RPN4_CANAL
ID RPN4_CANAL Reviewed; 536 AA.
AC Q59VM4; A0A1D8PD90;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Transcriptional regulator RPN4;
GN Name=RPN4; OrderedLocusNames=CAALFM_C104330WA; ORFNames=CaO19.1069;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=15534694; DOI=10.1371/journal.pbio.0020398;
RA Gasch A.P., Moses A.M., Chiang D.Y., Fraser H.B., Berardini M., Eisen M.B.;
RT "Conservation and evolution of cis-regulatory systems in ascomycete
RT fungi.";
RL PLoS Biol. 2:E398-E398(2004).
RN [5]
RP INDUCTION.
RX PubMed=16339080; DOI=10.1091/mbc.e05-06-0501;
RA Enjalbert B., Smith D.A., Cornell M.J., Alam I., Nicholls S., Brown A.J.P.,
RA Quinn J.;
RT "Role of the Hog1 stress-activated protein kinase in the global
RT transcriptional response to stress in the fungal pathogen Candida
RT albicans.";
RL Mol. Biol. Cell 17:1018-1032(2006).
RN [6]
RP INDUCTION.
RX PubMed=21592964; DOI=10.1074/jbc.m111.233569;
RA Singh R.P., Prasad H.K., Sinha I., Agarwal N., Natarajan K.;
RT "Cap2-HAP complex is a critical transcriptional regulator that has dual but
RT contrasting roles in regulation of iron homeostasis in Candida albicans.";
RL J. Biol. Chem. 286:25154-25170(2011).
RN [7]
RP INDUCTION.
RX PubMed=22265407; DOI=10.1016/j.cell.2011.10.048;
RA Nobile C.J., Fox E.P., Nett J.E., Sorrells T.R., Mitrovich Q.M.,
RA Hernday A.D., Tuch B.B., Andes D.R., Johnson A.D.;
RT "A recently evolved transcriptional network controls biofilm development in
RT Candida albicans.";
RL Cell 148:126-138(2012).
CC -!- FUNCTION: Transcriptional activator of a number of genes encoding
CC proteasomal subunits. Binds to the DNA sequence 5'-GAAGGCAAAA-3',
CC enriched in regions upstream of proteasome genes.
CC {ECO:0000269|PubMed:15534694}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- INDUCTION: Expression is induced by HAP43, by osmotic stress, by
CC oxidative stress, by heavy metal stress, and during biofilm formation.
CC {ECO:0000269|PubMed:16339080, ECO:0000269|PubMed:21592964,
CC ECO:0000269|PubMed:22265407}.
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DR EMBL; CP017623; AOW26107.1; -; Genomic_DNA.
DR RefSeq; XP_713673.1; XM_708580.2.
DR AlphaFoldDB; Q59VM4; -.
DR STRING; 237561.Q59VM4; -.
DR GeneID; 3644684; -.
DR KEGG; cal:CAALFM_C104330WA; -.
DR CGD; CAL0000195107; RPN4.
DR VEuPathDB; FungiDB:C1_04330W_A; -.
DR eggNOG; ENOG502RBAK; Eukaryota.
DR HOGENOM; CLU_024993_0_0_1; -.
DR InParanoid; Q59VM4; -.
DR OMA; DDDNYFQ; -.
DR OrthoDB; 1361991at2759; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:CGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:CGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:CGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:CGD.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Stress response; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..536
FT /note="Transcriptional regulator RPN4"
FT /id="PRO_0000426064"
FT ZN_FING 440..471
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 154..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 536 AA; 60153 MW; FCB82332A4C8F715 CRC64;
MTSLAILPQL KRTITDIMDE ELYQSPSSPN SMTSFPSGTG NLMSNTNHNT FNQSNNTPFN
MNYNHISNRN SINSSPNLSA TTFNNANNLG NVLNIPDSFL EQLASQDYID HLKSQQQQEQ
AFENPDDIYV QDVHENQVNP FNDYGNPDSF IRAQEQQSQL PQPQQPISQQ DKQRPQSQQQ
QATKAPLPQA FPTRRRRKIT LLNDIGGSST RKKHFDEDYL LYNPDISPGH IVTDCSLDSS
LVIPPNSNEL FLTESESPEF ANDIIPGYEN DYLFLDDDDE QIEEDVSDDE GDNYFQVDED
FDDYLMNNNG YDGYPTFNNY ESSGNNTDII NNNNNIVDET ISDANSNSEL EVVFDQPKEV
SPSAISPASP DSDDMMIDVE DETEIADATA AKEEINKKHS KSGKKESKSQ KENQLTTTTK
SKKHSHGISG AEITLNNPNH QCNLINPSTG EPCNKQFSRP YDLIRHQDTI HASMKKIFRC
VICEGRLNGG PGNGKEKTFS RGDALSRHIK IKHGLVGQDA LDLINEAKEN VEYIPV