URC2_YEAST
ID URC2_YEAST Reviewed; 772 AA.
AC Q04411; D6VTE1;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Uracil catabolism protein 2;
GN Name=URC2; OrderedLocusNames=YDR520C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
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 [4]
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).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP FUNCTION.
RX PubMed=16464826; DOI=10.1093/nar/gkj493;
RA Titz B., Thomas S., Rajagopala S.V., Chiba T., Ito T., Uetz P.;
RT "Transcriptional activators in yeast.";
RL Nucleic Acids Res. 34:955-967(2006).
CC -!- FUNCTION: Probable transcriptional activator involved in uracil
CC catabolism. {ECO:0000250, ECO:0000269|PubMed:16464826}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 937 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the URC2 family. {ECO:0000305}.
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DR EMBL; U33057; AAB64961.1; -; Genomic_DNA.
DR EMBL; AY692719; AAT92738.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12351.1; -; Genomic_DNA.
DR PIR; S69577; S69577.
DR RefSeq; NP_010808.3; NM_001180828.3.
DR AlphaFoldDB; Q04411; -.
DR SMR; Q04411; -.
DR BioGRID; 32571; 112.
DR DIP; DIP-4849N; -.
DR IntAct; Q04411; 10.
DR MINT; Q04411; -.
DR STRING; 4932.YDR520C; -.
DR MaxQB; Q04411; -.
DR PaxDb; Q04411; -.
DR PRIDE; Q04411; -.
DR EnsemblFungi; YDR520C_mRNA; YDR520C; YDR520C.
DR GeneID; 852133; -.
DR KEGG; sce:YDR520C; -.
DR SGD; S000002928; URC2.
DR VEuPathDB; FungiDB:YDR520C; -.
DR eggNOG; ENOG502QU5T; Eukaryota.
DR HOGENOM; CLU_020222_0_0_1; -.
DR InParanoid; Q04411; -.
DR OMA; TNTLTMF; -.
DR BioCyc; YEAST:G3O-30037-MON; -.
DR PRO; PR:Q04411; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04411; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0019858; P:cytosine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006212; P:uracil catabolic process; ISS:SGD.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; Cytosine metabolism; DNA-binding; Metal-binding;
KW Nucleotide metabolism; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..772
FT /note="Uracil catabolism protein 2"
FT /id="PRO_0000253827"
FT DNA_BIND 72..101
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 772 AA; 88648 MW; A31A93A4B4561DB6 CRC64;
MDINSNASVS PRPDGLPMTA GYNSASGKVR NSIRSIINHP EDSARAKERS ETNSPKNNGN
KKPRKKRKTF SCDTCRRVKT RCDFEPFIGK CYRCNVLQLD CSLARNKDNE ILNTLREDGL
LKKINSINHN LGSFSHLNAD SPNESQSSFE KNGTVNFDNY MIDKRLSSLE EHIKSLHQKM
DLIITTAKMS YNSDIKGPGD DIQNVDFSSN KTYDSRLTSG SETIRKTGEY RKENLFLNGF
KLKESPLKLL HDIDERLFPS KATSKAAKLA GQQRPYAVAR VNFLHFYENN QELCHKLAKE
FLVRSHFWII PGGRKEIDVE YAHSHLFITS VFTIIAMSFA DNDKYAAEQE ILYPLVERLL
TNTLTMFEKL TAFDIEAILY CCMFHISRKA KRYRQLKFNS LVLSNFALNS LLHVIDFYQI
KDRVLVKEVY NPEDLYHLRI LNSLTACYLE YSISYGDIRE QDDMLKEFNK LVAKFPQANF
GDDIKISEIN LGDIVNGIFI NLKNYFAQCL DDFNNDRYGG NADTFIFVFP ELNYWLKNWE
ELLAKDGAGV LLFTFDFYHI MICRTFITEF SSTLKSNQRF LKLILNTMKE HSFSLLNGFL
RLPPTLIRGA PIFTCHQLVY ACLTLCDYLY WFDSSERQRV LSLCTKVYWH LSTIGEKMNE
ATDNVGKIIK SIIDTSKTRI NFGSLSKENS DNDKMSTNAN NYTGAGNLHA AKPATSPTNV
GTLHENLSSS HFMIPDVDQF NSFEDFFQDF FDSLKPNSQK MFTSDKKTEQ TT
