ASO_BRARP
ID ASO_BRARP Reviewed; 570 AA.
AC M4DUF2;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=L-ascorbate oxidase {ECO:0000303|PubMed:27255930};
DE Short=AAO {ECO:0000305};
DE Short=AO {ECO:0000303|PubMed:27255930};
DE Short=ASO {ECO:0000305};
DE Short=Ascorbase {ECO:0000303|PubMed:27255930};
DE EC=1.10.3.3 {ECO:0000250|UniProtKB:Q8LPL3};
DE Flags: Precursor;
GN Name=AO {ECO:0000303|PubMed:27255930};
OS Brassica rapa subsp. pekinensis (Chinese cabbage) (Brassica pekinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=51351;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chiifu-401-42;
RX PubMed=21873998; DOI=10.1038/ng.919;
RG Brassica rapa Genome Sequencing Project Consortium;
RA Wang X., Wang H., Wang J., Sun R., Wu J., Liu S., Bai Y., Mun J.H.,
RA Bancroft I., Cheng F., Huang S., Li X., Hua W., Wang J., Wang X.,
RA Freeling M., Pires J.C., Paterson A.H., Chalhoub B., Wang B., Hayward A.,
RA Sharpe A.G., Park B.S., Weisshaar B., Liu B., Li B., Liu B., Tong C.,
RA Song C., Duran C., Peng C., Geng C., Koh C., Lin C., Edwards D., Mu D.,
RA Shen D., Soumpourou E., Li F., Fraser F., Conant G., Lassalle G.,
RA King G.J., Bonnema G., Tang H., Wang H., Belcram H., Zhou H., Hirakawa H.,
RA Abe H., Guo H., Wang H., Jin H., Parkin I.A., Batley J., Kim J.S., Just J.,
RA Li J., Xu J., Deng J., Kim J.A., Li J., Yu J., Meng J., Wang J., Min J.,
RA Poulain J., Wang J., Hatakeyama K., Wu K., Wang L., Fang L., Trick M.,
RA Links M.G., Zhao M., Jin M., Ramchiary N., Drou N., Berkman P.J., Cai Q.,
RA Huang Q., Li R., Tabata S., Cheng S., Zhang S., Zhang S., Huang S.,
RA Sato S., Sun S., Kwon S.J., Choi S.R., Lee T.H., Fan W., Zhao X., Tan X.,
RA Xu X., Wang Y., Qiu Y., Yin Y., Li Y., Du Y., Liao Y., Lim Y., Narusaka Y.,
RA Wang Y., Wang Z., Li Z., Wang Z., Xiong Z., Zhang Z.;
RT "The genome of the mesopolyploid crop species Brassica rapa.";
RL Nat. Genet. 43:1035-1039(2011).
RN [2]
RP FUNCTION, REPRESSION BY TURNIP MOSAIC VIRUS, AND INDUCTION BY JASMONIC ACID
RP AND HYDROGEN PEROXIDE.
RC STRAIN=cv. Aki-masari, and cv. Yukihime-kabu;
RX PubMed=27255930; DOI=10.1093/jxb/erw223;
RA Fujiwara A., Togawa S., Hikawa T., Matsuura H., Masuta C., Inukai T.;
RT "Ascorbic acid accumulates as a defense response to Turnip mosaic virus in
RT resistant Brassica rapa cultivars.";
RL J. Exp. Bot. 67:4391-4402(2016).
CC -!- FUNCTION: Ascorbate oxidase involved in a redox system involving
CC ascorbic acid (AsA) (PubMed:27255930). The oxidation of AsA represses
CC responses to high salinity and oxidative stress conditions such as
CC vegetative growth and seed production reductions (By similarity).
CC Negative regulator of defense responses toward incompatible Turnip
CC mosaic virus (TuMV strain UK1) by preventing jasmonic acid
CC (JA)- dependent accumulation of ascorbic acid (AsA, AS) and
CC dehydroascobic acid (DHA) (PubMed:27255930).
CC {ECO:0000250|UniProtKB:Q8LPL3, ECO:0000269|PubMed:27255930}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 L-ascorbate + O2 = 2 H2O + 4 monodehydro-L-ascorbate
CC radical; Xref=Rhea:RHEA:30243, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:59513; EC=1.10.3.3;
CC Evidence={ECO:0000250|UniProtKB:Q8LPL3};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P37064};
CC Note=Binds 4 Cu cations per monomer. {ECO:0000250|UniProtKB:P37064};
CC -!- PATHWAY: Cofactor degradation; L-ascorbate degradation.
