AP1_KLULA
ID AP1_KLULA Reviewed; 583 AA.
AC P56095;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=AP-1-like transcription factor YAP1 {ECO:0000305};
GN Name=YAP1; OrderedLocusNames=KLLA0A01760g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=9439570; DOI=10.1007/s004380050624;
RA Billard P., Dumond H., Bolotin-Fukuhara M.;
RT "Characterization of an AP-1-like transcription factor that mediates an
RT oxidative stress response in Kluyveromyces lactis.";
RL Mol. Gen. Genet. 257:62-70(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Transcription activator involved in oxidative stress response
CC and cadmium resistance (PubMed:9439570). Regulates the transcription of
CC genes encoding antioxidant enzymes and components of the cellular
CC thiol-reducing pathways. Activity of the transcription factor is
CC controlled through oxidation of specific cysteine residues resulting in
CC the alteration of its subcellular location. Activation by alkyl
CC hydroperoxides or cadmium induces nuclear accumulation and as a result
CC YAP1 transcriptional activity (By similarity).
CC {ECO:0000250|UniProtKB:P19880, ECO:0000269|PubMed:9439570}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P19880}. Cytoplasm
CC {ECO:0000250|UniProtKB:P19880}. Note=Oxidized YAP1 is found
CC predominantly in the nucleus, while reduced YAP1 is continuously
CC exported to the cytoplasm by CRM1/exportin 1.
CC {ECO:0000250|UniProtKB:P19880}.
CC -!- DOMAIN: Contains two cysteine rich domains (CRD), referred to as the
CC N- and C-terminal CRD's, n-CRD (Cys-265 and Cys-272) and c-CRD (Cys-
CC 531, Cys-553 and Cys-562), respectively. A nuclear export signal is
CC embedded in the c-CRD, with which the nuclear export protein
CC CRM1/exportin 1 interacts only in the absence of disulfide bonds (or
CC otherwise oxidized cysteines) within the c-CRD or between the c-CRD and
CC the n-CRD. {ECO:0000250|UniProtKB:P19880}.
CC -!- PTM: Oxidative stress induces conformational changes through oxidation
CC of cysteine residues, masking the nuclear export signal, thus
CC abolishing nuclear export by CRM1/exportin 1.
CC {ECO:0000250|UniProtKB:P19880}.
CC -!- SIMILARITY: Belongs to the bZIP family. YAP subfamily. {ECO:0000305}.
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DR EMBL; AF006499; AAC39320.1; -; Genomic_DNA.
DR EMBL; CR382121; CAH02665.1; -; Genomic_DNA.
DR RefSeq; XP_451077.1; XM_451077.1.
DR AlphaFoldDB; P56095; -.
DR SMR; P56095; -.
DR STRING; 28985.XP_451077.1; -.
DR PRIDE; P56095; -.
DR EnsemblFungi; CAH02665; CAH02665; KLLA0_A01760g.
DR GeneID; 2896569; -.
DR KEGG; kla:KLLA0_A01760g; -.
DR eggNOG; ENOG502RPD7; Eukaryota.
DR HOGENOM; CLU_032750_0_0_1; -.
DR InParanoid; P56095; -.
DR OMA; DFFTPYN; -.
DR Proteomes; UP000000598; Chromosome A.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:EnsemblFungi.
DR GO; GO:1900101; P:regulation of endoplasmic reticulum unfolded protein response; IEA:EnsemblFungi.
DR GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IEA:EnsemblFungi.
DR GO; GO:0009408; P:response to heat; IEA:EnsemblFungi.
DR GO; GO:0000304; P:response to singlet oxygen; IEA:EnsemblFungi.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:EnsemblFungi.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR013910; TF_PAP1.
DR InterPro; IPR023167; Yap1_redox_dom_sf.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF08601; PAP1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF111430; SSF111430; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 3: Inferred from homology;
KW Activator; Cytoplasm; Disulfide bond; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..583
FT /note="AP-1-like transcription factor YAP1"
FT /id="PRO_0000076531"
FT DOMAIN 51..114
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..77
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 79..86
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 177..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..272
FT /note="n-CRD"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT REGION 275..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..562
FT /note="c-CRD"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT MOTIF 41..48
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 120..127
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 547..554
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT COMPBIAS 36..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 265..531
FT /note="In nuclear retained form"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT DISULFID 272..562
FT /note="In nuclear retained form"
FT /evidence="ECO:0000250|UniProtKB:P19880"
SQ SEQUENCE 583 AA; 63886 MW; A4A96B12D7F5C983 CRC64;
MSTSTAKRPF DNKRAGSPDD GTDSDSGGNN SGSSPASKRR ERKPGRKPLE TEAKDKRTAQ
NRAAQRAFRE RRERKMKELE DKVSQLESLN KQSELETKFL RNQVTNLLSE LKRYNPELPK
KRDSILLDYL AKQRKASIDS NPDFSAAANK AANSKDSSTA ISSSNFQFEF PWKMDPSKIP
SPSSDSTSPS ASTSILDNAN NKSVSSTNLN HSRSSISNSS SSPSNVNGLS SRKHSNTLNL
YQTQSNVTSE FDFDSQFDES VSSFCSKLSM ACGTKSNPIP KASPVSTPSS SDLLKPKSNS
NVNITNHNNN KINSKDLSSS APLHDSASAS ALNNHDSVNA VSNQFSVDKQ YNDSSHSQAT
PNGLDNDSSV SAWQQPSFGQ LGFRTDQLFD LDLDSASPIT KQKDNNYSTT TNNTNSPAKA
DGMYWNFNTP LSNMVSRNMQ NPEIPFIDTG LAFPDYDDPL LDILKEEQEN EQVEGDSDPI
QALINEEPSM PLCHDPAANA GASVSETDKL SNQEEIVQDI IPSNDGKLLK CSEVWDRITA
HPRYSDLDID GLCLELRTKA KCSEKGVVVN AEDVQKALIS HMQ
