EED1_CANAL
ID EED1_CANAL Reviewed; 887 AA.
AC G1UB67; A0A1D8PU29;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Transcriptional regulator DEF1;
DE AltName: Full=EFG1-dependent transcript protein 1;
GN Name=DEF1; Synonyms=EDT1, EED1; OrderedLocusNames=CAALFM_CR09880WA;
GN ORFNames=CaO19.7561;
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 INDUCTION.
RX PubMed=15051880; DOI=10.1073/pnas.0401416101;
RA Chen H., Fujita M., Feng Q., Clardy J., Fink G.R.;
RT "Tyrosol is a quorum-sensing molecule in Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5048-5052(2004).
RN [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=17645752; DOI=10.1111/j.1462-5822.2007.01009.x;
RA Zakikhany K., Naglik J.R., Schmidt-Westhausen A., Holland G., Schaller M.,
RA Hube B.;
RT "In vivo transcript profiling of Candida albicans identifies a gene
RT essential for interepithelial dissemination.";
RL Cell. Microbiol. 9:2938-2954(2007).
RN [6]
RP INDUCTION.
RX PubMed=20435697; DOI=10.1128/ec.00034-10;
RA Rosenbach A., Dignard D., Pierce J.V., Whiteway M., Kumamoto C.A.;
RT "Adaptations of Candida albicans for growth in the mammalian intestinal
RT tract.";
RL Eukaryot. Cell 9:1075-1086(2010).
RN [7]
RP FUNCTION.
RX PubMed=21407800; DOI=10.1371/journal.pone.0017046;
RA Wachtler B., Wilson D., Haedicke K., Dalle F., Hube B.;
RT "From attachment to damage: defined genes of Candida albicans mediate
RT adhesion, invasion and damage during interaction with oral epithelial
RT cells.";
RL PLoS ONE 6:E17046-E17046(2011).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=21512583; DOI=10.1371/journal.pone.0018394;
RA Martin R., Moran G.P., Jacobsen I.D., Heyken A., Domey J., Sullivan D.J.,
RA Kurzai O., Hube B.;
RT "The Candida albicans-specific gene EED1 encodes a key regulator of hyphal
RT extension.";
RL PLoS ONE 6:E18394-E18394(2011).
RN [9]
RP INDUCTION.
RX PubMed=23210679; DOI=10.3109/13693786.2012.743051;
RA Hsu C.C., Lai W.L., Chuang K.C., Lee M.H., Tsai Y.C.;
RT "The inhibitory activity of linalool against the filamentous growth and
RT biofilm formation in Candida albicans.";
RL Med. Mycol. 51:473-482(2013).
CC -!- FUNCTION: Transcriptional regulator involved in extension of germ tubes
CC into elongated hyphae and maintenance of filamentous growth. Regulates
CC expression of UME6. Acts in a pathway that regulates maintenance of
CC hyphal growth by repressing hyphal-to-yeast transition and allows
CC dissemination within host epithelial tissues. Dispensable for invasion
CC into both host oral epithelial cells and enterocytes, but required for
CC epithelial damage. {ECO:0000269|PubMed:17645752,
CC ECO:0000269|PubMed:21407800, ECO:0000269|PubMed:21512583}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- INDUCTION: Regulated by EFG1, NRG1, and TUP1. Expression is increased
CC with increasing cell density and during host infection. Expression is
CC repressed by linalool. {ECO:0000269|PubMed:15051880,
CC ECO:0000269|PubMed:17645752, ECO:0000269|PubMed:20435697,
CC ECO:0000269|PubMed:21512583, ECO:0000269|PubMed:23210679}.
CC -!- DISRUPTION PHENOTYPE: Leads to yeast-locked cells.
CC {ECO:0000269|PubMed:21512583}.
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DR EMBL; CP017630; AOW31643.1; -; Genomic_DNA.
DR RefSeq; XP_719323.2; XM_714230.2.
DR AlphaFoldDB; G1UB67; -.
DR SMR; G1UB67; -.
DR BioGRID; 1222117; 1.
DR PRIDE; G1UB67; -.
DR GeneID; 3639023; -.
DR KEGG; cal:CAALFM_CR09880WA; -.
DR CGD; CAL0000189505; DEF1.
DR VEuPathDB; FungiDB:CR_09880W_A; -.
DR HOGENOM; CLU_331484_0_0_1; -.
DR PHI-base; PHI:2972; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
PE 2: Evidence at transcript level;
KW Coiled coil; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Virulence.
FT CHAIN 1..887
FT /note="Transcriptional regulator DEF1"
FT /id="PRO_0000424607"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 199..234
FT /evidence="ECO:0000255"
FT COMPBIAS 40..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..520
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 887 AA; 99555 MW; 1F51278DD3C8EEC3 CRC64;
MERRQFNTSN IRNGTGRPRK TPRSKLYMVY PPLSGEDSTN PEPEEGSSQE NNPTEPSSSQ
SNSVQNQDQS EDQSQLPQQE SNTQQESNTQ QESNTPSPRA SNTSTETPAP LSPIQPGIRN
IPSGLLLPQE KVGRLMGYPF YRDFNFTLNP ERYQKLIYVF QILKNAARNH RNGASLLRKY
FSLARRSKRT TDMFVTTIEE MRKRSLENSR KRELEEAQER EESNKRQHTE SSAEPNAESS
TESTTESNAE SGAEPNAEPS AESTTESNVE SGAEPNAESG AESGAEPTAE SNAELKQRIW
EILSYRLEQS NNETNNTGES NSTSQQPRQL PNNELIMNIR VLQKNTHAKP VLGRIKFTPD
KSNKTSLTGS QNKVHSTNTQ QSQKHPQQIL TNSETHKPQQ YSAQSQQQMV HQTNSHEPSQ
KRSPPPQQQQ QKQPSVPTSS VPLQVSQKQN QQQQELPLPP QPQPQQRTAP SAVKQQQSMQ
MQPPPQQQQQ QQRHQPLQQS PPTMPLQQQP VPPVQQVQTV PPPSSQPQTQ LSQQQQQQQQ
AQLQMQVPRC YQYQNRPPSQ QRQYSQTPQY NQPPPQQKVY ALPPQQVYAP PPRQVYAQPT
IACKQQYPQQ LYEQAPQEGS SYQHHYQQVQ QRQNQQPYMQ SAPTYQQPHV QTPKSTRSNK
QEKQRLPKGQ EQVPKATRTM FEAFTGSNIA VEKLRQRTLD NGREPERLRT EYVNVLSSPE
RAAEKSTSRS KQSSNQKPVV KQQSSFPPPI KHQQTQEQQG NILPPVSQLL AIQSSTVTSR
GSNASGAVMG SGNTQRVASR SFTNTFVAEA VVNNANNRGG PVPPTGPETN TRGGRASTRS
SGRPRGNRST QRAEGNVTGR VARSTDGSQS QNSGKASKIS NIRNLLN
