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Protein

AP-1-like transcription factor YAP2

Gene

CAD1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcription activator involved in oxidative stress response and cadmium resistance. Regulates the transcription of genes overrepresented for the function of stabilizing proteins including the inducible Hsp90-family protein HSP82. Preferentially binds to promoters with the core binding site 5'-TTA[CG]TAA-3'. Activity of the transcription factor is controlled through oxidation of specific cysteine residues resulting in the alteration of its subcellular location. Activation by alkyl hydroperoxides or cadmium induces nuclear accumulation and as a result CAD1/YAP2 transcriptional activity.8 Publications

Miscellaneous

One of 8 closely related fungi-specific YAP proteins (YAP1 to YAP8), which all seem to be transcription activators of the environmental stress response and metabolism control pathways and to have similar but not identical DNA binding specificities.1 Publication
Present with 623 molecules/cell in log phase SD medium.1 Publication

GO - Molecular functioni

GO - Biological processi

  • cellular response to cadmium ion Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter in response to stress Source: SGD

Keywordsi

Molecular functionActivator, DNA-binding
Biological processCadmium resistance, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-29964-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
AP-1-like transcription factor YAP2Curated
Alternative name(s):
Cadmium resistance protein 11 Publication
Transcription factor CAD1
Gene namesi
Name:CAD11 Publication
Synonyms:YAP21 Publication
Ordered Locus Names:YDR423CImported
ORF Names:D9461.12
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR423C.
SGDiS000002831. CAD1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • nucleus Source: SGD

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Hypersensitive to the cytotoxic metal cadmium.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi356C → A: Only partially accumulates in the nucleus in response to cadmium. Does not accumulate in the nucleus; when associated with A-387. 1 Publication1
Mutagenesisi378C → A: No effect. 1 Publication1
Mutagenesisi387C → A: Only partially accumulates in the nucleus in response to cadmium. Does not accumulate in the nucleus; when associated with A-356. 1 Publication1
Mutagenesisi391C → A: Does not accumulate in the nucleus in response to cadmium. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000765221 – 409AP-1-like transcription factor YAP2Add BLAST409

Post-translational modificationi

Depending on the oxidative stress inducing agent, CAD1/YAP2 can undergo two distinct conformational changes, both through oxidation of cysteine residues, and both masking the nuclear export signal, thus abolishing nuclear export by CRM1/exportin 1. Peroxide stress induces the formation of possible intramolecular disulfide bonds as well as intermolcular disulfide within a homodimer. Cadmium may bind directly to specific cysteine residues (Cys-391 and either Cys-356 or Cys-387) in the c-CRD.2 Publications

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP24813.
PRIDEiP24813.

Expressioni

Inductioni

CAD1/YAP2 expression is at least partially regulated at the level of mRNA stability. Two small upstream open reading frames (uORF) in its mRNA cause increased RNA decay. The translation initiation factor eIF2 counteracts this effect by causing reinitiation at the functional initiation site, thus suppressing RNA decay.1 Publication

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation (Probable). Interacts in the nucleus with the nuclear export protein CRM1 (PubMed:17187783). Interacts with RCK1 (PubMed:15341652).1 Publication2 Publications

Protein-protein interaction databases

BioGridi32482. 67 interactors.
DIPiDIP-4491N.
IntActiP24813. 4 interactors.
MINTiMINT-539300.
STRINGi4932.YDR423C.

Structurei

3D structure databases

ProteinModelPortaliP24813.
SMRiP24813.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini43 – 106bZIPPROSITE-ProRule annotationAdd BLAST64

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni46 – 69Basic motifPROSITE-ProRule annotationAdd BLAST24
Regioni71 – 99Leucine-zipperPROSITE-ProRule annotationAdd BLAST29
Regioni356 – 387c-CRDBy similarityAdd BLAST32

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi17 – 24Bipartite nuclear localization signalPROSITE-ProRule annotation8
Motifi47 – 54Bipartite nuclear localization signalPROSITE-ProRule annotation8
Motifi372 – 379Nuclear export signalBy similarity8

Domaini

Contains a C-terminal cysteine rich domain (c-CRD), but lacks the N-terminal CRD (n-CRD) found in its paralog YAP1. It probably also contains embedded in the c-CRD a nuclear export signal, with which the nuclear export protein CRM1/exportin 1 may interact in the absence of inter- or intramolecular disulfide bonds (or otherwise oxidized/modified cysteines) within the c-CRD.By similarity1 Publication

Sequence similaritiesi

Belongs to the bZIP family. YAP subfamily.Curated

Phylogenomic databases

GeneTreeiENSGT00530000069148.
InParanoidiP24813.
KOiK09043.
OrthoDBiEOG092C4KCZ.

