RGS19_MOUSE
ID RGS19_MOUSE Reviewed; 216 AA.
AC Q9CX84; Q99L50;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Regulator of G-protein signaling 19;
DE Short=RGS19;
GN Name=Rgs19;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AK019401; BAB31703.1; -; mRNA.
DR EMBL; BC003838; AAH03838.1; -; mRNA.
DR CCDS; CCDS17220.1; -.
DR RefSeq; NP_001278135.1; NM_001291206.1.
DR RefSeq; NP_001278136.1; NM_001291207.1.
DR RefSeq; NP_001278138.1; NM_001291209.1.
DR RefSeq; NP_001278139.1; NM_001291210.1.
DR RefSeq; NP_080722.1; NM_026446.4.
DR AlphaFoldDB; Q9CX84; -.
DR SMR; Q9CX84; -.
DR BioGRID; 208006; 2.
DR IntAct; Q9CX84; 2.
DR MINT; Q9CX84; -.
DR STRING; 10090.ENSMUSP00000002532; -.
DR iPTMnet; Q9CX84; -.
DR PhosphoSitePlus; Q9CX84; -.
DR SwissPalm; Q9CX84; -.
DR EPD; Q9CX84; -.
DR jPOST; Q9CX84; -.
DR MaxQB; Q9CX84; -.
DR PaxDb; Q9CX84; -.
DR PRIDE; Q9CX84; -.
DR ProteomicsDB; 255252; -.
DR Antibodypedia; 29985; 471 antibodies from 28 providers.
DR DNASU; 56470; -.
DR Ensembl; ENSMUST00000002532; ENSMUSP00000002532; ENSMUSG00000002458.
DR Ensembl; ENSMUST00000108776; ENSMUSP00000104406; ENSMUSG00000002458.
DR Ensembl; ENSMUST00000165416; ENSMUSP00000129026; ENSMUSG00000002458.
DR GeneID; 56470; -.
DR KEGG; mmu:56470; -.
DR UCSC; uc008onc.2; mouse.
DR CTD; 10287; -.
DR MGI; MGI:1915153; Rgs19.
DR VEuPathDB; HostDB:ENSMUSG00000002458; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000160391; -.
DR InParanoid; Q9CX84; -.
DR OMA; MSQHETS; -.
DR PhylomeDB; Q9CX84; -.
DR TreeFam; TF315837; -.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 56470; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Rgs19; mouse.
DR PRO; PR:Q9CX84; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9CX84; protein.
DR Bgee; ENSMUSG00000002458; Expressed in granulocyte and 251 other tissues.
DR ExpressionAtlas; Q9CX84; baseline and differential.
DR Genevisible; Q9CX84; MM.
DR GO; GO:0005903; C:brush border; ISO:MGI.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:MGI.
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 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_0000204230"
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 /evidence="ECO:0000250"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70521"
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 CONFLICT 82
FT /note="K -> E (in Ref. 2; AAH03838)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 216 AA; 24678 MW; 4F166A6607184F31 CRC64;
MPTPHEAEKQ HTGPEEADRP PSMSSHDAAP SGPPSRNPCC LCWCCCCSCS WNQERQRAWQ
VSRESKLQPL PSCEVCTPPS PKEVQSWAQS FDKLMHSPTG RSVFRAFLRT EYSEENMLFW
LACEELKAEA NQHVVDEKAR LIYEDYVSIL SPKEVSLDSR VREGINRKMQ EPSPHTFDDA
QLQIYTLMHR DSYPRFLTSP TYRSLLLQGA PQSSEA
