NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT PRO-411.
STRAIN=IFO 4917;
PubMed=2394718 [NCBI, ExPASy, EBI, Israel, Japan]
Kojima Y., Tsukuda Y., Kawai Y., Tsukamoto A., Sugiura J., Sakaino M., Kita Y.;
"Cloning, sequence analysis, and expression of ligninolytic phenoloxidase genes of the white-rot basidiomycete Coriolus hirsutus.";
J. Biol. Chem. 265:15224-15230(1990).

Comments

FUNCTION: Most probably plays an important role in lignin degradation. Cleaves the C-C and C-O bonds of some phenolic lignin model compounds (such as O- and P-quinols, aminophenols and phenylenediamine).
CATALYTIC ACTIVITY: 4 benzenediol + O₂ = 4 benzosemiquinone + 2 H₂O.
COFACTOR: Binds 4 copper ions per monomer (By similarity).
SUBCELLULAR LOCATION: Secreted.
POLYMORPHISM: 2 allelic forms exist in position 111.
SIMILARITY: Belongs to the multicopper oxidase family.
SIMILARITY: Contains 3 plastocyanin-like domains.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M60560; AAA33103.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M60561; AAA33104.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A35883; A35883.

3D structure databases

HSSP

Q96UT7; 1KYA. [HSSP ENTRY / PDB]

SMR

Q02497; 22-520.

ModBase

Q02497.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005507;	Molecular function: copper ion binding (inferred from electronic annotation from InterPro).
GO:0008471;	Molecular function: laccase activity (inferred from electronic annotation from EC).
GO:0046274;	Biological process: lignin catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001117; Cu-oxidase.
IPR011706; Cu-oxidase_2.
IPR011707; Cu-oxidase_3.
IPR002355; Cu_oxidase_Cu_BS.
IPR008972; Cupredoxin.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.40.420; Cupredoxin; 3.

Pfam

PF00394; Cu-oxidase; 1.
PF07731; Cu-oxidase_2; 1.
PF07732; Cu-oxidase_3; 1.
Pfam graphical view of domain structure.

PROSITE

PS00079; MULTICOPPER_OXIDASE1; 1.
PS00080; MULTICOPPER_OXIDASE2; FALSE_NEG.

ProtoNet

Q02497.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Copper; Direct protein sequencing; Glycoprotein; Lignin degradation; Metal-binding; Oxidoreductase; Repeat; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 21`	`21`
`CHAIN`	`22 520`	`499`	`Laccase.`	`PRO_0000002939`
`DOMAIN`	`23 148`	`126`	`Plastocyanin-like 1.`
`DOMAIN`	`160 302`	`143`	`Plastocyanin-like 2.`
`DOMAIN`	`369 491`	`123`	`Plastocyanin-like 3.`
`METAL`	`85 85`		`Copper 1; type 2 (By similarity).`
`METAL`	`87 87`		`Copper 2; type 3 (By similarity).`
`METAL`	`130 130`		`Copper 2; type 3 (By similarity).`
`METAL`	`132 132`		`Copper 3; type 3 (By similarity).`
`METAL`	`416 416`		`Copper 4; type 1 (By similarity).`
`METAL`	`419 419`		`Copper 1; type 2 (By similarity).`
`METAL`	`421 421`		`Copper 3; type 3 (By similarity).`
`METAL`	`473 473`		`Copper 3; type 3 (By similarity).`
`METAL`	`474 474`		`Copper 4; type 1 (By similarity).`
`METAL`	`475 475`		`Copper 2; type 3 (By similarity).`
`METAL`	`479 479`		`Copper 4; type 1 (By similarity).`
`CARBOHYD`	`50 50`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`72 72`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`75 75`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`210 210`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`229 229`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`354 354`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`457 457`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`106 509`		`Potential.`
`DISULFID`	`138 226`		`Potential.`
`VARIANT`	`411 411`	`1`	`A -> P.`
`CONFLICT`	`378 379`		`SG -> RR (in Ref. 1; AAA33104).`

Sequence information

Length: 520 AA [This is the length of the unprocessed precursor]

Molecular weight: 55688 Da [This is the MW of the unprocessed precursor]

CRC64: 977D8DFA551F7929 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSRFQSLLAF VVASLAAVAH AAIGPTADLT ISNAEVSPDG FARQAVVVNN VTPGPLVAGN 

        70         80         90        100        110        120 
KGDRFQLNVI DNLTNHTMLK STSIHWHGFF QKGTNWADGP AFVNQCPISS GHSFLYDFQV 

       130        140        150        160        170        180 
PDQAGTFWYH SHLSTQYCDG LRGPFVVYDP NDPHASLYDV DNDDTVITLA DWYHTAAKLG 

       190        200        210        220        230        240 
PAFPLGADAT LINGLGRSPS TTAADLAVIN VTKGKRYRFR LVSLSCDPNH TFSIDGHDLT 

       250        260        270        280        290        300 
IIEVDSINSQ PLVVDSIQIF AAQRYSFVLN ADQDVGNYWI RANPNFGNVG FAGGINSAIL 

       310        320        330        340        350        360 
RYDGADPVEP TTTQTTPTKP LNEVDLHPLA TMAVPGSPVA GGVDTAINMA FNFNGTNFFI 

       370        380        390        400        410        420 
NGASFVPPTV PVLLQIISGA QNAQDLLPSG SVYSLPSNAD IEISFPATAA APGAPHPFHL 

       430        440        450        460        470        480 
HGHAFAVVRS AGSTVYNYDN PIFRDVVSTG TPAAGDNVTI RFRTDNPGPW FLHCHIDFHL 

       490        500        510        520 
EAGFAVVFAE DIPDVASANP VPQAWSDLCP IYDALDVNDQ

Q02497 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools