YAP6_YEAST
ID YAP6_YEAST Reviewed; 383 AA.
AC Q03935; D6VSN9; Q03926; Q03931;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=AP-1-like transcription factor YAP6;
GN Name=YAP6; Synonyms=HAL7; OrderedLocusNames=YDR259C;
GN ORFNames=YD9320A.09C, YD9320A.10C;
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 FUNCTION, AND ISOLATION OF YAP FAMILY PROTEINS.
RX PubMed=9372930; DOI=10.1128/mcb.17.12.6982;
RA Fernandes L., Rodrigues-Pousada C., Struhl K.;
RT "Yap, a novel family of eight bZIP proteins in Saccharomyces cerevisiae
RT with distinct biological functions.";
RL Mol. Cell. Biol. 17:6982-6993(1997).
RN [5]
RP FUNCTION, AND SALT TOLERANCE.
RX PubMed=9559673; DOI=10.1016/s0014-5793(98)00249-x;
RA Mendizabal I., Rios G., Mulet J.M., Serrano R., de Larrinoa I.F.;
RT "Yeast putative transcription factors involved in salt tolerance.";
RL FEBS Lett. 425:323-328(1998).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND PLEIOTROPIC DRUG-RESISTANCE.
RX PubMed=11179441; DOI=10.1124/mol.59.3.470;
RA Furuchi T., Ishikawa H., Miura N., Ishizuka M., Kajiya K., Kuge S.,
RA Naganuma A.;
RT "Two nuclear proteins, Cin5 and Ydr259c, confer resistance to cisplatin in
RT Saccharomyces cerevisiae.";
RL Mol. Pharmacol. 59:470-474(2001).
RN [7]
RP FUNCTION, AND IDENTIFICATION OF TARGET PROMOTERS.
RX PubMed=12399584; DOI=10.1126/science.1075090;
RA Lee T.I., Rinaldi N.J., Robert F., Odom D.T., Bar-Joseph Z., Gerber G.K.,
RA Hannett N.M., Harbison C.T., Thompson C.M., Simon I., Zeitlinger J.,
RA Jennings E.G., Murray H.L., Gordon D.B., Ren B., Wyrick J.J., Tagne J.B.,
RA Volkert T.L., Fraenkel E., Gifford D.K., Young R.A.;
RT "Transcriptional regulatory networks in Saccharomyces cerevisiae.";
RL Science 298:799-804(2002).
RN [8]
RP FUNCTION, AND REGULATORY TRANSCRIPTION MODULES.
RX PubMed=14555958; DOI=10.1038/nbt890;
RA Bar-Joseph Z., Gerber G.K., Lee T.I., Rinaldi N.J., Yoo J.Y., Robert F.,
RA Gordon D.B., Fraenkel E., Jaakkola T.S., Young R.A., Gifford D.K.;
RT "Computational discovery of gene modules and regulatory networks.";
RL Nat. Biotechnol. 21:1337-1342(2003).
RN [9]
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).
CC -!- FUNCTION: Transcription activator involved in the regulation of genes
CC expressed in response to environmental changes and metabolic
CC requirements. According to genome-wide promoter binding and gene
CC expression studies it regulates, among others, genes involved in
CC ribosome biogenesis, protein synthesis, carbohydrate metabolism, and
CC carbohydrate transport. It may also be involved in pleiotropic drug
CC resistance. When overexpressed, it confers resistance to cisplatin,
CC methylmethanosulfonate, and mitomycin C, and increases cellular
CC tolerance to sodium and lithium. {ECO:0000269|PubMed:11179441,
CC ECO:0000269|PubMed:12399584, ECO:0000269|PubMed:14555958,
CC ECO:0000269|PubMed:9372930, ECO:0000269|PubMed:9559673}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11179441}.
CC -!- INDUCTION: Seems to activate its own expression and that of the
CC repressor ROX1 which in turn represses YAP6 expression.
CC -!- MISCELLANEOUS: One of 8 closely related fungi-specific YAP proteins
CC (YAP1 to YAP8), which all seem to be transcription activators of the
CC environmental stress response and metabolism control pathways and to
CC have similar but not identical DNA binding specificities.
CC -!- MISCELLANEOUS: Present with 1400 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the bZIP family. YAP subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA92717.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z70202; CAA94098.1; -; Genomic_DNA.
DR EMBL; Z68329; CAA92716.1; -; Genomic_DNA.
DR EMBL; Z68329; CAA92717.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AY557790; AAS56116.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12099.1; -; Genomic_DNA.
DR PIR; S67462; S67462.
DR RefSeq; NP_010545.3; NM_001180567.3.
DR AlphaFoldDB; Q03935; -.
DR SMR; Q03935; -.
DR BioGRID; 32309; 87.
DR DIP; DIP-4253N; -.
DR IntAct; Q03935; 14.
DR MINT; Q03935; -.
DR STRING; 4932.YDR259C; -.
DR iPTMnet; Q03935; -.
DR MaxQB; Q03935; -.
DR PaxDb; Q03935; -.
DR PRIDE; Q03935; -.
DR EnsemblFungi; YDR259C_mRNA; YDR259C; YDR259C.
DR GeneID; 851846; -.
DR KEGG; sce:YDR259C; -.
DR SGD; S000002667; YAP6.
DR VEuPathDB; FungiDB:YDR259C; -.
DR eggNOG; ENOG502SC5V; Eukaryota.
DR GeneTree; ENSGT00940000176707; -.
DR HOGENOM; CLU_077201_0_0_1; -.
DR InParanoid; Q03935; -.
DR OMA; PYRINPT; -.
DR BioCyc; YEAST:G3O-29830-MON; -.
DR PRO; PR:Q03935; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03935; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0001010; F:RNA polymerase II sequence-specific DNA-binding transcription factor recruiting activity; IPI:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF00170; bZIP_1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..383
FT /note="AP-1-like transcription factor YAP6"
FT /id="PRO_0000076526"
FT DOMAIN 221..284
FT /note="bZIP"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..247
FT /note="Basic motif"
FT /evidence="ECO:0000250"
FT REGION 249..277
FT /note="Leucine-zipper"
FT /evidence="ECO:0000250"
FT COMPBIAS 168..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 383 AA; 43597 MW; 396C20006DEB7319 CRC64;
MQNPPLIRPD MYNQGSSSMA TYNASEKNLN EHPSPQIAQP STSQKLPYRI NPTTTNGDTD
ISVNSNPIQP PLPNLMHLSG PSDYRSMHQS PIHPSYIIPP HSNERKQSAS YNRPQNAHVS
IQPSVVFPPK SYSISYAPYQ INPPLPNGLP NQSISLNKEY IAEEQLSTLP SRNTSVTTAP
PSFQNSADTA KNSADNNDNN DNVTKPVPDK DTQLISSSGK TLRNTRRAAQ NRTAQKAFRQ
RKEKYIKNLE QKSKIFDDLL AENNNFKSLN DSLRNDNNIL IAQHEAIRNA ITMLRSEYDV
LCNENNMLKN ENSIIKNEHN MSRNENENLK LENKRFHAEY IRMIEDIENT KRKEQEQRDE
IEQLKKKIRS LEEIVGRHSD SAT
