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