RGS16_PIG
ID RGS16_PIG Reviewed; 200 AA.
AC F1S668; A9QVL1;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2017, sequence version 3.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Regulator of G-protein signaling 16;
DE Short=poRGS16 {ECO:0000303|PubMed:19570954};
GN Name=RGS16;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc;
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INTERACTION WITH PCV2 ORF3
RP (MICROBIAL INFECTION).
RX PubMed=19570954; DOI=10.1099/vir.0.008896-0;
RA Timmusk S., Merlot E., Lovgren T., Jarvekulg L., Berg M., Fossum C.;
RT "Regulator of G protein signalling 16 is a target for a porcine circovirus
RT type 2 protein.";
RL J. Gen. Virol. 90:2425-2436(2009).
RN [3]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH PCV2 ORF3 (MICROBIAL
RP INFECTION).
RX PubMed=25575706; DOI=10.1099/vir.0.000046;
RA Choi C.Y., Rho S.B., Kim H.S., Han J., Bae J., Lee S.J., Jung W.W.,
RA Chun T.;
RT "The ORF3 protein of porcine circovirus type 2 promotes secretion of IL-6
RT and IL-8 in porcine epithelial cells by facilitating proteasomal
RT degradation of regulator of G protein signalling 16 through physical
RT interaction.";
RL J. Gen. Virol. 96:1098-1108(2015).
CC -!- FUNCTION: Regulates G protein-coupled receptor signaling cascades.
CC Inhibits signal transduction by increasing the GTPase activity of G
CC protein alpha subunits, thereby driving them into their inactive GDP-
CC bound form. Plays an important role in the phototransduction cascade by
CC regulating the lifetime and effective concentration of activated
CC transducin alpha. May regulate extra and intracellular mitogenic
CC signals. {ECO:0000250|UniProtKB:P97428}.
CC -!- FUNCTION: (Microbial infection) Gets inactivated and/or degraded by
CC porcine circovirus 2 ORF3 protein, leading to enhanced expression of
CC IL-6 and IL-8 in infected lymphocytes. This would explain chronic
CC inflammatory response of PCV2 infected pigs.
CC {ECO:0000269|PubMed:25575706}.
CC -!- SUBUNIT: Interacts with GNAI1 and GNAQ. Interacts with GNAI3, GNAI3 and
CC GNAO1. {ECO:0000250|UniProtKB:O15492, ECO:0000250|UniProtKB:P97428}.
CC -!- SUBUNIT: (Microbial infection) Interacts with porcine circovirus 2 ORF3
CC protein. {ECO:0000269|PubMed:25575706}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P97428}; Lipid-
CC anchor {ECO:0000250|UniProtKB:P97428}.
CC -!- PTM: Palmitoylated on Cys-2 and/or Cys-12.
CC {ECO:0000250|UniProtKB:P97428}.
CC -!- PTM: Phosphorylated. Phosphorylation at Tyr-168 by EGFR enhances GTPase
CC accelerating (GAP) activity toward GNAI1.
CC {ECO:0000250|UniProtKB:O15492}.
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DR EMBL; AEMK02000070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; EU271873; ABX71210.1; -; mRNA.
DR RefSeq; NP_001106488.1; NM_001113017.1.
DR RefSeq; XP_013835375.1; XM_013979921.1.
DR AlphaFoldDB; F1S668; -.
DR SMR; F1S668; -.
DR STRING; 9823.ENSSSCP00000016486; -.
DR PaxDb; F1S668; -.
DR PRIDE; F1S668; -.
DR Ensembl; ENSSSCT00000016940; ENSSSCP00000016486; ENSSSCG00000015550.
DR Ensembl; ENSSSCT00035035903; ENSSSCP00035014270; ENSSSCG00035027152.
DR Ensembl; ENSSSCT00065005655; ENSSSCP00065002514; ENSSSCG00065004108.
DR GeneID; 397544; -.
DR CTD; 6004; -.
DR VGNC; VGNC:92262; RGS16.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000154304; -.
DR HOGENOM; CLU_059863_3_4_1; -.
DR InParanoid; F1S668; -.
DR OMA; KSPAYQD; -.
DR OrthoDB; 1296189at2759; -.
DR TreeFam; TF315837; -.
DR Reactome; R-SSC-416476; G alpha (q) signalling events.
DR Reactome; R-SSC-418594; G alpha (i) signalling events.
DR Reactome; R-SSC-418597; G alpha (z) signalling events.
DR Proteomes; UP000008227; Chromosome 9.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000015550; Expressed in dorsal plus ventral thalamus and 41 other tissues.
DR ExpressionAtlas; F1S668; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0031224; C:intrinsic component of membrane; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:Ensembl.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.10.196.10; -; 1.
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 GTPase activation; Host-virus interaction; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Reference proteome;
KW Signal transduction inhibitor.
FT CHAIN 1..200
FT /note="Regulator of G-protein signaling 16"
FT /id="PRO_0000445695"
FT DOMAIN 65..181
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT MOD_RES 168
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O15492"
FT MOD_RES 177
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O15492"
FT LIPID 2
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P97428"
FT LIPID 12
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P97428"
FT CONFLICT 148
FT /note="T -> S (in Ref. 2; ABX71210)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="A -> ASA (in Ref. 2; ABX71210)"
FT /evidence="ECO:0000305"
FT CONFLICT 189..192
FT /note="PSSG -> ASSS (in Ref. 2; ABX71210)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 200 AA; 22473 MW; 3D197BBF5B567A19 CRC64;
MCRTLAAFPT TCLERAKEFK TRLGIFLHKS ELGSDPASVG KFEWGSKHSK DGRNFSEDVL
GWRESFDLLL SSKNGVAAFH TFLKTEFSEE NLEFWLACEE FKKLRSATKL ASRAHRIFEE
FIRSEAPKEV NLDHETRELT RTNLQAATAT CFDVAQGKTR TLMEKDSYPR FLKSPAYRDL
AAQAASASPS SGSPAEPSHT
