LAC1_CRYNB
ID LAC1_CRYNB Reviewed; 624 AA.
AC Q55P57; Q9UQZ7;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Laccase-1 {ECO:0000305};
DE EC=1.10.3.2 {ECO:0000269|PubMed:8300520};
DE AltName: Full=Diphenol oxidase 1 {ECO:0000303|PubMed:8300520};
DE Flags: Precursor;
GN Name=LAC1 {ECO:0000303|PubMed:8300520}; OrderedLocusNames=CNBG3550;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 21-37; 240-248;
RP 282-313 AND 325-332, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND INDUCTION.
RC STRAIN=B-3501A;
RX PubMed=8300520; DOI=10.1128/jb.176.3.656-664.1994;
RA Williamson P.R.;
RT "Biochemical and molecular characterization of the diphenol oxidase of
RT Cryptococcus neoformans: identification as a laccase.";
RL J. Bacteriol. 176:656-664(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 118-210.
RX PubMed=11050543; DOI=10.1046/j.1365-294x.2000.01021.x;
RA Xu J., Vilgalys R., Mitchell T.G.;
RT "Multiple gene genealogies reveal recent dispersion and hybridization in
RT the human pathogenic fungus Cryptococcus neoformans.";
RL Mol. Ecol. 9:1471-1481(2000).
RN [4]
RP FUNCTION.
RX PubMed=1100669; DOI=10.1128/jcm.1.6.509-514.1975;
RA Chaskes S., Tyndall R.L.;
RT "Pigment production by Cryptococcus neoformans from para- and ortho-
RT Diphenols: effect of the nitrogen source.";
RL J. Clin. Microbiol. 1:509-514(1975).
RN [5]
RP FUNCTION.
RX PubMed=6807845; DOI=10.1128/iai.36.3.1175-1184.1982;
RA Rhodes J.C., Polacheck I., Kwon-Chung K.J.;
RT "Phenoloxidase activity and virulence in isogenic strains of Cryptococcus
RT neoformans.";
RL Infect. Immun. 36:1175-1184(1982).
RN [6]
RP FUNCTION.
RX PubMed=6804444; DOI=10.1128/jb.150.3.1414-1421.1982;
RA Kwon-Chung K.J., Polacheck I., Popkin T.J.;
RT "Melanin-lacking mutants of Cryptococcus neoformans and their virulence for
RT mice.";
RL J. Bacteriol. 150:1414-1421(1982).
RN [7]
RP INDUCTION, DISRUPTION PHENOTYPE, FUNCTION, AND MUTAGENESIS OF HIS-164.
RX PubMed=8760791; DOI=10.1084/jem.184.2.377;
RA Salas S.D., Bennett J.E., Kwon-Chung K.J., Perfect J.R., Williamson P.R.;
RT "Effect of the laccase gene CNLAC1, on virulence of Cryptococcus
RT neoformans.";
RL J. Exp. Med. 184:377-386(1996).
RN [8]
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 [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14977977; DOI=10.1128/iai.72.3.1693-1699.2004;
RA Noverr M.C., Williamson P.R., Fajardo R.S., Huffnagle G.B.;
RT "CNLAC1 is required for extrapulmonary dissemination of Cryptococcus
RT neoformans but not pulmonary persistence.";
RL Infect. Immun. 72:1693-1699(2004).
RN [10]
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 (PubMed:1100669, PubMed:6807845, PubMed:6804444,
CC PubMed:8760791). Able to oxidize a wide variety of aromatic diphenol
CC and diamino groups in the ortho, meta, and para positions but not
CC monophenolic groups such as in phenol, tyramine, or tyrosine
CC (PubMed:8300520). Plays an important role in virulence
CC (PubMed:8760791). Plays a role in dissemination to extrapulmonary sites
CC but is not involved in pulmonary growth or in elicitation of cellular
CC immune responses in the lung (PubMed:14977977).
