ECE1_CANAL
ID ECE1_CANAL Reviewed; 271 AA.
AC Q07730; A0A1D8PLT9; Q59PG4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Extent of cell elongation protein 1 {ECO:0000303|PubMed:8359888};
DE Contains:
DE RecName: Full=ECE1-I {ECO:0000303|PubMed:27027296};
DE Contains:
DE RecName: Full=ECE1-II {ECO:0000303|PubMed:27027296};
DE Contains:
DE RecName: Full=Candidalysin ECE1-III {ECO:0000303|PubMed:27027296};
DE Contains:
DE RecName: Full=ECE1-IV {ECO:0000303|PubMed:27027296};
DE Contains:
DE RecName: Full=ECE1-V {ECO:0000303|PubMed:27027296};
DE Contains:
DE RecName: Full=ECE1-VI {ECO:0000303|PubMed:27027296};
DE Contains:
DE RecName: Full=ECE1-VII {ECO:0000303|PubMed:27027296};
DE Contains:
DE RecName: Full=ECE1-VIII {ECO:0000303|PubMed:27027296};
DE Flags: Precursor;
GN Name=ECE1 {ECO:0000303|PubMed:8359888}; OrderedLocusNames=CAALFM_C403470CA;
GN ORFNames=CaO19.10882, CaO19.3374;
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 DEVELOPMENTAL STAGE.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=8359888; DOI=10.1128/iai.61.9.3648-3655.1993;
RA Birse C.E., Irwin M.Y., Fonzi W.A., Sypherd P.S.;
RT "Cloning and characterization of ECE1, a gene expressed in association with
RT cell elongation of the dimorphic pathogen Candida albicans.";
RL Infect. Immun. 61:3648-3655(1993).
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 INDUCTION.
RX PubMed=10464197; DOI=10.1128/jb.181.17.5273-5279.1999;
RA Sharkey L.L., McNemar M.D., Saporito-Irwin S.M., Sypherd P.S., Fonzi W.A.;
RT "HWP1 functions in the morphological development of Candida albicans
RT downstream of EFG1, TUP1, and RBF1.";
RL J. Bacteriol. 181:5273-5279(1999).
RN [6]
RP INDUCTION.
RX PubMed=10790384; DOI=10.1093/genetics/155.1.57;
RA Braun B.R., Johnson A.D.;
RT "TUP1, CPH1 and EFG1 make independent contributions to filamentation in
RT Candida albicans.";
RL Genetics 155:57-67(2000).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=16839200; DOI=10.1371/journal.ppat.0020063;
RA Nobile C.J., Andes D.R., Nett J.E., Smith F.J., Yue F., Phan Q.T.,
RA Edwards J.E., Filler S.G., Mitchell A.P.;
RT "Critical role of Bcr1-dependent adhesins in C. albicans biofilm formation
RT in vitro and in vivo.";
RL PLoS Pathog. 2:E63-E63(2006).
RN [8]
RP CLEAVAGE BY KEX2.
RX PubMed=18625069; DOI=10.1186/1471-2180-8-116;
RA Bader O., Krauke Y., Hube B.;
RT "Processing of predicted substrates of fungal Kex2 proteinases from Candida
RT albicans, C. glabrata, Saccharomyces cerevisiae and Pichia pastoris.";
RL BMC Microbiol. 8:116-116(2008).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=23136884; DOI=10.1111/mmi.12087;
RA Rohm M., Lindemann E., Hiller E., Ermert D., Lemuth K., Trkulja D.,
RA Sogukpinar O., Brunner H., Rupp S., Urban C.F., Sohn K.;
RT "A family of secreted pathogenesis-related proteins in Candida albicans.";
RL Mol. Microbiol. 87:132-151(2013).
RN [10]
RP INDUCTION.
RX PubMed=24673895; DOI=10.1186/1471-2180-14-80;
RA Ding X., Liu Z., Su J., Yan D.;
RT "Human serum inhibits adhesion and biofilm formation in Candida albicans.";
RL BMC Microbiol. 14:80-80(2014).
RN [11]
RP FUNCTION (CANDIDALYSIN ECE1-III), DISRUPTION PHENOTYPE, CLEAVAGE BY KEX2,
RP AND SUBCELLULAR LOCATION (CANDIDALYSIN ECE1-III).
RX PubMed=27027296; DOI=10.1038/nature17625;
RA Moyes D.L., Wilson D., Richardson J.P., Mogavero S., Tang S.X.,
RA Wernecke J., Hoefs S., Gratacap R.L., Robbins J., Runglall M., Murciano C.,
RA Blagojevic M., Thavaraj S., Foerster T.M., Hebecker B., Kasper L.,
RA Vizcay G., Iancu S.I., Kichik N., Haeder A., Kurzai O., Luo T., Krueger T.,
RA Kniemeyer O., Cota E., Bader O., Wheeler R.T., Gutsmann T., Hube B.,
RA Naglik J.R.;
RT "Candidalysin is a fungal peptide toxin critical for mucosal infection.";
RL Nature 532:64-68(2016).
CC -!- FUNCTION: Secreted protein involved in biofilm formation
CC (PubMed:16839200). Further cleaved by KEX2 in 8 similar peptides (ECE1-
CC I to ECE1-VIII) (PubMed:27027296). {ECO:0000269|PubMed:16839200,
CC ECO:0000269|PubMed:27027296}.
