ID   RGS19_BOVIN             Reviewed;         223 AA.
AC   Q08DC7;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Regulator of G-protein signaling 19;
DE            Short=RGS19;
GN   Name=RGS19;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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, with the
CC       order G(i)a3 > G(i)a1 > G(o)a >> G(z)a/G(i)a2. Activity on G(z)-alpha
CC       is inhibited by phosphorylation and palmitoylation of the G-protein (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with GIPC PDZ domain. {ECO:0000250}.
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. {ECO:0000250}.
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DR   EMBL; BC123821; AAI23822.1; -; mRNA.
DR   RefSeq; NP_001070383.1; NM_001076915.1.
DR   AlphaFoldDB; Q08DC7; -.
DR   BMRB; Q08DC7; -.
DR   SMR; Q08DC7; -.
DR   STRING; 9913.ENSBTAP00000050801; -.
DR   PaxDb; Q08DC7; -.
DR   PRIDE; Q08DC7; -.
DR   Ensembl; ENSBTAT00000054910; ENSBTAP00000050801; ENSBTAG00000021837.
DR   GeneID; 539036; -.
DR   KEGG; bta:539036; -.
DR   CTD; 10287; -.
DR   VEuPathDB; HostDB:ENSBTAG00000021837; -.
DR   VGNC; VGNC:33918; RGS19.
DR   eggNOG; KOG3589; Eukaryota.
DR   GeneTree; ENSGT00940000160391; -.
DR   HOGENOM; CLU_059863_0_2_1; -.
DR   InParanoid; Q08DC7; -.
DR   OMA; MSQHETS; -.
DR   OrthoDB; 1409647at2759; -.
DR   TreeFam; TF315837; -.
DR   Proteomes; UP000009136; Chromosome 13.
DR   Bgee; ENSBTAG00000021837; Expressed in neutrophil and 103 other tissues.
DR   ExpressionAtlas; Q08DC7; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Autophagy; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Reference proteome; Signal transduction inhibitor.
FT   CHAIN           1..223
FT                   /note="Regulator of G-protein signaling 19"
FT                   /id="PRO_0000284971"
FT   DOMAIN          96..212
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          213..223
FT                   /note="Interaction with GIPC"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         24
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O70521"
FT   MOD_RES         103
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P49795"
FT   MOD_RES         157
FT                   /note="Phosphoserine; by MAPK1 and MAPK3"
FT                   /evidence="ECO:0000250|UniProtKB:P49795"
SQ   SEQUENCE   223 AA;  25353 MW;  5B8D69B952E04A68 CRC64;
     MPTPPEAEKQ QTGPEEADQP PSMSSHDAAP PAPPRRNPCC LCWCCCCSCS WNEERRRAWR
     ASRESRLQPL PSCEVCATPT PTPTPTPEEV RSWAQSFDKL MHSPAGRSVF REFLRTEYSE
     ENMLFWLACE ELKAEANQHV VDEKARLIYE DYVSILSPKE VSLDSRVREG INKKMQEPSA
     HTFDDAQLQI YTLMHRDSYP RFLSSPAYRA LLLQGASQSS SEA