CC {ECO:0000269|PubMed:1100669, ECO:0000269|PubMed:14977977,
CC ECO:0000269|PubMed:6804444, ECO:0000269|PubMed:6807845,
CC ECO:0000269|PubMed:8300520, ECO:0000269|PubMed:8760791}.
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:8300520};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000269|PubMed:8300520};
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 -!- INDUCTION: Expressed during infection of host (PubMed:8760791).
CC Expression is repressed by glucose (PubMed:8300520).
CC {ECO:0000269|PubMed:8300520, ECO:0000269|PubMed:8760791}.
CC -!- DISRUPTION PHENOTYPE: Decreases virulence in mice (PubMed:8760791,
CC PubMed:14977977). {ECO:0000269|PubMed:14977977,
CC ECO:0000269|PubMed:8760791}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF140150; AAD49810.1; -; Genomic_DNA.
DR EMBL; AF140151; AAD49811.1; -; Genomic_DNA.
DR EMBL; AF140153; AAD49813.1; -; Genomic_DNA.
DR EMBL; AF140156; AAD49816.1; -; Genomic_DNA.
DR EMBL; AF140178; AAD49838.1; -; Genomic_DNA.
DR EMBL; AAEY01000038; EAL19727.1; -; Genomic_DNA.
DR PIR; A36962; A36962.
DR RefSeq; XP_774374.1; XM_769281.1.
DR AlphaFoldDB; Q55P57; -.
DR SMR; Q55P57; -.
DR EnsemblFungi; EAL19727; EAL19727; CNBG3550.
DR GeneID; 4937391; -.
DR KEGG; cnb:CNBG3550; -.
DR VEuPathDB; FungiDB:CNBG3550; -.
DR HOGENOM; CLU_006504_7_1_1; -.
DR Proteomes; UP000001435; Chromosome 7.
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; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Metal-binding; Oxidoreductase; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:8300520"
FT CHAIN 21..624
FT /note="Laccase-1"
FT /evidence="ECO:0000255"
FT /id="PRO_5004250357"
FT DOMAIN 72..183
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 195..343
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 469..562
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT REGION 579..604
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 149
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 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"
FT MUTAGEN 164
FT /note="H->Y: In mel2; impairs melanin production and
FT decreases virulence."
FT /evidence="ECO:0000269|PubMed:8760791"
SQ SEQUENCE 624 AA; 68270 MW; A675C03F8940224B CRC64;
MRGLAKLFFL SCSFVSLVSS EKTDESPTAV SDNYMPKATA TIDPSVFALS NDFEITDVPT
TREYTFDIAK AFASPDGYER EVYVVNNMFP GPVIEANTGD TIIVHVNNHL DEGQSLHWHG
LRQLGTAFMD GVPGITQCPI PPGGSFTYNF TVSHQSGTYW WHSHYSNSMA DGIWGPLIVH
SPNEPLQRGR DYDEDRIVFI TDWMHDNSEI IIAALATPEG YKGNIAPPQG DAILINGRGQ
TNCTATGSSS CFYPPPPEIQ VPVNCRVRLR FISATAHPMY RISIDNHPME VVEADGTAVY
GPTVHEISVA PGERYSAIIN TNEGKEGDAF WLRTSVALSC MFGAVSQEGL AVVRYTGNGM
VSTEEPQTSA WSDLAGVTVP CTGLDQTYTL SPRDSLSAPR EPLQSHFFNS ERGAFVNVLG
NTFQGYGFNN ISYQNQIFNP LLSIVQRGGS CENTLVSSRT FPDFGPGNII INNLDTVIDH
PYHLHGNEFQ VIGRGTGALS IDNLTNIDFT LDNPVRKDTL WIQGGSWAVL RITADNPGVW
ALHCHIGWHL TEGKLAVIVV QPSAIGHMES PESWTNLCAN TDPNAFGPAK RSSSPSIQSS
KTSSFQYLRE VKGKVVKRRG AREA
