PACC_KLULA
ID PACC_KLULA Reviewed; 517 AA.
AC Q6CQ07; Q9Y850;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=pH-response transcription factor pacC/RIM101;
GN Name=RIM101; OrderedLocusNames=KLLA0E00726g;
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 [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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-372.
RC STRAIN=ATCC 76492 / CBS 2359/152 / CLIB 210;
RX PubMed=10669872;
RX DOI=10.1002/1097-0061(20000315)16:4<343::aid-yea534>3.0.co;2-f;
RA Bao W.-G., Fukuhara H.;
RT "The ubiquitin-encoding genes of Kluyveromyces lactis.";
RL Yeast 16:343-351(2000).
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; CR382125; CAG99069.1; -; Genomic_DNA.
DR EMBL; AJ243800; CAB50896.1; -; Genomic_DNA.
DR PIR; T45524; T45524.
DR RefSeq; XP_453982.1; XM_453982.1.
DR AlphaFoldDB; Q6CQ07; -.
DR STRING; 28985.XP_453982.1; -.
DR EnsemblFungi; CAG99069; CAG99069; KLLA0_E00793g.
DR GeneID; 2894720; -.
DR KEGG; kla:KLLA0_E00793g; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_029652_0_0_1; -.
DR InParanoid; Q6CQ07; -.
DR OMA; HITNSSE; -.
DR Proteomes; UP000000598; Chromosome E.
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 Pfam; PF00096; zf-C2H2; 1.
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; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..517
FT /note="pH-response transcription factor pacC/RIM101"
FT /id="PRO_0000046836"
FT ZN_FING 111..136
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 147..171
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 177..199
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 355..358
FT /note="YPX[LI] motif 1"
FT MOTIF 512..515
FT /note="YPX[LI] motif 2"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 517 AA; 57274 MW; 058CD05FABAE16C0 CRC64;
MSPIAHLLNA STGTDSGSHL RDIHGHHDSH DHGSEEQAVS PLSPRSYPSP RSNSSSSCEE
SQSSAGVLAN IHTGPASPHG KACVASSPLS TTGMRSASTP SSSDEDTVHL HRCQWKGCSL
EFTSPELLYH HLCQDHVGRK SQKNLQLNCQ WGDCQTKTVK RDHITSHLRV HVQLKPFACS
TCNKKFKRPQ DLKKHLKVHN EELSLLKKKR GPKPSNKLGK ISNDRSRAHQ RFTLPSISLD
KFIHEEVKTQ QPVYSQQLAE KMAIVLLLPV NNNNATSPPS ASSASSTAVS PNLVSHHMVL
PYQTQQRPLV GHGAELRSAV GFFNNLSMDM SRNYANNNLP TANLGPNPVP APQSYPLIPK
LPSISARPNV GAPPPVLSVF NRFDTHQTSP SSSSSAFYPQ HYSNNYSLHQ RTALLDAEAN
EDIPEKDNVS LEESFTSLNL SSEEQDLELF YETYSTVKLV KDYLLCELME ELDEFKEEEE
EQGFTSFDEF SDSKECVIEG RIPSNKISLS KYPQVVI
