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IFH1_CANAL
ID   IFH1_CANAL              Reviewed;         885 AA.
AC   Q5AG97; A0A1D8PNH2; Q5AGN3;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 2.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Transcriptional regulator IFH1;
GN   Name=IFH1; OrderedLocusNames=CAALFM_C502650CA;
GN   ORFNames=CaO19.11758, CaO19.4282;
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 [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   [2]
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   [3]
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   [4]
RP   FUNCTION.
RX   PubMed=20231876; DOI=10.1371/journal.pbio.1000329;
RA   Lavoie H., Hogues H., Mallick J., Sellam A., Nantel A., Whiteway M.;
RT   "Evolutionary tinkering with conserved components of a transcriptional
RT   regulatory network.";
RL   PLoS Biol. 8:E1000329-E1000329(2010).
RN   [5]
RP   INDUCTION.
RX   PubMed=22265407; DOI=10.1016/j.cell.2011.10.048;
RA   Nobile C.J., Fox E.P., Nett J.E., Sorrells T.R., Mitrovich Q.M.,
RA   Hernday A.D., Tuch B.B., Andes D.R., Johnson A.D.;
RT   "A recently evolved transcriptional network controls biofilm development in
RT   Candida albicans.";
RL   Cell 148:126-138(2012).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH FLH1 AND TBF1.
RX   PubMed=23625919; DOI=10.1074/jbc.m112.436683;
RA   Mallick J., Whiteway M.;
RT   "The evolutionary rewiring of the ribosomal protein transcription pathway
RT   modifies the interaction of transcription factor heteromer Ifh1-Fhl1
RT   (interacts with forkhead 1-forkhead-like 1) with the DNA-binding
RT   specificity element.";
RL   J. Biol. Chem. 288:17508-17519(2013).
CC   -!- FUNCTION: In complex with IFH1, acts as a transcriptional regulator of
CC       rRNA and ribosomal protein genes. The FHL1-IFH1 complex is targeted to
CC       the ribosomal protein genes by the DNA-binding factor TBF1.
CC       {ECO:0000269|PubMed:20231876, ECO:0000269|PubMed:23625919}.
CC   -!- SUBUNIT: Interacts with FLH1 and TBF1. {ECO:0000269|PubMed:23625919}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- INDUCTION: Induced during biofilm formation.
CC       {ECO:0000269|PubMed:22265407}.
CC   -!- SIMILARITY: Belongs to the IFH1 family. {ECO:0000305}.
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DR   EMBL; CP017627; AOW29690.1; -; Genomic_DNA.
DR   RefSeq; XP_720590.2; XM_715497.2.
DR   AlphaFoldDB; Q5AG97; -.
DR   STRING; 237561.Q5AG97; -.
DR   GeneID; 3637770; -.
DR   KEGG; cal:CAALFM_C502650CA; -.
DR   CGD; CAL0000182191; IFH1.
DR   VEuPathDB; FungiDB:C5_02650C_A; -.
DR   eggNOG; ENOG502QQB6; Eukaryota.
DR   HOGENOM; CLU_910745_0_0_1; -.
DR   OrthoDB; 1166731at2759; -.
DR   PRO; PR:Q5AG97; -.
DR   Proteomes; UP000000559; Chromosome 5.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0060962; P:regulation of ribosomal protein gene transcription by RNA polymerase II; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR018837; TF_CRF1/IFH1.
DR   PANTHER; PTHR28057; PTHR28057; 1.
DR   Pfam; PF10380; CRF1; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..885
FT                   /note="Transcriptional regulator IFH1"
FT                   /id="PRO_0000426085"
FT   REGION          1..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          150..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          234..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          465..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          680..708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          813..835
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..79
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..376
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..407
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..505
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..586
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..618
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        621..639
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   885 AA;  98826 MW;  F29CDE4A7D9BEB8B CRC64;
     MGYKNSDNTN NKFSRKSMSP SLTGGKGRKT VGKKVKKTIP RKTVNWSSYD VNSDSNEDSD
     EESENENDSD NDDEDDDETE HHHLDGLYSL MGKRPHDSSS NGDDDDDDDD DNDNKNIFSS
     TSSDGDSDEA MFSSSDDDSD VDFVKLQAQQ KAHALKIAKA RKGLKSKPKN ESNDNAIASS
     SESESNSESD NEDDDDDVVS LKKLKPRKKS FLKYGRRRSD AVLPDINFKF EFDTGENDEL
     EAGNQETHIK EPEEEDIGEE VDYSPENPVD SNNVPSLEFE FDHHLIEVPK INEEELNSDE
     DYEIDDNELL ATLQAENDAE EFLPPITKGN SQPQRNDSLI SSTIEEEEND NDNEEASKGG
     DGDDDDDDDD DENDPFLKEE EKYLVNEFET NGFDENEEDE DEDDLHTFDS DFSTTNRIVN
     SFKGIGEDRS KPIVKYESSV SGGSDYDEDD YIDLINFDVP LFDDKNGHLD GGKKNSHHKG
     NTDKLKKDKV KQRANSNHNS DEDDDSYLWN YFFSSDNDSS SEETDDKNNS KTVNKSRKNK
     KNKKALTNNA ITGADELFEQ IENDNTFKSK SKSNHHGNSL YKAYSDSPMT IQDLEAEIRA
     GADDDDDDDD DYDSSESTDV DESLPKSSSN NSLVGSSKKA TEVLSSKTAD YRPPKLGSWV
     TVDCKPFGVI DGLSTRTLQL NKSQEPRSAA QSGTSHSTSI VNSSNGSGLG LPTTSIASSL
     AANPRKSIVV GPTNVPSSMI SSDDSALGLD ELLNVSELDN DDENDVKIWR DFNNNQNKKK
     IPLGAFRNKS VLYNNHIYQD DQHHHLHRRN SNADKKFNGS GHIKKQQPIR RQSQSKIERR
     RASIVEAVSQ GYRPTKSGLF SETALADVEE LLGDDRDLME LIQGL
 
 
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