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LAC12_ORYSJ
ID   LAC12_ORYSJ             Reviewed;         574 AA.
AC   B9FJH4; A0A0P0WND9; Q0DHL2; Q0DHL3; Q65XF7;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   11-MAY-2016, sequence version 2.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Laccase-12;
DE            EC=1.10.3.2;
DE   AltName: Full=Benzenediol:oxygen oxidoreductase 12;
DE   AltName: Full=Diphenol oxidase 12;
DE   AltName: Full=Urishiol oxidase 12;
DE   Flags: Precursor;
GN   Name=LAC12; OrderedLocusNames=Os05g0458500, LOC_Os05g38410;
GN   ORFNames=OJ1362_D02.9, OsJ_018046;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (OS05G0458500 AND
RP   OS05G0458600).
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA   Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA   Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA   Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT   "A fine physical map of the rice chromosome 5.";
RL   Mol. Genet. Genomics 274:337-345(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (OS05G0458500 AND
RP   OS05G0458600).
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (OS05G0458500 AND
RP   OS05G0458600).
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
CC   -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC       products. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds 4 Cu cations per monomer. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAU44018.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAF17660.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EEE63977.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC105770; AAU44018.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008211; BAF17660.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014961; BAS94387.1; -; Genomic_DNA.
DR   EMBL; CM000142; EEE63977.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_015638168.1; XM_015782682.1.
DR   RefSeq; XP_015638169.1; XM_015782683.1.
DR   AlphaFoldDB; B9FJH4; -.
DR   SMR; B9FJH4; -.
DR   STRING; 4530.OS05T0458500-00; -.
DR   PaxDb; B9FJH4; -.
DR   PRIDE; B9FJH4; -.
DR   EnsemblPlants; Os05t0458500-00; Os05t0458500-00; Os05g0458500.
DR   EnsemblPlants; Os05t0458600-01; Os05t0458600-01; Os05g0458600.
DR   GeneID; 4339003; -.
DR   GeneID; 4339004; -.
DR   Gramene; Os05t0458500-00; Os05t0458500-00; Os05g0458500.
DR   Gramene; Os05t0458600-01; Os05t0458600-01; Os05g0458600.
DR   KEGG; osa:4339003; -.
DR   KEGG; osa:4339004; -.
DR   eggNOG; KOG1263; Eukaryota.
DR   OMA; CTISGVW; -.
DR   OrthoDB; 454773at2759; -.
DR   Proteomes; UP000000763; Chromosome 5.
DR   Proteomes; UP000007752; Chromosome 5.
DR   Proteomes; UP000059680; Chromosome 5.
DR   ExpressionAtlas; B9FJH4; baseline and differential.
DR   Genevisible; Q0DHL2; OS.
DR   GO; GO:0048046; C:apoplast; 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   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd13849; CuRO_1_LCC_plant; 1.
DR   CDD; cd13875; CuRO_2_LCC_plant; 1.
DR   CDD; cd13897; CuRO_3_LCC_plant; 1.
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; IPR033138; Cu_oxidase_CS.
DR   InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR034288; CuRO_1_LCC.
DR   InterPro; IPR034285; CuRO_2_LCC.
DR   InterPro; IPR034289; CuRO_3_LCC.
DR   InterPro; IPR017761; Laccase.
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.
DR   TIGRFAMs; TIGR03389; laccase; 1.
DR   PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
DR   PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE   3: Inferred from homology;
KW   Apoplast; Copper; Glycoprotein; Lignin degradation; Metal-binding;
KW   Oxidoreductase; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..574
FT                   /note="Laccase-12"
FT                   /id="PRO_0000291897"
FT   DOMAIN          35..151
FT                   /note="Plastocyanin-like 1"
FT   DOMAIN          161..314
FT                   /note="Plastocyanin-like 2"
FT   DOMAIN          424..558
FT                   /note="Plastocyanin-like 3"
FT   BINDING         85
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         87
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         132
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         475
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         478
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         480
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         537
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         538
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         539
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         543
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        190
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        206
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        242
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        302
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        335
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        342
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        381
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        388
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        398
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        434
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        441
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        447
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   574 AA;  62348 MW;  27DD915DD4F41C13 CRC64;
     MAAASSVLRC CLLVAALMTL SAMGAEAITR QYLFDVQTTS VTRLCSTKSI VTVNGQYPGP
     TLFAREGDHV EVTVVNHSPY NMSIHWHGIR QLLSGWADGP SYITQCPIQP GGSYVYRFTI
     TGQRGTLWWH AHISWLRATV HGPMVILPPA GVGYPFPAPH EEVPIMFGEW WNNDTEAVIS
     QALQTGGGPN ISDAYTLNGL PGPLYNCSAQ DTFKLKVKPG KTYMLRLINA ALNDELFFSI
     ANHTLTVVDV DALYVKPFTV DTLIIAPGQT SNVLLTAKPT YPGASYYMLA RPYTTTQGTF
     DNTTVAGVLE YDDPCPTTAA GKIVPIFSPT LPQINDTNAV SNFTAKLRSL ASAGYPAAVP
     QQVDHRFFFT VGLGTHPCAV NGTCQGPNGS RFAASINNVS FVLPATALLQ SHFAGKSKGV
     YASNFPYYPL NPFNYTGTPP NNTNVMNGTK VLVLPYGANV ELVMQDTSIL GAESHPLHLH
     GFNFFVVGQG FGNFDPINDP AKFNLYDPVE RNTVGVPAGG WVAIRFHADN PGVWFMHCHL
     EVHMSWGLKM AWLVLDGSRP DQKLPPPPLD LPKC
 
 
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