PACC_CANAL
ID PACC_CANAL Reviewed; 661 AA.
AC Q9UW14; A0A1D8PFX3; Q59ZU5;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=pH-response transcription factor pacC/RIM101;
DE AltName: Full=pH-response regulator protein 2;
GN Name=RIM101; Synonyms=HRM101, PRR2; OrderedLocusNames=CAALFM_C114340CA;
GN ORFNames=CaO19.7247;
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 [GENOMIC DNA], AND MUTAGENESIS OF 463-SER--PHE-661.
RC STRAIN=SC5314 / CAI4 / ATCC MYA-682;
RX PubMed=10629054; DOI=10.1128/mcb.20.3.971-978.2000;
RA Davis D.A., Wilson R.B., Mitchell A.P.;
RT "RIM101-dependent and -independent pathways govern pH responses in Candida
RT albicans.";
RL Mol. Cell. Biol. 20:971-978(2000).
RN [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=10601210; DOI=10.1128/jb.181.24.7524-7530.1999;
RA Ramon A.M., Porta A., Fonzi W.A.;
RT "Effect of environmental pH on morphological development of Candida
RT albicans is mediated via the PacC-related transcription factor encoded by
RT PRR2.";
RL J. Bacteriol. 181:7524-7530(1999).
RN [6]
RP MUTAGENESIS OF 476-GLN--PHE-661 AND 584-SER--PHE-661.
RX PubMed=10848590; DOI=10.1128/mcb.20.13.4635-4647.2000;
RA El Barkani A., Kurzai O., Fonzi W.A., Ramon A.M., Porta A., Frosch M.,
RA Muehlschlegel F.A.;
RT "Dominant active alleles of RIM101 (PRR2) bypass the pH restriction on
RT filamentation of Candida albicans.";
RL Mol. Cell. Biol. 20:4635-4647(2000).
RN [7]
RP DNA-BINDING, AND FUNCTION IN TRANSCRIPTIONAL ACTIVATION.
RX PubMed=12912891; DOI=10.1128/ec.2.4.718-728.2003;
RA Ramon A.M., Fonzi W.A.;
RT "Diverged binding specificity of Rim101p, the Candida albicans ortholog of
RT PacC.";
RL Eukaryot. Cell 2:718-728(2003).
RN [8]
RP PROTEOLYTIC PROCESSING.
RX PubMed=15189995; DOI=10.1128/ec.3.3.741-751.2004;
RA Li M., Martin S.J., Bruno V.M., Mitchell A.P., Davis D.A.;
RT "Candida albicans Rim13p, a protease required for Rim101p processing at
RT acidic and alkaline pHs.";
RL Eukaryot. Cell 3:741-751(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. Specifically recognizes and binds the consensus
CC sequence 5'-CCAAGAA-3'. Required for the control of alkaline pH-induced
CC filamentation (dimorphic switch) and virulence.
CC {ECO:0000269|PubMed:10601210, ECO:0000269|PubMed:12912891}.
CC -!- SUBUNIT: Binds to DNA. Interacts with RIM20, which binds to the YPX[LI]
CC motifs and is required for proteolytic processing (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- INDUCTION: By alkaline conditions. {ECO:0000269|PubMed:10601210}.
CC -!- PTM: Activated by C-terminal proteolytic cleavage. At neutral to
CC alkaline ambient pH, the signaling protease (probably RIM13) cleaves
CC RIM101 to yield the 74 kDa functional form. Also exists as a 65 kDa
CC form at acidic pH, which may govern pH-independent processes.
CC {ECO:0000269|PubMed:15189995}.
CC -!- SIMILARITY: Belongs to the pacC/RIM101 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD51714.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF173841; AAD51714.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP017623; AOW27034.1; -; Genomic_DNA.
DR RefSeq; XP_715047.1; XM_709954.1.
DR AlphaFoldDB; Q9UW14; -.
DR BioGRID; 1226374; 1.
DR IntAct; Q9UW14; 1.
DR STRING; 237561.Q9UW14; -.
DR GeneID; 3643280; -.
DR KEGG; cal:CAALFM_C114340CA; -.
DR CGD; CAL0000174156; RIM101.
DR VEuPathDB; FungiDB:C1_14340C_A; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_028624_0_0_1; -.
DR InParanoid; Q9UW14; -.
DR OMA; WENCGTT; -.
DR OrthoDB; 1270413at2759; -.
DR PHI-base; PHI:185; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:CGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071469; P:cellular response to alkaline pH; IMP:CGD.
