RGS2_YEAST
ID RGS2_YEAST Reviewed; 309 AA.
AC Q99188; D6W2G6;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Regulator of G-protein signaling 2;
GN Name=RGS2; OrderedLocusNames=YOR107W; ORFNames=YOR3224w;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION, INTERACTION WITH GPA2, AND MUTAGENESIS OF ASN-63 AND LEU-144.
RX PubMed=10523302; DOI=10.1093/emboj/18.20.5577;
RA Versele M., de Winde J.H., Thevelein J.M.;
RT "A novel regulator of G protein signalling in yeast, Rgs2, downregulates
RT glucose-activation of the cAMP pathway through direct inhibition of Gpa2.";
RL EMBO J. 18:5577-5591(1999).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
CC -!- FUNCTION: GTPase activating protein for GPA2. Negatively down-regulates
CC glucose-induced cAMP signaling via GPA2. {ECO:0000269|PubMed:10523302}.
CC -!- SUBUNIT: Interacts with GPA2. {ECO:0000269|PubMed:10523302}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
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DR EMBL; X94335; CAA64027.1; -; Genomic_DNA.
DR EMBL; Z75015; CAA99305.1; -; Genomic_DNA.
DR EMBL; AY692864; AAT92883.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10882.1; -; Genomic_DNA.
DR PIR; S61665; S61665.
DR RefSeq; NP_014750.3; NM_001183526.3.
DR AlphaFoldDB; Q99188; -.
DR SMR; Q99188; -.
DR BioGRID; 34503; 47.
DR DIP; DIP-5571N; -.
DR IntAct; Q99188; 2.
DR STRING; 4932.YOR107W; -.
DR PaxDb; Q99188; -.
DR PRIDE; Q99188; -.
DR EnsemblFungi; YOR107W_mRNA; YOR107W; YOR107W.
DR GeneID; 854274; -.
DR KEGG; sce:YOR107W; -.
DR SGD; S000005633; RGS2.
DR VEuPathDB; FungiDB:YOR107W; -.
DR eggNOG; KOG3589; Eukaryota.
DR HOGENOM; CLU_900808_0_0_1; -.
DR InParanoid; Q99188; -.
DR OMA; FANNEVP; -.
DR BioCyc; YEAST:G3O-33638-MON; -.
DR PRO; PR:Q99188; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q99188; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005096; F:GTPase activator activity; IDA:SGD.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IMP:SGD.
DR Gene3D; 1.10.167.10; -; 1.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR Pfam; PF00615; RGS; 1.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..309
FT /note="Regulator of G-protein signaling 2"
FT /id="PRO_0000268701"
FT DOMAIN 37..161
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT REGION 213..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 63
FT /note="N->S: Decreases the ability to suppress glucose-
FT induced cAMP signaling when overexpressed."
FT /evidence="ECO:0000269|PubMed:10523302"
FT MUTAGEN 144
FT /note="L->H: Abolishes the ability to suppress glucose-
FT induced cAMP signaling when overexpressed."
FT /evidence="ECO:0000269|PubMed:10523302"
SQ SEQUENCE 309 AA; 35100 MW; 875CCEA36173EDEC CRC64;
MASVPSLCDI LIPLEKNSRS DGDAESSNTV LIQLRKGHHE RMRSPYTIQK FYKFLKRAHC
EENLEFFEKA HQFLQLKQNR SISEEKLLEV WNKSLYIKYI AVDSPKECNF SQDTREIFEK
CFANNEVPAD VDVLCAISHV MGLLMDGYHR FVSSVNEKKY SATYAHNDSA TEQDLKNEST
TSFSSLGVED ISEDRNSYLK KPDINGLSTI IQETSANTTN ESQCSDRTSR PSESSSSLNT
TSSTYKNTST RNLQKPQNTG ILNSGKGLLQ KLNFVKKRKS FKQPSGVICS HYNSNVQNRL
KGQNSHQQR
