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pH-response transcription factor pacC/RIM101 [Cleaved into: pH-response transcription factor pacC/RIM101 closed form; pH-response transcription factor pacC/RIM101 open form 1; pH-response transcription factor pacC/RIM101 open form 2]

 PACC_EMENI              Reviewed;         678 AA.
Q00202; C8VJC9; Q5B9C5;
21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
10-OCT-2018, entry version 111.
RecName: Full=pH-response transcription factor pacC/RIM101;
Contains:
RecName: Full=pH-response transcription factor pacC/RIM101 closed form;
Contains:
RecName: Full=pH-response transcription factor pacC/RIM101 open form 1;
Contains:
RecName: Full=pH-response transcription factor pacC/RIM101 open form 2;
Flags: Precursor;
Name=pacC; ORFNames=AN2855;
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
194 / M139) (Aspergillus nidulans).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=227321;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, DNA-BINDING,
AND MUTAGENESIS.
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=7882981;
Tilburn J., Sarkar S., Widdick D.A., Espeso E.A., Orejas M.,
Mungroo J., Penalva M.A., Arst H.N. Jr.;
"The Aspergillus PacC zinc finger transcription factor mediates
regulation of both acid- and alkaline-expressed genes by ambient pH.";
EMBO J. 14:779-790(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=16372000; DOI=10.1038/nature04341;
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
"Sequencing of Aspergillus nidulans and comparative analysis with A.
fumigatus and A. oryzae.";
Nature 438:1105-1115(2005).
[3]
GENOME REANNOTATION.
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
"The 2008 update of the Aspergillus nidulans genome annotation: a
community effort.";
Fungal Genet. Biol. 46:S2-13(2009).
[4]
FUNCTION, AND PROTEOLYTIC PROCESSING.
PubMed=7628696; DOI=10.1101/gad.9.13.1622;
Orejas M., Espeso E.A., Tilburn J., Sarkar S., Arst H.N. Jr.,
Penalva M.A.;
"Activation of the Aspergillus PacC transcription factor in response
to alkaline ambient pH requires proteolysis of the carboxy-terminal
moiety.";
Genes Dev. 9:1622-1632(1995).
[5]
DNA-BINDING.
PubMed=9417928; DOI=10.1006/jmbi.1997.1428;
Espeso E.A., Tilburn J., Sanchez-Pulido L., Brown C.V., Valencia A.,
Arst H.N. Jr., Penalva M.A.;
"Specific DNA recognition by the Aspergillus nidulans three zinc
finger transcription factor PacC.";
J. Mol. Biol. 274:466-480(1997).
[6]
IDENTIFICATION OF PROBABLE INITIATION SITE, AND MUTAGENESIS OF
LEU-259; LEU-266 AND LEU-340.
PubMed=9891072; DOI=10.1128/MCB.19.2.1390;
Mingot J.-M., Tilburn J., Diez E., Bignell E., Orejas M.,
Widdick D.A., Sarkar S., Brown C.V., Caddick M.X., Espeso E.A.,
Arst H.N. Jr., Penalva M.A.;
"Specificity determinants of proteolytic processing of Aspergillus
PacC transcription factor are remote from the processing site, and
processing occurs in yeast if pH signalling is bypassed.";
Mol. Cell. Biol. 19:1390-1400(1999).
[7]
INTRAMOLECULAR INTERACTION, AND MUTAGENESIS OF LEU-340; ARG-573 AND
ARG-579.
PubMed=10675341; DOI=10.1093/emboj/19.4.719;
Espeso E.A., Roncal T., Diez E., Rainbow L., Bignell E., Alvaro J.,
Suarez T., Denison S.H., Tilburn J., Arst H.N. Jr., Penalva M.A.;
"On how a transcription factor can avoid its proteolytic activation in
the absence of signal transduction.";
EMBO J. 19:719-728(2000).
[8]
SUBCELLULAR LOCATION.
PubMed=11238906; DOI=10.1128/MCB.21.5.1688-1699.2001;
Mingot J.-M., Espeso E.A., Diez E., Penalva M.A.;
"Ambient pH signaling regulates nuclear localization of the
Aspergillus nidulans PacC transcription factor.";
Mol. Cell. Biol. 21:1688-1699(2001).
[9]
PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF LEU-498.
PubMed=11889040; DOI=10.1093/emboj/21.6.1350;
Diez E., Alvaro J., Espeso E.A., Rainbow L., Suarez T., Tilburn J.,
Arst H.N. Jr., Penalva M.A.;
"Activation of the Aspergillus PacC zinc finger transcription factor
requires two proteolytic steps.";
EMBO J. 21:1350-1359(2002).
[10]
DNA-BINDING, AND DOMAINS.