DR GO; GO:0071280; P:cellular response to copper ion; IMP:CGD.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IMP:CGD.
DR GO; GO:0071285; P:cellular response to lithium ion; IMP:CGD.
DR GO; GO:0036244; P:cellular response to neutral pH; IMP:CGD.
DR GO; GO:0071467; P:cellular response to pH; IDA:CGD.
DR GO; GO:0001410; P:chlamydospore formation; IMP:CGD.
DR GO; GO:0044409; P:entry into host; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:0036171; P:filamentous growth of a population of unicellular organisms in response to chemical stimulus; IMP:CGD.
DR GO; GO:0036178; P:filamentous growth of a population of unicellular organisms in response to neutral pH; IMP:CGD.
DR GO; GO:0036177; P:filamentous growth of a population of unicellular organisms in response to pH; IMP:CGD.
DR GO; GO:0044416; P:induction by symbiont of host defense response; IMP:CGD.
DR GO; GO:1900430; P:positive regulation of filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:1900439; P:positive regulation of filamentous growth of a population of unicellular organisms in response to chemical stimulus; IMP:CGD.
DR GO; GO:0002666; P:positive regulation of T cell tolerance induction; IMP:CGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:CGD.
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 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Repressor; Zinc; Zinc-finger.
FT CHAIN 1..661
FT /note="pH-response transcription factor pacC/RIM101"
FT /id="PRO_0000046824"
FT ZN_FING 208..233
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 244..268
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 274..296
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 626..654
FT /evidence="ECO:0000255"
FT MOTIF 290..296
FT /note="Nuclear localization signal"
FT MOTIF 498..501
FT /note="YPX[LI] motif 1"
FT MOTIF 531..534
FT /note="YPX[LI] motif 2"
FT MOTIF 655..658
FT /note="YPX[LI] motif 3"
FT COMPBIAS 93..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..586
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 463..661
FT /note="Missing: In RIM101-405; is active independent on
FT proteolytic processing. Allows filamentation at alkaline pH
FT in the absence of RIM13 or RIM8 and RIM20."
FT /evidence="ECO:0000269|PubMed:10629054"
FT MUTAGEN 476..661
FT /note="Missing: In CEM-1; dominant active allele that
FT allows filamentation, activates alkaline-expressed and
FT represses acid-expressed genes at acidic pH."
FT /evidence="ECO:0000269|PubMed:10848590"
FT MUTAGEN 584..661
FT /note="Missing: In CEM-2; dominant active allele that
FT allows filamentation, activates alkaline-expressed and
FT represses acid-expressed genes at acidic pH."
FT /evidence="ECO:0000269|PubMed:10848590"
FT CONFLICT 401..407
FT /note="AGSAEFT -> RRFWSSSP (in Ref. 1; AAD51714)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 661 AA; 74695 MW; B3C1C613CD8CAA95 CRC64;
MNYNIHPVTY LNADSNTGAS ESTASHHGSK KSPSSDIDVD NATSPSSFTS SQSPHINAMG
NSPHSSFTSQ SAANSPITDA KQHLVKPTTT KPAAFAPSAN QSNTTASQSY TQPAQQLPTQ
LHPSLNQAYN NQPSYYLHQP TYGYQQQQQQ QQQHQEFNQP SQQYHDHHGY YSNNNILNQN
QPAPQQNPVK PFKKTYKKIR DEDLKGPFKC LWSNCNIIFE TPEILYDHLC DDHVGRKSSN
NLSLTCLWEN CGTTTVKRDH ITSHLRVHVP LKPFHCDLCP KSFKRPQDLK KHSKTHAEDH
PKKLKKAQRE LMKQQQKEAK QQQKLANKRA NSMNATTASD LQLNYYSGNP ADGLNYDDTS
RKRRYENNSQ HNMYVVNSIL NDFNFQQMAQ APQQPGVVGT AGSAEFTTKR MKAGTEYNID
VFNKLNHLDD HLHHHHPQQQ HPQQQYGGNI YEAEKFFNSL SNSIDMQYQN MSTQYQQQHA
GSTFAQQKPT QQASGQLYPS LPTIGNGSYT TSGSSHKEGL VNNHNGYLPS YPQINRSLPY
SSGVAQQPPS ALEFGGVSTY QKSAQSYEED SSDSSEEDDY STSSEDELDT LFDKLNIDDN
KVEEVTIDGF NLKDVAKHRE MIHAVLGYLR NQIEQQEKEK SKEQKEVDVN ETKLYPTITA
F
