LAC1_CRYNH
ID LAC1_CRYNH Reviewed; 624 AA.
AC J9VY90;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Laccase-1 {ECO:0000305};
DE EC=1.10.3.2 {ECO:0000269|PubMed:12581355};
DE AltName: Full=Diphenol oxidase 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=LAC1; ORFNames=CNAG_03465;
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=11500433; DOI=10.1128/iai.69.9.5589-5596.2001;
RA Zhu X., Gibbons J., Garcia-Rivera J., Casadevall A., Williamson P.R.;
RT "Laccase of Cryptococcus neoformans is a cell wall-associated virulence
RT factor.";
RL Infect. Immun. 69:5589-5596(2001).
RN [3]
RP INDUCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=12581355; DOI=10.1046/j.1365-2958.2003.03340.x;
RA Zhu X., Gibbons J., Zhang S., Williamson P.R.;
RT "Copper-mediated reversal of defective laccase in a Deltavph1 avirulent
RT mutant of Cryptococcus neoformans.";
RL Mol. Microbiol. 47:1007-1014(2003).
RN [4]
RP REVIEW.
RX PubMed=15381117; DOI=10.1016/j.femsyr.2004.04.004;
RA Zhu X., Williamson P.R.;
RT "Role of laccase in the biology and virulence of Cryptococcus neoformans.";
RL FEMS Yeast Res. 5:1-10(2004).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=16524904; DOI=10.1128/ec.5.3.488-498.2006;
RA Siafakas A.R., Wright L.C., Sorrell T.C., Djordjevic J.T.;
RT "Lipid rafts in Cryptococcus neoformans concentrate the virulence
RT determinants phospholipase B1 and Cu/Zn superoxide dismutase.";
RL Eukaryot. Cell 5:488-498(2006).
CC -!- FUNCTION: Laccase that catalyzes the oxidation of certain aromatic
CC compounds, including L-dopa, to quinones, which then polymerize to
CC melanin (By similarity). Able to oxidize a wide variety of aromatic
CC diphenol and diamino groups in the ortho, meta, and para positions but
CC not monophenolic groups such as in phenol, tyramine, or tyrosine (By
CC similarity). Plays an important role in virulence (By similarity).
CC Plays a role in dissemination to extrapulmonary sites but is not
CC involved in pulmonary growth or in elicitation of cellular immune
CC responses in the lung (By similarity). {ECO:0000250|UniProtKB:Q55P57,
CC ECO:0000303|PubMed:15381117}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O;
CC Xref=Rhea:RHEA:11276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17594, ChEBI:CHEBI:17977; EC=1.10.3.2;
CC Evidence={ECO:0000269|PubMed:12581355};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000269|PubMed:12581355};
CC Note=Binds 4 Cu cations per monomer. {ECO:0000250|UniProtKB:Q70KY3};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11500433,
CC ECO:0000269|PubMed:12581355}. Secreted, cell wall
CC {ECO:0000269|PubMed:11500433, ECO:0000269|PubMed:12581355,
CC ECO:0000269|PubMed:16524904}. Note=Does not associate with the cell
CC membrane. {ECO:0000269|PubMed:16524904}.
CC -!- INDUCTION: Induced by copper (PubMed:12581355). Transcriptional
CC induction by copper is dependent on enhancer region II, at position
CC -1792 to -1614 within the 5'-untranslated region (PubMed:12581355).
CC {ECO:0000269|PubMed:12581355}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; CP003827; AFR96690.1; -; Genomic_DNA.
DR RefSeq; XP_012051278.1; XM_012195888.1.
DR AlphaFoldDB; J9VY90; -.
DR SMR; J9VY90; -.
DR EnsemblFungi; AFR96690; AFR96690; CNAG_03465.
DR GeneID; 23886969; -.
DR VEuPathDB; FungiDB:CNAG_03465; -.
DR HOGENOM; CLU_006504_7_1_1; -.
DR PHI-base; PHI:9058; -.
DR Proteomes; UP000010091; Chromosome 8.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0052716; F:hydroquinone:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
PE 1: Evidence at protein level;
KW Cell wall; Copper; Disulfide bond; Glycoprotein; Metal-binding;
KW Oxidoreductase; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..624
FT /note="Laccase-1"
FT /evidence="ECO:0000255"
FT /id="PRO_5003829395"
FT DOMAIN 69..183
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 195..355
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 469..562
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT REGION 582..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 119
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 162
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 164
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 480
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 483
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 485
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 543
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 544
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 545
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 549
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 138..578
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
SQ SEQUENCE 624 AA; 68107 MW; CACD3577C439C6C2 CRC64;
MRGVVKLFFL SCSLVSLVSS EETGKSPTAN YDHYMPKATA TIDPSVFALS NDFEITDVPT
TREYTFDITK ALASPDGYER EVYVVNNMFP GPVIEANTGD TIIVHVNNHL EEGQSIHWHG
LRQLGTAFMD GVPGITQCPI PPGSSFTYQF TVSHQSGTFW WHSHYSNSMA DGIWGPLIIH
SPNEPLQRGR DYDEDRIVFI TDWVHDNSEV VIAALATPEG YKGSPAPPQG DAILINGRGQ
TNCTATGSSS CTYPPPPEIH VPVNCRVRLR FISATAHPMY RITIDNHPLE VVETDGTAVY
GPTVHEISIA PGERYSAIIN TSEGKEGDAF WLRTSVALGC MFGGIDQVGL AVVRYTGNGM
VSTEEPQTTA WSDLAGATTP CAGLDQTYTL SPRESFSAPR EFSQSHVFNS QRGAFVNVYG
NTFQGYGFNN ISYQNQIFNP LLSIVQRGGS CESTLVASTT FPDLGSGNII INNLDGVIDH
PYHLHGNEFQ VIGRGTGALS LDNLTNIDFN LDNPVRKDTL WIQGGSWVVL RITTDNPGVW
ALHCHIGWHL TEGKLAVVVI QPGAIGHMEG PESWTNLCAN TDPNAFGPAR RSPSPSIQSS
KTSTFQYLRE VKGKVVKRRG AREA