Family and domain databases

Gene3Di1.10.238.100. 1 hit.
InterProiView protein in InterPro
IPR004827. bZIP.
IPR013910. TF_PAP1.
IPR023167. Yap1_redox_dom.
PfamiView protein in Pfam
PF00170. bZIP_1. 1 hit.
PF08601. PAP1. 1 hit.
SMARTiView protein in SMART
SM00338. BRLZ. 1 hit.
SUPFAMiSSF111430. SSF111430. 1 hit.
PROSITEiView protein in PROSITE
PS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.

Sequencei

Sequence statusi: Complete.

P24813-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNILRKGQQ IYLAGDMKKQ MLLNKDGTPK RKVGRPGRKR IDSEAKSRRT
60 70 80 90 100
AQNRAAQRAF RDRKEAKMKS LQERVELLEQ KDAQNKTTTD FLLCSLKSLL
110 120 130 140 150
SEITKYRAKN SDDERILAFL DDLQEQQKRE NEKGTSTAVS KAAKELPSPN
160 170 180 190 200
SDENMTVNTS IEVQPHTQEN EKVMWNIGSW NAPSLTNSWD SPPGNRTGAV
210 220 230 240 250
TIGDESINGS EMPDFSLDLV SNDRQTGLEA LDYDIHNYFP QHSERLTAEK
260 270 280 290 300
IDTSACQCEI DQKYLPYETE DDTLFPSVLP LAVGSQCNNI CNRKCIGTKP
310 320 330 340 350
CSNKEIKCDL ITSHLLNQKS LASVLPVAAS HTKTIRTQSE AIEHISSAIS
360 370 380 390 400
NGKASCYHIL EEISSLPKYS SLDIDDLCSE LIIKAKCTDD CKIVVKARDL

QSALVRQLL
Length:409
Mass (Da):45,752
Last modified:October 1, 1993 - v2
Checksum:i21133AAAF40B0ED7
GO

Sequence cautioni

The sequence AAA34463 differs from that shown. Reason: Frameshift at positions 286 and 339.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti36P → L in AAA34463 (PubMed:1514324).Curated1
Sequence conflicti90D → N in AAA34463 (PubMed:1514324).Curated1
Sequence conflicti102E → K in AAA34463 (PubMed:1514324).Curated1
Sequence conflicti125E → Q in AAA34463 (PubMed:1514324).Curated1
Sequence conflicti131N → D in AAA34463 (PubMed:1514324).Curated1
Sequence conflicti142A → V in AAA34463 (PubMed:1514324).Curated1
Sequence conflicti145E → G in AAA34463 (PubMed:1514324).Curated1
Sequence conflicti327V → L in AAB29937 (PubMed:8107671).Curated1
Sequence conflicti337T → I in AAB29937 (PubMed:8107671).Curated1
Sequence conflicti347S → I in AAB29937 (PubMed:8107671).Curated1
Sequence conflicti354A → P in AAB29937 (PubMed:8107671).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14289 Unassigned DNA. Translation: AAA02920.1.
X69106 mRNA. Translation: CAA48858.1.
S68847 Genomic DNA. Translation: AAB29937.1.
U33007 Genomic DNA. Translation: AAB64878.1.
M58331 Genomic DNA. Translation: AAA34463.1. Frameshift.
BK006938 Genomic DNA. Translation: DAA12263.1.
PIRiA48890.
RefSeqiNP_010711.3. NM_001180731.3.

Genome annotation databases

EnsemblFungiiYDR423C; YDR423C; YDR423C.
GeneIDi852033.
KEGGisce:YDR423C.

Similar proteinsi

Entry informationi

Entry nameiAP2_YEAST
AccessioniPrimary (citable) accession number: P24813
Secondary accession number(s): D6VT53, Q02259
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: October 1, 1993
Last modified: August 30, 2017
This is version 165 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names