CC {ECO:0000250|UniProtKB:Q8LPL3}.
CC -!- SUBUNIT: Dimer. {ECO:0000250|UniProtKB:P37064}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P37064}.
CC -!- INDUCTION: Repressed progressively during incompatible Turnip mosaic
CC virus (TuMV) infection (strain UK1) in resistant cultivars (e.g. cv.
CC Aki-masari) but not in susceptible cultivars (e.g. cv. Yukihime-kabu)
CC (PubMed:27255930). When the plant is infected by a compatible TuMV
CC strain (UK1 m2), the down-regulation is transient and last two days
CC (PubMed:27255930). Induced by jasmonic acid (JA) and hydrogen peroxide
CC H(2)O(2) treatments (PubMed:27255930). {ECO:0000269|PubMed:27255930}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; CM001635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M4DUF2; -.
DR SMR; M4DUF2; -.
DR STRING; 51351.M4DUF2; -.
DR EnsemblPlants; Bra020145.1; Bra020145.1-P; Bra020145.
DR Gramene; Bra020145.1; Bra020145.1-P; Bra020145.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_8_3_1; -.
DR InParanoid; M4DUF2; -.
DR OMA; DLWHISS; -.
DR UniPathway; UPA00263; -.
DR Proteomes; UP000011750; Chromosome A02.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0008447; F:L-ascorbate oxidase activity; ISS:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0019854; P:L-ascorbic acid catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0050687; P:negative regulation of defense response to virus; IDA:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR CDD; cd13893; CuRO_3_AAO; 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; IPR034267; CuRO_3_AAO.
DR InterPro; IPR017760; L-ascorbate_oxidase_pln.
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; TIGR03388; ascorbase; 1.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 2: Evidence at transcript level;
KW Copper; Disulfide bond; Glycoprotein; Metal-binding; Oxidoreductase;
KW Plant defense; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..570
FT /note="L-ascorbate oxidase"
FT /evidence="ECO:0000255"
FT /id="PRO_5004051517"
FT DOMAIN 33..140
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 154..317
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 426..543
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT BINDING 77
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:P37064"
FT BINDING 79
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:P37064"
FT BINDING 121
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:P37064"
FT BINDING 123
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:P37064"
FT BINDING 463
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:P37064"
FT BINDING 466
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:P37064"
FT BINDING 468
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:P37064"
FT BINDING 525
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:P37064"
FT BINDING 526
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:P37064"
FT BINDING 527
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:P37064"
FT BINDING 531
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:P37064"
FT BINDING 536
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:P37064"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 36..219
FT /evidence="ECO:0000250|UniProtKB:P37064"
FT DISULFID 98..557
FT /evidence="ECO:0000250|UniProtKB:P37064"
FT DISULFID 197..211
FT /evidence="ECO:0000250|UniProtKB:P37064"
SQ SEQUENCE 570 AA; 63250 MW; 92CB2E18AFA1CF20 CRC64;
MGMWWIVAVA ILAHTASAAV REYAWEVEYK FGWPDCKEGM VMAVNGQFPG PTIHALAGDT
IVVHLTNKLA TEGLVIHWHG IRQLGSPWAD GAAGVTQCAI SPGETFTYNF TVDKPGTHFY
HGHYGMQRSA GLYGSLIIDV AKGKKEPLRY DGEFNLLLSD WWHEDVLSQE IGLSSRPMRW
IGEAQSILIN GRGQFNCSLA AQFSSTSLPT CTFKEGDQCA PQRLHVEPNK TYRIRLASST
ALASLNFAVQ GHKLVVVEAD GNYITPFTTD DIDIYSGETY SVLLTTDQDP SQNYYITAGV
RGRKPNTPPA LTVLNYVTAP SSQLPTSPPP ETPRWNDFDR SKNFSKKIFA AMGSPSPPET
FDERLILLNT QNLIEGFTKW AINNVSLAVP GTPYLGSVKY NLRTGFNRSS PPKDYPVDYD
IMTPPRNRNA KQGNVSCVFP FNVTVDVILQ NANGLNANAS EIHPWHLHGH DFWVLGYGEG
KFKPGVDEKT YNLKNPPLRN TVALYPYGWT ALRFVTDNPG VWFFHCHIEP HLHMGMGVVF
AEGLNRIGKV PDEALGCGLT KQFLMNRNNP