CC -!- FUNCTION: [Candidalysin ECE1-III]: Acts as a cytolytic pepdide toxin
CC that directly damages host epithelial membranes, triggers a danger
CC response signaling pathway and activates epithelial immunity
CC (PubMed:27027296). Probably acts similarly to cationic antimicrobial
CC peptide toxins, inducing lesions after binding to target cell membranes
CC and causing an inward current associated with calcium influx
CC (PubMed:27027296). {ECO:0000269|PubMed:27027296}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23136884}.
CC -!- SUBCELLULAR LOCATION: [Candidalysin ECE1-III]: Host cell membrane
CC {ECO:0000269|PubMed:27027296}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Expressed in elongating hyphae but not in budding
CC yeast cells (PubMed:8359888). {ECO:0000269|PubMed:8359888}.
CC -!- INDUCTION: Expression is induced by human serum (PubMed:24673895).
CC Expression is regulated by the transcription factor EFG1
CC (PubMed:10464197, PubMed:10790384). Expression is also regulated by the
CC transcription factor BCR1 (PubMed:16839200).
CC {ECO:0000269|PubMed:10464197, ECO:0000269|PubMed:10790384,
CC ECO:0000269|PubMed:16839200, ECO:0000269|PubMed:24673895}.
CC -!- DOMAIN: The N-ter alpha-helix of peptide ECE1-III allows insertion of
CC the toxin into host epithelial cells membranes (PubMed:27027296).
CC {ECO:0000269|PubMed:27027296}.
CC -!- PTM: Cleavage by KEX2 generates 8 peptides ECE1-I to ECE1-VIII, all
CC terminating in Lys-Arg (PubMed:18625069, PubMed:27027296). Only peptide
CC ECE1-III, called candidalysin, shows toxin activity (PubMed:27027296).
CC {ECO:0000269|PubMed:18625069, ECO:0000269|PubMed:27027296}.
CC -!- DISRUPTION PHENOTYPE: Impairs damaging of epithelia and induction of p-
CC MKP1/c-Fos-mediated danger responses and cytokine secretion
CC (PubMed:27027296). {ECO:0000269|PubMed:27027296}.
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DR EMBL; L17087; AAA34338.2; -; Genomic_DNA.
DR EMBL; CP017626; AOW29105.1; -; Genomic_DNA.
DR RefSeq; XP_711594.1; XM_706502.1.
DR AlphaFoldDB; Q07730; -.
DR SMR; Q07730; -.
DR GeneID; 3646814; -.
DR KEGG; cal:CAALFM_C403470CA; -.
DR CGD; CAL0000199701; ECE1.
DR VEuPathDB; FungiDB:C4_03470C_A; -.
DR HOGENOM; CLU_1019397_0_0_1; -.
DR OMA; HAPEFNM; -.
DR OrthoDB; 1723169at2759; -.
DR PHI-base; PHI:7644; -.
DR PHI-base; PHI:7759; -.
DR PHI-base; PHI:7895; -.
DR PHI-base; PHI:8546; -.
DR PHI-base; PHI:8787; -.
DR PRO; PR:Q07730; -.
DR Proteomes; UP000000559; Chromosome 4.
DR GO; GO:0005576; C:extracellular region; IDA:CGD.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0001897; P:cytolysis by symbiont of host cells; IDA:CGD.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Host cell membrane; Host membrane;
KW Membrane; Reference proteome; Repeat; Secreted; Signal; Toxin;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..31
FT /note="ECE1-I"
FT /evidence="ECO:0000305|PubMed:27027296"
FT /id="PRO_0000086910"
FT CHAIN 32..61
FT /note="ECE1-II"
FT /evidence="ECO:0000305|PubMed:27027296"
FT /id="PRO_0000436401"
FT CHAIN 62..93
FT /note="Candidalysin ECE1-III"
FT /evidence="ECO:0000305|PubMed:27027296"
FT /id="PRO_0000436402"
FT CHAIN 94..126
FT /note="ECE1-IV"
FT /evidence="ECO:0000305|PubMed:27027296"
FT /id="PRO_0000436403"
FT CHAIN 127..160
FT /note="ECE1-V"
FT /evidence="ECO:0000305|PubMed:27027296"
FT /id="PRO_0000436404"
FT CHAIN 161..194
FT /note="ECE1-VI"
FT /evidence="ECO:0000305|PubMed:27027296"
FT /id="PRO_0000436405"
FT CHAIN 195..228
FT /note="ECE1-VII"
FT /evidence="ECO:0000305|PubMed:27027296"
FT /id="PRO_0000436406"
FT CHAIN 229..271
FT /note="ECE1-VIII"
FT /evidence="ECO:0000305|PubMed:27027296"
FT /id="PRO_0000436407"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 271 AA; 28878 MW; 2AF8DF50498EF230 CRC64;
MKFSKIACAT VFALSSQAAI IHHAPEFNMK RDVAPAAPAA PADQAPTVPA PQEFNTAITK
RSIIGIIMGI LGNIPQVIQI IMSIVKAFKG NKREDIDSVV AGIIADMPFV VRAVDTAMTS
VASTKRDGAN DDVANAVVRL PEIVARVATG VQQSIENAKR DGVPDVGLNL VANAPRLISN
VFDGVSETVQ QAKRDGLEDF LDELLQRLPQ LITRSAESAL KDSQPVKRDA GSVALSNLIK
KSIETVGIEN AAQIVSERDI SSLIEEYFGK A
