EBP1_CANAL
ID EBP1_CANAL Reviewed; 407 AA.
AC A0A1D8PPK1;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Probable NADPH dehydrogenase {ECO:0000250|UniProtKB:P43084};
DE EC=1.6.99.1 {ECO:0000250|UniProtKB:P43084};
DE AltName: Full=Estrogen-binding protein {ECO:0000250|UniProtKB:P43084};
DE Short=EBP {ECO:0000250|UniProtKB:P43084};
GN Name=EBP1 {ECO:0000312|CGD:CAL0000199513};
GN OrderedLocusNames=orf19.125 {ECO:0000312|CGD:CAL0000199513};
GN ORFNames=CAALFM_C601180CA {ECO:0000312|EMBL:AOW30064.1};
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 {ECO:0000312|Proteomes:UP000000559};
RN [1] {ECO:0000312|Proteomes:UP000000559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000312|Proteomes:UP000000559};
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] {ECO:0000312|Proteomes:UP000000559}
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000312|Proteomes:UP000000559};
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] {ECO:0000312|Proteomes:UP000000559}
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] {ECO:0000305}
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=34986357; DOI=10.1016/j.celrep.2021.110183;
RA Kumwenda P., Cottier F., Hendry A.C., Kneafsey D., Keevan B., Gallagher H.,
RA Tsai H.J., Hall R.A.;
RT "Estrogen promotes innate immune evasion of Candida albicans through
RT inactivation of the alternative complement system.";
RL Cell Rep. 38:110183-110183(2022).
CC -!- FUNCTION: Oxidoreductase that binds mammalian estrogens with high
CC affinity. {ECO:0000250|UniProtKB:P43084}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + H(+) + NADPH = AH2 + NADP(+); Xref=Rhea:RHEA:13149,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.99.1;
CC Evidence={ECO:0000250|UniProtKB:P43084};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q02899};
CC -!- INDUCTION: Induced by estrogen (17beta-estradiol).
CC {ECO:0000269|PubMed:34986357}.
CC -!- DISRUPTION PHENOTYPE: Decreases phagocytosis of the fungus by host
CC cells (PubMed:34986357). Increases expression of GPD2
CC (PubMed:34986357). {ECO:0000269|PubMed:34986357}.
CC -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC family. {ECO:0000305}.
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DR EMBL; CP017628; AOW30064.1; -; Genomic_DNA.
DR RefSeq; XP_714331.2; XM_709238.2.
DR SMR; A0A1D8PPK1; -.
DR GeneID; 3644060; -.
DR KEGG; cal:CAALFM_C601180CA; -.
DR CGD; CAL0000199513; EBP1.
DR VEuPathDB; FungiDB:C6_01180C_A; -.
DR OMA; YQDTPGL; -.
DR OrthoDB; 978998at2759; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:CGD.
DR GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
DR GO; GO:0099130; F:estrogen binding; ISS:UniProtKB.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0042562; F:hormone binding; IDA:CGD.
DR GO; GO:0003959; F:NADPH dehydrogenase activity; IDA:CGD.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0005496; F:steroid binding; IDA:CGD.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IBA:GO_Central.
DR GO; GO:0008202; P:steroid metabolic process; IDA:CGD.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR InterPro; IPR045247; Oye-like.
DR PANTHER; PTHR22893; PTHR22893; 1.
DR Pfam; PF00724; Oxidored_FMN; 1.
PE 2: Evidence at transcript level;
KW Flavoprotein; FMN; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..407
FT /note="Probable NADPH dehydrogenase"
FT /id="PRO_0000456036"
FT ACT_SITE 206
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q02899"
FT BINDING 49
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q02899"
FT BINDING 124
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q02899"
FT BINDING 254
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q02899"
FT BINDING 357
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q02899"
SQ SEQUENCE 407 AA; 46089 MW; 9E19211953CA83D5 CRC64;
MTIESTNSFV VPSDTELIDV TPLGSTKLFQ PIKVGNNVLP QRIAYVPTTR FRASKDHIPS
DLQLNYYNAR SQYPGTLIIT EATFASERGG IDLHVPGIYN DAQAKSWKKI NEAIHGNGSF
SSVQLWYLGR VANAKDLKDS GLPLIAPSAV YWDENSEKLA KEAGNELRAL TEEEIDHIVE
VEYPNAAKHA LEAGFDYVEI HGAHGYLLDQ FLNLASNKRT DKYGCGSIEN RARLLLRVVD
KLIEVVGANR LALRLSPWAS FQGMEIEGEE IHSYILQQLQ QRADNGQQLA YISLVEPRVT
GIYDVSLKDQ QGRSNEFAYK IWKGNFIRAG NYTYDAPEFK TLINDLKNDR TIIGFSRFFT
SNPDLVEKLK LGKPLNYYNR EEFYKYYNYG YNSYDESEKQ VIGKPLA
