[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 26003; DOI=10.1007/s004380050261; PubMed=8914515 [NCBI, ExPASy, EBI, Israel, Japan] Fernandez-Larrea J., Stahl U.; "Isolation and characterization of a laccase gene from Podospora anserina."; Mol. Gen. Genet. 252:539-551(1996).

Comments

FUNCTION: Probably involved in lignin degradation and in the detoxification of lignin-derived products in its natural habitat (herbivorous dung), which is rich in lignin of grasses and straw. Probably involved in melanin synthesis and in perithecia development.
CATALYTIC ACTIVITY: 4 benzenediol + O₂ = 4 benzosemiquinone + 2 H₂O.
COFACTOR: Binds 4 copper ions per monomer (By similarity).
SUBUNIT: Monomer.
SUBCELLULAR LOCATION: Secreted.
DEVELOPMENTAL STAGE: Low basic levels throughout the growth phase; increases at least 20-fold at the beginning of the autolytic phase and decreases again thereafter.
INDUCTION: Under oxidative stress on the mycelium by aromatic xenobiotics (guaiacol, hydroquinone, benzoquinone), and by copper salt at a concentration of 1mM (growing mycelium).
PTM: Proteolytically processed at both its N-terminus and its C-terminus.
MISCELLANEOUS: Podospora anserina contains at least 3 laccase isozymes named I, II, and III. They differ in their substrate specificity, number of subunits, isoelectronic point and heat stability.
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

Y08827; CAA70061.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S72493; S72493.

3D structure databases

HSSP

Q9Y780; 1HFU. [HSSP ENTRY / PDB]

SMR

P78722; 46-605.

ModBase

P78722.

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:0006583;	Biological process: melanin biosynthetic process from tyrosine (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; 1.

ProtoNet

P78722.

Other

UniRef

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

Keywords

Copper; Glycoprotein; Lignin degradation; Melanin biosynthesis; Metal-binding; Oxidoreductase; Repeat; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 23`	`23`	`Potential.`
`PROPEP`	`24 48`	`25`	`Potential.`	`PRO_0000002931`
`CHAIN`	`49 605`	`557`	`Laccase-2.`	`PRO_0000002932`
`PROPEP`	`606 621`	`16`	`Potential.`	`PRO_0000002933`
`DOMAIN`	`78 201`	`124`	`Plastocyanin-like 1.`
`DOMAIN`	`210 367`	`158`	`Plastocyanin-like 2.`
`DOMAIN`	`430 566`	`137`	`Plastocyanin-like 3.`
`METAL`	`138 138`		`Copper 1; type 2 (By similarity).`
`METAL`	`140 140`		`Copper 2; type 3 (By similarity).`
`METAL`	`183 183`		`Copper 2; type 3 (By similarity).`
`METAL`	`185 185`		`Copper 3; type 3 (By similarity).`
`METAL`	`476 476`		`Copper 4; type 1 (By similarity).`
`METAL`	`479 479`		`Copper 1; type 2 (By similarity).`
`METAL`	`481 481`		`Copper 3; type 3 (By similarity).`
`METAL`	`548 548`		`Copper 3; type 3 (By similarity).`
`METAL`	`549 549`		`Copper 4; type 1 (By similarity).`
`METAL`	`550 550`		`Copper 2; type 3 (By similarity).`
`METAL`	`554 554`		`Copper 4; type 1 (By similarity).`
`CARBOHYD`	`133 133`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`261 261`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`276 276`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`289 289`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`325 325`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`334 334`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`401 401`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`421 421`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`441 441`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 621 AA [This is the length of the unprocessed precursor]

Molecular weight: 68129 Da [This is the MW of the unprocessed precursor]

CRC64: 79F85E2ED25C1CA7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MMKSFFSAAA LLLGLVAPSA VLAAPSLPGV PREVTRDLLR PVEERQSSCH TAANRACWAP 

        70         80         90        100        110        120 
GFDINTDYEV STPNTGVTRT YTLTLTEVDN WLGPDGVVKQ KVMLVNGDIF GPTITANWGD 

       130        140        150        160        170        180 
WIQVNVINNL RTNGTSIHWH GLHQKGTNMH DGANGVTECP IPPKGGSRIY RFRAQQYGTS 

       190        200        210        220        230        240 
WYHSHFSAQY GNGVVGTIVV NGPASVPYDI DLGVFPITDY YHKPADVLVE ETMNGGPPPS 

       250        260        270        280        290        300 
DTVLFKGHGK NPQTGAGKFA NVTLTPGKRH RLRIINTSTH DHFQLKLQNH TMTIIAADMV 

       310        320        330        340        350        360 
PVQAQTVDSL FLAVGQRYDV TIDANKSVGN YWFNATFGGG LACGASLNPH PAAVFRYQGA 

       370        380        390        400        410        420 
PNTLPTNIGT PAADANCMDL NNLTPVVSRS VPTSGFTPRP NNTLPVSLTL GGTPLFVWKV 

       430        440        450        460        470        480 
NGSSINVDWD KPIVDYVIAQ NTSYPPQANV ITVNSVNQWT YWLIENDPTG PFSIPHPMHL 

       490        500        510        520        530        540 
HGHDFLVVGR SPDQPAGVPQ TRYRFNPATD MALLKSSNPV RRDVAMLPAN GWLLIAFKSD 

       550        560        570        580        590        600 
NPGAWLFHCH IAWHVSGGLS VQYLERPNDL RNGFSQADKN QHNNNCNAWR AYWPTNPFPK 

       610        620 
IDSGLKVKKW VGEHPDWYIK N

P78722 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