PACC_DEBHA
ID PACC_DEBHA Reviewed; 617 AA.
AC Q6BSZ4;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=pH-response transcription factor pacC/RIM101;
GN Name=RIM101; OrderedLocusNames=DEHA2D04796g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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 factor that mediates regulation of both
CC acid- and alkaline-expressed genes in response to ambient pH. At
CC alkaline ambient pH, activates transcription of alkaline-expressed
CC genes (including RIM101 itself) and represses transcription of acid-
CC expressed genes (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to DNA. Interacts with RIM20, which binds to the two
CC YPX[LI] motifs and is required for proteolytic processing (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- PTM: Activated by C-terminal proteolytic cleavage by signaling protease
CC (probably palB/RIM13) at neutral to alkaline ambient pH. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pacC/RIM101 family. {ECO:0000305}.
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DR EMBL; CR382136; CAG86815.2; -; Genomic_DNA.
DR RefSeq; XP_458676.2; XM_458676.1.
DR AlphaFoldDB; Q6BSZ4; -.
DR STRING; 4959.XP_458676.2; -.
DR EnsemblFungi; CAG86815; CAG86815; DEHA2D04796g.
DR GeneID; 2901330; -.
DR KEGG; dha:DEHA2D04796g; -.
DR VEuPathDB; FungiDB:DEHA2D04796g; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_028624_0_0_1; -.
DR InParanoid; Q6BSZ4; -.
DR OMA; THTDSHA; -.
DR OrthoDB; 1270413at2759; -.
DR Proteomes; UP000000599; Chromosome D.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 3: Inferred from homology;
KW Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..617
FT /note="pH-response transcription factor pacC/RIM101"
FT /id="PRO_0000046831"
FT ZN_FING 163..188
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 199..223
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 229..251
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 471..474
FT /note="YPX[LI] motif"
FT /evidence="ECO:0000255"
FT MOTIF 611..614
FT /note="YPX[LI] motif"
FT COMPBIAS 53..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 617 AA; 70169 MW; 1AAA26398708C0EE CRC64;
MSFNLHPISY LDADTNAGRP GNDQGTGNGH GHGAGHEHGN GYRMFDSDLN LDIDGISTGS
PLTSSQSTND SPQSSFTSQS SENSPHQKGE YMKFFGEGDK DIRGSGLSEG SYDVPTMIVE
DEGSVETKIA GGETTSGVDR DDGSVKPKKI YRKVKDEDMK GPFKCHWNDC AVIFDTPELL
YDHLCDDHVG RKSSNNLSLT CYWDNCLVTT VKRDHITSHL RVHVPLKPFH CDVCPKSFKR
PQDLKKHSKI HADDHPKKLK KAHRRQQEEH DHEREYEHEH EHEQEQYRQS HFHNPSHSQP
QSQSHQFQTM QPYPFDNMLN YDINYQMYPS MQSDMAMMND GVDRKRRFDN GNNNMVNNIL
NDFNFHNISA MAPDYSNKKV KVEPSYNLDM FNKLNSFDDR YISSHPHQHQ AQAPPHHAHP
QHQQQQYPNN VNSQNLLEAE KFFNSLSSSI DLQYQKLSTN YQYKPQPQQL YPSVPQISKT
NDNGMGGHNG GVPPNFPQVN RSFNYQANHP ISMEFGGVSN FQKSAKPLEE ASSEDKETDD
AIESLNKLSI NEFKLDDVAK HKQMVDSVIA YLANMKKTIV ANKEIETKSS PEDTYSASQL
SEKEGLSRNL YPKIASF
