LAC2_CRYNH
ID LAC2_CRYNH Reviewed; 594 AA.
AC J9VQZ4;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 2.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Laccase-2 {ECO:0000305};
DE EC=1.10.3.2 {ECO:0000250|UniProtKB:J9VY90};
DE AltName: Full=Diphenol oxidase 2 {ECO:0000305};
DE Flags: Precursor;
GN Name=LAC2; ORFNames=CNAG_03464;
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 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).
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:0000250|UniProtKB:J9VY90};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:J9VY90};
CC Note=Binds 4 Cu cations per monomer. {ECO:0000250|UniProtKB:Q70KY3};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11500433}. Secreted,
CC cell wall {ECO:0000269|PubMed:11500433}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; CP003827; AFR96688.2; -; Genomic_DNA.
DR RefSeq; XP_012050964.1; XM_012195574.1.
DR AlphaFoldDB; J9VQZ4; -.
DR SMR; J9VQZ4; -.
DR EnsemblFungi; AFR96688; AFR96688; CNAG_03464.
DR GeneID; 23886968; -.
DR VEuPathDB; FungiDB:CNAG_03464; -.
DR HOGENOM; CLU_006504_7_1_1; -.
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 3: Inferred from homology;
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..594
FT /note="Laccase-2"
FT /evidence="ECO:0000255"
FT /id="PRO_5003827757"
FT DOMAIN 70..183
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 195..357
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 466..563
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
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:P17489"
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:P17489"
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:P17489"
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:P17489"
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:P17489"
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:P17489"
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:P17489"
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 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 286
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 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 397
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 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 508
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 594 AA; 65066 MW; E71D60C20BD6C102 CRC64;
MGGIIKLSFL FCSLISLVNS ENTGKLPTAI SDHSVPKATA TTDPSVFVLS NDFEITDVPT
TREYTFNLTE ALASPDGYER LVYAVNNMLP GPVIEANTGD TVIVHVNNYL HEGQGIHWHG
LRQNGTALMD GVPGITQCSI PPGGSFTYQF TVSHQSGTFW WHSHYSNSMA DGIWGPLIVH
SPNEPLQRGR DYDEDRIVAV TDWMHDESET IVEALISSEG YRGRPFPPQG DAILINGRGQ
TNCTATGSPS CTYPPPPEIH VPVNCRVRLR FISAASHPMY RISIDNHSME IVETDGTAVY
GPTIHEISIS SGERYSVIIN TTEGKEGDAF WLRTSVALDC MAQGVTQVGL AVVRYTGNGS
ITTAEPRTEA WTDLARPDTP CVGLDEMYHL SPRELVNASQ TALESRVLDS KLGKFVDVYG
NSFEGYGFNN VTYQNQINDP LLYVVQRGGT CNSSLIANAT FADIGPVNII INNLDSHIGH
PYHMHGTEFQ LMGRGTGALT LDDLPNTNLT LDNPTRKDTI WMQGGSWALL RIISDNPGVW
ALHCHIGWHL AKGKMAVVVV QPEAIKKIQW PESWMDLCAN TDPNAFGPAR RSVS
