PACC_CANDC
ID PACC_CANDC Reviewed; 666 AA.
AC Q873Y3; B9WA50;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=pH-response transcription factor pacC/RIM101;
GN Name=RIM101; ORFNames=CD36_13310;
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Eckert S.E., Wicker M., Muehlschlegel F.A.;
RT "Molecular cloning of the Candida dubliniensis Rim101 gene.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(2009).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- PTM: Activated by C-terminal proteolytic cleavage by signaling protease
CC at neutral to alkaline ambient pH. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pacC/RIM101 family. {ECO:0000305}.
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DR EMBL; AY211614; AAO61620.1; -; Genomic_DNA.
DR EMBL; FM992688; CAX45688.1; -; Genomic_DNA.
DR RefSeq; XP_002417970.1; XM_002417925.1.
DR AlphaFoldDB; Q873Y3; -.
DR STRING; 42374.XP_002417970.1; -.
DR EnsemblFungi; CAX45688; CAX45688; CD36_13310.
DR GeneID; 8045521; -.
DR KEGG; cdu:CD36_13310; -.
DR CGD; CAL0000161840; Cd36_13310.
DR VEuPathDB; FungiDB:CD36_13310; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_028624_0_0_1; -.
DR OrthoDB; 1270413at2759; -.
DR Proteomes; UP000002605; Chromosome 1.
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; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 3: Inferred from homology;
KW Activator; Coiled coil; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Repeat; Repressor; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..666
FT /note="pH-response transcription factor pacC/RIM101"
FT /id="PRO_0000046825"
FT ZN_FING 215..240
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 251..275
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 281..303
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 591..660
FT /evidence="ECO:0000255"
FT MOTIF 500..503
FT /note="YPX[LI] motif 1"
FT MOTIF 534..537
FT /note="YPX[LI] motif 2"
FT MOTIF 660..663
FT /note="YPX[LI] motif 3"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..593
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 295
FT /note="D -> N (in Ref. 1; AAO61620)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="Y -> C (in Ref. 1; AAO61620)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 666 AA; 75299 MW; 78BC3890A6CE419A CRC64;
MNYNIHPVTY LNADSSNTGT AETTTQHHHG SKKSPSSDID VDNATSPSSF TSSQSPHINA
MGNSPHSSFT SQSAANSPIT DAKQHLVKTT TNEHKPAAFT PSVGQQPASQ TNTTAPQSYT
QPAQQLPTQL HPSLNQVYNN QPSYYLHQPA YGYQQQPLHQ EYNQQPQQYH DHHGYYANNN
NIPSINELNQ KPPAPVKPFK KTYKKIRDED LKGPFKCLWS NCNIIFETPE ILYDHLCDDH
VGRKSSNNLS LTCLWENCGT TTVKRDHITS HLRVHVPLKP FHCDLCTKSF KRPQDLKKHS
KTHAEDHPKK LKKAQRELMK QQQKEAKQQQ KLANKRANAT TASDLQLNYY SGNPGDGLYD
EASRKRRYEN NSQHNMYVVN SILNDFNFQQ MAQPPQQPGA VSTAVSSEFT TKRMKSGSEY
NIDVFNKLNH LDDHLHHHHP QQNPQQYGGN IYEAEKFFNS LSNSIDMQYQ NMSSQYQQQN
PGVASFAQQK PAQQTNGQLY PSLPTIGNGS YTTSSSSSHK EGLVNNHNGY LPSYPQINRS
LPYSGVAQQP PSALEFGGVS TYQKSAQSYE DSSESSDDDD DDEDDDDYST SSEEELDALF
DKLNIVDKNV EEVTIDGFNL KDVAKHRDMI HSVLVYLRKQ IEQQEKEKSQ EQKDDVNQLY
PTITAF
