TreeFam; TF315837; -.
DR Reactome; R-GGA-416476; G alpha (q) signalling events.
DR Reactome; R-GGA-418594; G alpha (i) signalling events.
DR Reactome; R-GGA-418597; G alpha (z) signalling events.
DR PRO; PR:Q9PWA0; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000026034; Expressed in brain and 4 other tissues.
DR ExpressionAtlas; Q9PWA0; baseline and differential.
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; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Cytoplasm; Glycoprotein; GTPase activation; Membrane; Nucleus;
KW Reference proteome; Signal transduction inhibitor; Synapse; Synaptosome;
KW Ubl conjugation.
FT CHAIN 1..210
FT /note="Regulator of G-protein signaling 17"
FT /id="PRO_0000204226"
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"
SQ SEQUENCE 210 AA; 24326 MW; 6581AAD5BADDEE7C CRC64;
MRKRQQSQNE GTSAVSQAPG NQRPNNTCCF CWCCCCSCSC LTVRNEDRGD NAGRPTHTTK
MESIQVIEEC QNPTADEILS WAQNFDKMMK TPAGRNLFRE FLRTEYSEEN LLFWLACEDL
KKEQNKKVIE EKARLIYEDY ISILSPKEVS LDSRVREVIN RNLLDPSPHM YEDAQLQIYT
LMHRDSFPRF LNSQIYKSLV ESITGSTSET
