RGS19_RAT
ID RGS19_RAT Reviewed; 216 AA.
AC O70521;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Regulator of G-protein signaling 19;
DE Short=RGS19;
DE AltName: Full=G-alpha-interacting protein;
DE Short=GAIP;
GN Name=Rgs19; Synonyms=Gaip;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=9571244; DOI=10.1091/mbc.9.5.1123;
RA de Vries L., Elenko E., McCaffery J.M., Fischer T., Hubler L.,
RA McQuistan T., Watson N., Farquhar M.G.;
RT "RGS-GAIP, a GTPase-activating protein for Galphai heterotrimeric G
RT proteins, is located on clathrin-coated vesicles.";
RL Mol. Biol. Cell 9:1123-1134(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
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 [3]
RP PHOSPHORYLATION AT SER-24, AND MUTAGENESIS OF SER-24.
RX PubMed=10760275; DOI=10.1073/pnas.97.8.4040;
RA Fischer T., Elenko E., Wan L., Thomas G., Farquhar M.G.;
RT "Membrane-associated GAIP is a phosphoprotein and can be phosphorylated by
RT clathrin-coated vesicles.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:4040-4045(2000).
CC -!- FUNCTION: Inhibits signal transduction by increasing the GTPase
CC activity of G protein alpha subunits thereby driving them into their
CC inactive GDP-bound form. Binds to G-alpha subfamily 1 members,
CC predominantly to G(i)-alpha-3. Activity on G(z)-alpha is inhibited by
CC phosphorylation and palmitoylation of the G-protein (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with GIPC PDZ domain.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}.
CC -!- PTM: Fatty acylated. Heavily palmitoylated in the cysteine string motif
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated, mainly on serine residues.
CC {ECO:0000269|PubMed:10760275}.
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DR EMBL; AF068136; AAC19130.1; -; mRNA.
DR EMBL; BC088141; AAH88141.1; -; mRNA.
DR RefSeq; NP_067693.1; NM_021661.2.
DR RefSeq; XP_006235863.2; XM_006235801.3.
DR AlphaFoldDB; O70521; -.
DR SMR; O70521; -.
DR BioGRID; 248744; 1.
DR MINT; O70521; -.
DR STRING; 10116.ENSRNOP00000022451; -.
DR iPTMnet; O70521; -.
DR PhosphoSitePlus; O70521; -.
DR PaxDb; O70521; -.
DR Ensembl; ENSRNOT00000022451; ENSRNOP00000022451; ENSRNOG00000016547.
DR GeneID; 59293; -.
DR KEGG; rno:59293; -.
DR UCSC; RGD:629471; rat.
DR CTD; 10287; -.
DR RGD; 629471; Rgs19.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000160391; -.
DR HOGENOM; CLU_059863_0_2_1; -.
DR InParanoid; O70521; -.
DR OMA; MSQHETS; -.
DR OrthoDB; 1409647at2759; -.
DR PhylomeDB; O70521; -.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:O70521; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000016547; Expressed in spleen and 19 other tissues.
DR Genevisible; O70521; RN.
DR GO; GO:0005903; C:brush border; IDA:RGD.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0000139; C:Golgi membrane; TAS:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IDA:RGD.
DR GO; GO:0005096; F:GTPase activator activity; TAS:RGD.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; TAS:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.10.196.10; -; 2.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR024066; RGS_subdom1/3.
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 Lipoprotein; Membrane; Palmitate; Phosphoprotein; Reference proteome;
KW Signal transduction inhibitor.
FT CHAIN 1..216
FT /note="Regulator of G-protein signaling 19"
FT /id="PRO_0000204231"
FT DOMAIN 90..206
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..216
FT /note="Interaction with GIPC"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:10760275"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49795"
FT MOD_RES 151
FT /note="Phosphoserine; by MAPK1 and MAPK3"
FT /evidence="ECO:0000250|UniProtKB:P49795"
FT MUTAGEN 24
FT /note="S->A: 50% reduction of phosphorylation."
FT /evidence="ECO:0000269|PubMed:10760275"
SQ SEQUENCE 216 AA; 24738 MW; 554C479D4DD89238 CRC64;
MPTPHEAEKQ HTGPEEADRP PSMSSHDAAP SGPPSRNPCC LCWCCCCSCS WNQERQRAWQ
VSRESKLQPL PSCEVCTPPS PEEVQSWAQS FDKLMHSPTG RSVFRAFLRT EYSEENMLFW
LACEELKTEA DRHVVDEKAR LIYEDYVSIL SPKEVSLDSR VREGINRKMQ EPSPHTFDDA
QLQIYTLMHR DSYPRFLTSP TYRSLLLQGA PQSSEA