PubMed=14636595; DOI=10.1016/j.jmb.2003.09.072;
Fernandez-Martinez J., Brown C.V., Diez E., Tilburn J., Arst H.N. Jr.,
Penalva M.A., Espeso E.A.;
"Overlap of nuclear localisation signal and specific DNA-binding
residues within the zinc finger domain of PacC.";
J. Mol. Biol. 334:667-684(2003).
[11]
INTERACTION WITH PALA, AND MUTAGENESIS OF TYR-455 AND TYR-662.
PubMed=12588984; DOI=10.1128/MCB.23.5.1647-1655.2003;
Vincent O., Rainbow L., Tilburn J., Arst H.N. Jr., Penalva M.A.;
"YPXL/I is a protein interaction motif recognized by Aspergillus PalA
and its human homologue, AIP1/Alix.";
Mol. Cell. Biol. 23:1647-1655(2003).
[12]
FUNCTION IN VIRULENCE.
PubMed=15686555; DOI=10.1111/j.1365-2958.2004.04472.x;
Bignell E., Negrete-Urtasun S., Calcagno A.M., Haynes K.,
Arst H.N. Jr., Rogers T.;
"The Aspergillus pH-responsive transcription factor PacC regulates
virulence.";
Mol. Microbiol. 55:1072-1084(2005).
-!- FUNCTION: Transcription factor that mediates regulation of both
acid- and alkaline-expressed genes in response to ambient pH. At
alkaline ambient pH, activates transcription of alkaline-expressed
genes (including pacC itself) and represses transcription of acid-
expressed genes. Specifically recognizes and binds the consensus
sequence 5'-GCCARG-3'. Required for virulence in invasive
pulmonary aspergillosis (IPA). {ECO:0000269|PubMed:15686555,
ECO:0000269|PubMed:7628696, ECO:0000269|PubMed:7882981}.
-!- SUBUNIT: Binds to DNA. Interacts with palA, which binds to the two
YPX[LI] motifs and is required for proteolytic processing.
{ECO:0000269|PubMed:12588984}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11238906}.
Nucleus {ECO:0000269|PubMed:11238906}. Note=Cytoplasmic at acidic
ambient pH, and nuclear in its processed form at alkaline ambient
pH.
-!- INDUCTION: By alkaline conditions. {ECO:0000269|PubMed:7882981}.
-!- DOMAIN: Only zinc fingers 2 and 3 contact DNA. Zinc finger 1
interacts with zinc finger 2. {ECO:0000269|PubMed:14636595}.
-!- DOMAIN: Interacting regions A, B and C form intramolecular
interactions in the full-length translation product at acidic
ambient pH, keeping the protein in a 'closed' conformation
preventing proteolytic cleavage by the processing protease.
{ECO:0000269|PubMed:14636595}.
-!- PTM: Activated by C-terminal proteolytic cleavage. At neutral to
alkaline ambient pH, the signaling protease (probably palB)
cleaves pacC within the conserved 24-residue signaling protease
box, removing the C-terminal interacting region C and producing a
53 kDa 'open' conformation intermediate protein, which is
committed to further processing. In an ambient pH-independent
reaction, the processing protease (probably the proteasome)
removes additional C-terminal residues to yield the 27 kDa
functional form. {ECO:0000269|PubMed:11889040,
ECO:0000269|PubMed:7628696}.
-!- SIMILARITY: Belongs to the pacC/RIM101 family. {ECO:0000305}.
-!- CAUTION: Met-5 is the major initiator, but Met-1 may also be used.
{ECO:0000305}.
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EMBL; Z47081; CAA87390.1; -; Genomic_DNA.
EMBL; AACD01000051; EAA63426.1; -; Genomic_DNA.
EMBL; BN001306; CBF83867.1; -; Genomic_DNA.
PIR; S54308; S54308.
RefSeq; XP_660459.1; XM_655367.1.
ProteinModelPortal; Q00202; -.
SMR; Q00202; -.
ELM; Q00202; -.
STRING; 162425.CADANIAP00010235; -.
EnsemblFungi; EAA63426; EAA63426; AN2855.2.
GeneID; 2873843; -.
KEGG; ani:AN2855.2; -.
HOGENOM; HOG000198116; -.
InParanoid; Q00202; -.
OrthoDB; EOG092C1EDI; -.
Proteomes; UP000000560; Chromosome VI.
Proteomes; UP000005890; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
Pfam; PF00096; zf-C2H2; 1.
SMART; SM00355; ZnF_C2H2; 3.
SUPFAM; SSF57667; SSF57667; 2.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
1: Evidence at protein level;
Activator; Complete proteome; Cytoplasm; DNA-binding; Metal-binding;
Nucleus; Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 678 pH-response transcription factor
pacC/RIM101 closed form.
/FTId=PRO_0000046832.
CHAIN 1 ?493 pH-response transcription factor
pacC/RIM101 open form 2.
