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Protein

Laccase-2

Gene

LCC2

Organism
Trametes versicolor (White-rot fungus) (Coriolus versicolor)
Status
Reviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Lignin degradation and detoxification of lignin-derived products.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Cu cation1 PublicationNote: Binds 4 Cu cations per monomer.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi84Copper 1; type 2Combined sources1 Publication1
Metal bindingi86Copper 2; type 3Combined sources1 Publication1
Metal bindingi129Copper 2; type 3Combined sources1 Publication1
Metal bindingi131Copper 3; type 3Combined sources1 Publication1
Metal bindingi415Copper 4; type 1Combined sources1 Publication1
Metal bindingi418Copper 1; type 2Combined sources1 Publication1
Metal bindingi420Copper 3; type 3Combined sources1 Publication1
Metal bindingi472Copper 3; type 3Combined sources1 Publication1
Metal bindingi473Copper 4; type 1Combined sources1 Publication1
Metal bindingi474Copper 2; type 3Combined sources1 Publication1
Metal bindingi478Copper 4; type 1Combined sources1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
Biological processLignin degradation
LigandCopper, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-17211

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
AA1 Auxiliary Activities 1

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Laccase-2 (EC:1.10.3.2)
Alternative name(s):
Benzenediol:oxygen oxidoreductase 2
Diphenol oxidase 2
Laccase I
Urishiol oxidase 2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:LCC2
Synonyms:LCCI
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiTrametes versicolor (White-rot fungus) (Coriolus versicolor)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri5325 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesPolyporaceaeTrametes

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 20Sequence analysisAdd BLAST20
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000294021 – 519Laccase-2Add BLAST499

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi74N-linked (GlcNAc...) asparagineCombined sources1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi105 ↔ 508Combined sources1 Publication
Disulfide bondi137 ↔ 225Combined sources1 Publication
Glycosylationi161N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi228N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi237N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi271N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi353N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi361N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi456N-linked (GlcNAc...) asparagineCombined sources1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1519
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q12718

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q12718

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q12718

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini22 – 147Plastocyanin-like 1Add BLAST126
Domaini159 – 301Plastocyanin-like 2Add BLAST143
Domaini368 – 490Plastocyanin-like 3Add BLAST123

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the multicopper oxidase family.Curated

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.420, 3 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001117 Cu-oxidase
IPR011706 Cu-oxidase_2
IPR011707 Cu-oxidase_3
IPR033138 Cu_oxidase_CS
IPR008972 Cupredoxin

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00394 Cu-oxidase, 1 hit
PF07731 Cu-oxidase_2, 1 hit
PF07732 Cu-oxidase_3, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49503 SSF49503, 3 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00079 MULTICOPPER_OXIDASE1, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q12718-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGLQRFSFFV TLALVARSLA AIGPVASLVV ANAPVSPDGF LRDAIVVNGV
60 70 80 90 100
VPSPLITGKK GDRFQLNVDD TLTNHSMLKS TSIHWHGFFQ AGTNWADGPA
110 120 130 140 150
FVNQCPIASG HSFLYDFHVP DQAGTFWYHS HLSTQYCDGL RGPFVVYDPK
160 170 180 190 200
DPHASRYDVD NESTVITLTD WYHTAARLGP RFPLGADATL INGLGRSAST
210 220 230 240 250
PTAALAVINV QHGKRYRFRL VSISCDPNYT FSIDGHNLTV IEVDGINSQP
260 270 280 290 300
LLVDSIQIFA AQRYSFVLNA NQTVGNYWVR ANPNFGTVGF AGGINSAILR
310 320 330 340 350
YQGAPVAEPT TTQTTSVIPL IETNLHPLAR MPVPGSPTPG GVDKALNLAF
360 370 380 390 400
NFNGTNFFIN NATFTPPTVP VLLQILSGAQ TAQDLLPAGS VYPLPAHSTI
410 420 430 440 450
EITLPATALA PGAPHPFHLH GHAFAVVRSA GSTTYNYNDP IFRDVVSTGT
460 470 480 490 500
PAAGDNVTIR FQTDNPGPWF LHCHIDFHLD AGFAIVFAED VADVKAANPV
510
PKAWSDLCPI YDGLSEANQ
Length:519
Mass (Da):55,811
Last modified:November 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iBFFB5B4CD0007702
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti69D → V in AAC49828 (PubMed:9322748).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U44851 Genomic DNA Translation: AAA86659.1
U44430 mRNA Translation: AAC49828.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U44851 Genomic DNA Translation: AAA86659.1
U44430 mRNA Translation: AAC49828.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GYCX-ray1.90A21-519[»]
ProteinModelPortaliQ12718
SMRiQ12718
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiAA1 Auxiliary Activities 1

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17211

Miscellaneous databases

EvolutionaryTraceiQ12718

Family and domain databases

Gene3Di2.60.40.420, 3 hits
InterProiView protein in InterPro
IPR001117 Cu-oxidase
IPR011706 Cu-oxidase_2
IPR011707 Cu-oxidase_3
IPR033138 Cu_oxidase_CS
IPR008972 Cupredoxin
PfamiView protein in Pfam
PF00394 Cu-oxidase, 1 hit
PF07731 Cu-oxidase_2, 1 hit
PF07732 Cu-oxidase_3, 1 hit
SUPFAMiSSF49503 SSF49503, 3 hits
PROSITEiView protein in PROSITE
PS00079 MULTICOPPER_OXIDASE1, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLAC2_TRAVE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q12718
Secondary accession number(s): Q12716
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: December 5, 2018
This is version 94 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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