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   24-JAN-2024, entry version 157.
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. Interacts with GNAO1.
CC       {ECO:0000250|UniProtKB:P49795}.
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; 10116-ENSRNOP00000022451; -.
DR   Ensembl; ENSRNOT00000022451.5; ENSRNOP00000022451.4; ENSRNOG00000016547.6.
DR   Ensembl; ENSRNOT00055002045; ENSRNOP00055001612; ENSRNOG00055001222.
DR   Ensembl; ENSRNOT00060002087; ENSRNOP00060001283; ENSRNOG00060001420.
DR   Ensembl; ENSRNOT00065023124; ENSRNOP00065018012; ENSRNOG00065014006.
DR   GeneID; 59293; -.
DR   KEGG; rno:59293; -.
DR   UCSC; RGD:629471; rat.
DR   AGR; RGD:629471; -.
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; 22856at2759; -.
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 cell types or tissues.
DR   GO; GO:0005903; C:brush border; IDA:RGD.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IDA:RGD.
DR   GO; GO:0000139; C:Golgi membrane; TAS: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; 1.10.196.10; -; 2.
DR   Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR   InterPro; IPR016137; RGS.
DR   InterPro; IPR036305; RGS_sf.
DR   InterPro; IPR024066; RGS_subdom1/3.
DR   InterPro; IPR044926; RGS_subdomain_2.
DR   PANTHER; PTHR10845; REGULATOR OF G PROTEIN SIGNALING; 1.
DR   PANTHER; PTHR10845:SF145; REGULATOR OF G-PROTEIN SIGNALING 19; 1.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR   PROSITE; PS50132; RGS; 1.
DR   Genevisible; O70521; RN.
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
//