/FTId=PRO_0000312590.
CHAIN 1 ?252 pH-response transcription factor
pacC/RIM101 open form 1.
/FTId=PRO_0000312589.
PROPEP ?253 ?493 Removed in open form 1; by processing
protease.
/FTId=PRO_0000312591.
PROPEP ?494 678 Removed in open form 2; by signaling
protease.
/FTId=PRO_0000312592.
ZN_FING 76 101 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 112 136 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 142 164 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 169 301 Interacting region A.
REGION 252 254 Processing protease cleavage.
REGION 334 410 Interacting region B.
REGION 479 502 Signaling protease box.
REGION 493 500 Signaling protease cleavage.
REGION 529 592 Interacting region C.
MOTIF 158 164 Nuclear localization signal.
MOTIF 455 458 YPX[LI] motif 1.
MOTIF 662 665 YPX[LI] motif 2.
COMPBIAS 41 51 Poly-Ala.
COMPBIAS 593 618 Asp/Gln/Glu-rich (acidic).
MUTAGEN 259 259 L->R: Prevents intramolecular
interactions, resulting in the 'open'
conformation protein committed to
processing independent on ambient pH.
{ECO:0000269|PubMed:9891072}.
MUTAGEN 266 266 L->F: Prevents intramolecular
interactions, resulting in the 'open'
conformation protein committed to
processing independent on ambient pH.
{ECO:0000269|PubMed:9891072}.
MUTAGEN 340 340 L->S: Prevents intramolecular
interactions, resulting in the 'open'
conformation protein committed to
processing independent on ambient pH.
{ECO:0000269|PubMed:10675341,
ECO:0000269|PubMed:9891072}.
MUTAGEN 455 455 Y->D: Abolishes interaction with palA.
Severely reduces proteolytic processing
of the full-length translation product by
signaling protease, causing a stringent
loss-of-function, acidity-mimicking
phenotype. {ECO:0000269|PubMed:12588984}.
MUTAGEN 498 498 L->F: Partially reduces proteolytic
cleavage of the full-length translation
product by signaling protease.
{ECO:0000269|PubMed:11889040}.
MUTAGEN 498 498 L->S: Completely prevents proteolytic
cleavage of the full-length translation
product by signaling protease.
{ECO:0000269|PubMed:11889040}.
MUTAGEN 573 573 R->W: Prevents intramolecular
interactions, resulting in the 'open'
conformation protein committed to
processing independent on ambient pH.
{ECO:0000269|PubMed:10675341}.
MUTAGEN 579 579 R->G,T: Prevents intramolecular
interactions, resulting in the 'open'
conformation protein committed to
processing independent on ambient pH.
{ECO:0000269|PubMed:10675341}.
MUTAGEN 662 662 Y->N: Abolishes interaction with palA.
Partially reduces proteolytic processing
of the full-length translation product by
signaling protease, causing a weak loss-
of-function phenotype.
{ECO:0000269|PubMed:12588984}.
CONFLICT 189 189 G -> F (in Ref. 2; EAA63426/CBF83867).
{ECO:0000305}.
SEQUENCE 678 AA; 72939 MW; 7B626632C8366342 CRC64;
MLGAMAEEAV APVAVPTTQE QPTSQPAAAQ VTTVTSPSVT ATAAAATAAV ASPQANGNAA
SPVAPASSTS RPAEELTCMW QGCSEKLPTP ESLYEHVCER HVGRKSTNNL NLTCQWGSCR
TTTVKRDHIT SHIRVHVPLK PHKCDFCGKA FKRPQDLKKH VKTHADDSVL VRSPEPGSRN
PDMMFGGNGK GYAAAHYFEP ALNPVPSQGY AHGPPQYYQA HHAPQPSNPS YGNVYYALNT
GPEPHQASYE SKKRGYDALN EFFGDLKRRQ FDPNSYAAVG QRLLSLQNLS LPVLTAAPLP
EYQAMPAPVA VASGPYGGGP HPAPAYHLPP MSNVRTKNDL INIDQFLQQM QDTIYENDDN
VAAAGVAQPG AHYIHNGISY RTTHSPPTQL PSAHATTQTT AGPIISNTSA HSPSSSTPAL
TPPSSAQSYT SGRSPISLPS AHRVSPPHES GSSMYPRLPS ATDGMTSGYT AASSAAPPST
LGGIFDNDER RRYTGGTLQR ARPASRAASE SMDLSSDDKE SGERTPKQIS ASLIDPALHS
GSPGEDDVTR TAKAATEVAE RSDVQSEWVE KVRLIEYLRN YIANRLERGE FSDDSEQEQD
QEQEQDQEQE QDQEQGQDRV SRSPVSKADV DMEGVERDSL PRSPRTVPIK TDGESAEDSV
MYPTLRGLDE DGDSKMPS


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