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YAP3_YEAST
ID   YAP3_YEAST              Reviewed;         330 AA.
AC   P38749; D3DKQ4;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=AP-1-like transcription factor YAP3;
GN   Name=YAP3; OrderedLocusNames=YHL009C;
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=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
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   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   [4]
RP   FUNCTION, AND MULTIDRUG RESISTANCE.
RX   PubMed=9864335; DOI=10.1128/jb.181.1.231-240.1999;
RA   Talibi D., Raymond M.;
RT   "Isolation of a putative Candida albicans transcriptional regulator
RT   involved in pleiotropic drug resistance by functional complementation of a
RT   pdr1 pdr3 mutation in Saccharomyces cerevisiae.";
RL   J. Bacteriol. 181:231-240(1999).
RN   [5]
RP   FUNCTION, AND MULTIDRUG RESISTANCE.
RX   PubMed=11561289; DOI=10.1002/yea.770;
RA   Yang X., Talibi D., Weber S., Poisson G., Raymond M.;
RT   "Functional isolation of the Candida albicans FCR3 gene encoding a bZip
RT   transcription factor homologous to Saccharomyces cerevisiae Yap3p.";
RL   Yeast 18:1217-1225(2001).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH PDR5.
RX   PubMed=11957110; DOI=10.1007/s10142-001-0040-4;
RA   Subba Rao G., Bachhawat A.K., Gupta C.M.;
RT   "Two-hybrid-based analysis of protein-protein interactions of the yeast
RT   multidrug resistance protein, Pdr5p.";
RL   Funct. Integr. Genomics 1:357-366(2002).
RN   [7]
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   [8]
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   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Transcription activator involved in the regulation of genes
CC       expressed in response to environmental changes. When overexpressed it
CC       activates transcription of the multidrug resistance ABC transporter
CC       PDR5, thus conferring resistance to the fungicide fluconazole (FCZ) and
CC       cycloheximide. When overexpressed, it also confers, independent of
CC       PDR5, increased resistance to 4-nitroquinoline-N-oxide (4-NQO) (By
CC       similarity). Preferentially binds 5'-TTACTAA-3'. {ECO:0000250,
CC       ECO:0000269|PubMed:11561289, ECO:0000269|PubMed:11957110,
CC       ECO:0000269|PubMed:9372930, ECO:0000269|PubMed:9864335}.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with the C-terminal,
CC       cytoplasmic tail of the multidrug resistance ABC transporter PDR5.
CC       {ECO:0000250, ECO:0000269|PubMed:11957110}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:14562095}.
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 1700 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the bZIP family. YAP subfamily. {ECO:0000305}.
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DR   EMBL; U11581; AAB69745.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06677.1; -; Genomic_DNA.
DR   PIR; S46819; S46819.
DR   RefSeq; NP_011854.1; NM_001179089.1.
DR   AlphaFoldDB; P38749; -.
DR   SMR; P38749; -.
DR   BioGRID; 36414; 72.
DR   DIP; DIP-1668N; -.
DR   IntAct; P38749; 10.
DR   MINT; P38749; -.
DR   STRING; 4932.YHL009C; -.
DR   iPTMnet; P38749; -.
DR   MaxQB; P38749; -.
DR   PaxDb; P38749; -.
DR   PRIDE; P38749; -.
DR   EnsemblFungi; YHL009C_mRNA; YHL009C; YHL009C.
DR   GeneID; 856377; -.
DR   KEGG; sce:YHL009C; -.
DR   SGD; S000001001; YAP3.
DR   VEuPathDB; FungiDB:YHL009C; -.
DR   eggNOG; ENOG502S2TX; Eukaryota.
DR   HOGENOM; CLU_071890_0_0_1; -.
DR   InParanoid; P38749; -.
DR   OMA; RSGNENF; -.
DR   BioCyc; YEAST:G3O-31031-MON; -.
DR   PRO; PR:P38749; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P38749; protein.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IC:SGD.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:SGD.
DR   GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR   GO; GO:0036003; P:positive regulation of transcription from RNA polymerase II promoter in response to stress; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA: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; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   1: Evidence at protein level;
KW   Activator; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..330
FT                   /note="AP-1-like transcription factor YAP3"
FT                   /id="PRO_0000076523"
FT   DOMAIN          144..207
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          114..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          147..168
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          172..207
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   COMPBIAS        114..140
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         135
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   330 AA;  37955 MW;  9868389698623A27 CRC64;
     MTPSNMDDNT SGFMKFINPQ CQEEDCCIRN SLFQEDSKCI KQQPDLLSEQ TAPFPILEDQ
     CPALNLDRSN NDLLLQNNIS FPKGSDLQAI QLTPISGDYS TYVMADNNNN DNDSYSNTNY
     FSKNNGISPS SRSPSVAHNE NVPDDSKAKK KAQNRAAQKA FRERKEARMK ELQDKLLESE
     RNRQSLLKEI EELRKANTEI NAENRLLLRS GNENFSKDIE DDTNYKYSFP TKDEFFTSMV
     LESKLNHKGK YSLKDNEIMK RNTQYTDEAG RHVLTVPATW EYLYKLSEER DFDVTYVMSK
     LQGQECCHTH GPAYPRSLID FLVEEATLNE
 
 
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