ASO_ARATH
ID ASO_ARATH Reviewed; 573 AA.
AC Q8LPL3;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=L-ascorbate oxidase {ECO:0000303|PubMed:15883131};
DE Short=AAO {ECO:0000303|PubMed:15883131};
DE Short=AO {ECO:0000303|PubMed:27255930};
DE Short=ASO {ECO:0000305};
DE Short=Ascorbase {ECO:0000303|PubMed:15883131, ECO:0000303|PubMed:27255930};
DE EC=1.10.3.3 {ECO:0000269|PubMed:15883131};
DE Flags: Precursor;
GN Name=AAO {ECO:0000303|PubMed:15883131};
GN Synonyms=AO {ECO:0000303|PubMed:27255930};
GN OrderedLocusNames=At5g21100 {ECO:0000312|Araport:AT5G21100};
GN ORFNames=T10F18.130 {ECO:0000312|EMBL:AAO73900.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=cv. Columbia;
RX PubMed=15883131; DOI=10.1093/jxb/eri167;
RA Yamamoto A., Bhuiyan M.N., Waditee R., Tanaka Y., Esaka M., Oba K.,
RA Jagendorf A.T., Takabe T.;
RT "Suppressed expression of the apoplastic ascorbate oxidase gene increases
RT salt tolerance in tobacco and Arabidopsis plants.";
RL J. Exp. Bot. 56:1785-1796(2005).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND REPRESSION BY TURNIP MOSAIC VIRUS.
RC STRAIN=cv. Columbia;
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:15883131, PubMed:27255930). The oxidation
CC of AsA represses responses to high salinity and oxidative stress
CC conditions such as vegetative growth and seed production reductions
CC (PubMed:15883131). Negative regulator of defense responses toward
CC incompatible Turnip mosaic virus (TuMV strain UK1) by preventing
CC jasmonic acid (JA)- dependent accumulation of ascorbic acid (AsA, AS)
CC and dehydroascobic acid (DHA) (PubMed:27255930).
CC {ECO:0000269|PubMed:15883131, 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:0000269|PubMed:15883131};
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:0000269|PubMed:15883131}.
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) (PubMed:27255930). When the plant
CC is infected by a compatible TuMV strain (UK1 m2), the down-regulation
CC is transient and last two days (PubMed:27255930).
CC {ECO:0000269|PubMed:27255930}.
CC -!- DISRUPTION PHENOTYPE: Impaired ascorbate oxidase activity and reduced
CC apoplastic hydrogen peroxide H(2)O(2) and ascorbate peroxidase
CC accumulation, especially in high salinity (PubMed:15883131). Short
CC stems and late flowering (PubMed:15883131). Slightly increased
CC ascorbate (AsA) contents in the apoplasm but lower monodehydroascorbate
CC (DHA) contents (PubMed:15883131, PubMed:27255930). Increased tolerance
CC for high salinity during vegetative growth, seed production and seed
CC germination (PubMed:15883131). Higher resistance to oxidative stress
CC agents such as methyl viologen (MV) and hydrogen peroxide H(2)O(2)
CC (PubMed:15883131). Enhanced resistance to Turnip mosaic virus (TuMV)
CC associated with an increased accumulation of ascorbic acid (AsA, AS)
CC and dehydroascobic acid (DHA) due to a reduction of AS oxidation and
CC activation of AS recycling (PubMed:27255930).
CC {ECO:0000269|PubMed:15883131, ECO:0000269|PubMed:27255930}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; AC140977; AAO73900.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92931.1; -; Genomic_DNA.
DR EMBL; AY099586; AAM20438.1; -; mRNA.
DR EMBL; BT003407; AAO30070.1; -; mRNA.
DR RefSeq; NP_197609.1; NM_122118.5.
DR AlphaFoldDB; Q8LPL3; -.
DR SMR; Q8LPL3; -.
DR STRING; 3702.AT5G21100.1; -.
DR PaxDb; Q8LPL3; -.
DR PRIDE; Q8LPL3; -.
DR ProteomicsDB; 185385; -.
DR EnsemblPlants; AT5G21100.1; AT5G21100.1; AT5G21100.
DR GeneID; 832234; -.
DR Gramene; AT5G21100.1; AT5G21100.1; AT5G21100.
DR KEGG; ath:AT5G21100; -.
DR Araport; AT5G21100; -.
DR TAIR; locus:2178973; AT5G21100.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_8_3_1; -.
DR InParanoid; Q8LPL3; -.
DR OMA; CKEGIVM; -.
DR OrthoDB; 454773at2759; -.
DR PhylomeDB; Q8LPL3; -.
DR BioCyc; ARA:AT5G21100-MON; -.
DR UniPathway; UPA00263; -.
DR PRO; PR:Q8LPL3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LPL3; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0008447; F:L-ascorbate oxidase activity; IMP: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; IMP:UniProtKB.
DR GO; GO:1901001; P:negative regulation of response to salt stress; IMP:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IMP: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 1: Evidence at protein level;
KW Copper; Disulfide bond; Glycoprotein; Metal-binding; Oxidoreductase;
KW Plant defense; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..573
FT /note="L-ascorbate oxidase"
FT /id="PRO_5014312243"
FT DOMAIN 30..145
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 154..318
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 423..545
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT BINDING 80
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 82
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 124
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 126
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 464
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 467
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 469
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="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P37064"
FT BINDING 527
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 528
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 532
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 537
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 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 336
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 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 39..220
FT /evidence="ECO:0000250|UniProtKB:P37064"
FT DISULFID 101..560
FT /evidence="ECO:0000250|UniProtKB:P37064"
FT DISULFID 197..212
FT /evidence="ECO:0000250|UniProtKB:P37064"
SQ SEQUENCE 573 AA; 64266 MW; 2BF025493692355D CRC64;
MAVIVWWLLT VVVVAFHSAS AAVVESTWEV EYKYWWPDCK EGIVMAINGQ FPGPTIDAVA
GDTVIIHVVN KLSTEGVVIH WHGIRQKGTP WADGAAGVTQ CPINPGETFT YKFIVDKAGT
HFYHGHYGMQ RSSGLYGMLI VRSPKERLIY DGEFNLLLSD WWHQSIHAQE LALSSRPMRW
IGEPQSLLIN GRGQFNCSQA AYFNKGGEKD VCTFKENDQC APQTLRVEPN RVYRLRIAST
TALASLNLAV QGHQLVVVEA DGNYVAPFTV NDIDVYSGET YSVLLKTNAL PSKKYWISVG
VRGREPKTPQ ALTVINYVDA TESRPSHPPP VTPIWNDTDR SKSFSKKIFA AKGYPKPPEK
SHDQLILLNT QNLYEDYTKW SINNVSLSVP VTPYLGSIRY GLKSAYDLKS PAKKLIMDNY
DIMKPPPNPN TTKGSGIYNF AFGIVVDVIL QNANVLKGVI SEIHPWHIHG HDFWVLGYGE
GKFKPGIDEK TFNLKNPPLR NTVVLYPFGW TAIRFVTDNP GVWFFHCHIE PHLHMGMGVV
FVEGVDRIGK MEIPDEALGC GLTRKWLMNR GRP
