CAOA3_ARATH
ID CAOA3_ARATH Reviewed; 681 AA.
AC F4IAX1; Q8GZ62; Q9C6W0; Q9C6W1;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Amine oxidase [copper-containing] alpha 3, peroxisomal {ECO:0000303|PubMed:31862580};
DE Short=AtCuAO2 {ECO:0000303|PubMed:23915037};
DE Short=AtCuAOalpha3 {ECO:0000303|PubMed:31862580};
DE Short=Copper amine oxidase 2 {ECO:0000303|PubMed:23915037};
DE EC=1.4.3.21 {ECO:0000269|PubMed:23915037};
GN Name=CuAOalpha3 {ECO:0000303|PubMed:31862580};
GN Synonyms=CuAO2 {ECO:0000303|PubMed:23915037};
GN OrderedLocusNames=At1g31710 {ECO:0000312|Araport:AT1G31710};
GN ORFNames=F27M3.10 {ECO:0000312|EMBL:AAG60145.1},
GN F27M3.9 {ECO:0000312|EMBL:AAG60142.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-681.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INDUCTION BY WOUNDING AND JASMONATE, GENE FAMILY, AND
RP NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=23915037; DOI=10.1186/1471-2229-13-109;
RA Planas-Portell J., Gallart M., Tiburcio A.F., Altabella T.;
RT "Copper-containing amine oxidases contribute to terminal polyamine
RT oxidation in peroxisomes and apoplast of Arabidopsis thaliana.";
RL BMC Plant Biol. 13:109-109(2013).
RN [6]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION BY JASMONATE; ABSCISIC
RP ACID; SALICYLIC ACID; DEHYDRATION RECOVERY; WOUNDING; PUTRESCINE AND AUXIN,
RP GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=31862580; DOI=10.1016/j.plaphy.2019.11.037;
RA Fraudentali I., Ghuge S.A., Carucci A., Tavladoraki P., Angelini R.,
RA Rodrigues-Pousada R.A., Cona A.;
RT "Developmental, hormone- and stress-modulated expression profiles of four
RT members of the Arabidopsis copper-amine oxidase gene family.";
RL Plant Physiol. Biochem. 147:141-160(2020).
CC -!- FUNCTION: Copper amine oxidase that can use putrescine and spermidine
CC as substrates (PubMed:23915037). Involved in putrescine catabolism in
CC peroxisomes (PubMed:23915037). {ECO:0000269|PubMed:23915037}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58001; EC=1.4.3.21;
CC Evidence={ECO:0000269|PubMed:23915037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16154;
CC Evidence={ECO:0000269|PubMed:23915037};
CC -!- PATHWAY: Amine and polyamine degradation; putrescine degradation.
CC {ECO:0000269|PubMed:23915037}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:23915037}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4IAX1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4IAX1-2; Sequence=VSP_061527;
CC -!- TISSUE SPECIFICITY: Mostly expressed in stems, and, at lower levels, in
CC flowers and leaves (PubMed:23915037). Mainly detectable in stipules,
CC hypocotyls and roots (PubMed:31862580). {ECO:0000269|PubMed:23915037,
CC ECO:0000269|PubMed:31862580}.
CC -!- DEVELOPMENTAL STAGE: In young seedlings, expressed in hypocotyls,
CC hypocotyl/root junctions and roots, especially in vascular tissue (e.g.
CC xylem and metaxylem) (PubMed:31862580). Observed in shoot apex,
CC associated with stipules (PubMed:31862580).
CC {ECO:0000269|PubMed:31862580}.
CC -!- INDUCTION: Induced transiently by auxin (IAA) (PubMed:31862580).
CC Induced by jasmonic acid (MeJA) (PubMed:23915037, PubMed:31862580).
CC Accumulates during dehydration recovery and treatment with putrescine
CC (Put) (PubMed:31862580). Repressed by abscisic acid (ABA) and salicylic
CC acid (SA) (PubMed:31862580). Triggered by wounding (PubMed:23915037,
CC PubMed:31862580). {ECO:0000269|PubMed:23915037,
CC ECO:0000269|PubMed:31862580}.
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000250|UniProtKB:P46883}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG60142.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC41866.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC074360; AAG60142.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC074360; AAG60145.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31384.1; -; Genomic_DNA.
DR EMBL; BT011581; AAS46634.1; -; mRNA.
DR EMBL; BT012254; AAS76741.1; -; mRNA.
DR EMBL; AK117190; BAC41866.1; ALT_INIT; mRNA.
DR RefSeq; NP_174452.2; NM_102906.4.
DR SMR; F4IAX1; -.
DR STRING; 3702.AT1G31710.1; -.
DR PaxDb; F4IAX1; -.
DR PRIDE; F4IAX1; -.
DR ProteomicsDB; 197361; -.
DR EnsemblPlants; AT1G31710.1; AT1G31710.1; AT1G31710.
DR GeneID; 840058; -.
DR Gramene; AT1G31710.1; AT1G31710.1; AT1G31710.
DR KEGG; ath:AT1G31710; -.
DR Araport; AT1G31710; -.
DR TAIR; locus:2028606; AT1G31710.
DR eggNOG; KOG1186; Eukaryota.
DR HOGENOM; CLU_011500_5_4_1; -.
DR InParanoid; F4IAX1; -.
DR OMA; CYMYIVA; -.
DR OrthoDB; 1320015at2759; -.
DR BioCyc; ARA:AT1G31710-MON; -.
DR BRENDA; 1.4.3.21; 399.
DR UniPathway; UPA00188; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4IAX1; baseline and differential.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0052595; F:aliphatic-amine oxidase activity; IDA:UniProtKB.
DR GO; GO:0052594; F:aminoacetone:oxygen oxidoreductase(deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0008131; F:primary amine oxidase activity; IBA:GO_Central.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0009308; P:amine metabolic process; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009733; P:response to auxin; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:1904585; P:response to putrescine; IEP:UniProtKB.
DR GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR Gene3D; 2.70.98.20; -; 1.
DR InterPro; IPR000269; Cu_amine_oxidase.
DR InterPro; IPR015798; Cu_amine_oxidase_C.
DR InterPro; IPR036460; Cu_amine_oxidase_C_sf.
DR InterPro; IPR016182; Cu_amine_oxidase_N-reg.
DR InterPro; IPR015800; Cu_amine_oxidase_N2.
DR InterPro; IPR015802; Cu_amine_oxidase_N3.
DR PANTHER; PTHR10638; PTHR10638; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR Pfam; PF02727; Cu_amine_oxidN2; 1.
DR Pfam; PF02728; Cu_amine_oxidN3; 1.
DR SUPFAM; SSF49998; SSF49998; 1.
DR SUPFAM; SSF54416; SSF54416; 2.
DR PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Copper; Disulfide bond; Manganese; Metal-binding;
KW Oxidoreductase; Peroxisome; Reference proteome; TPQ.
FT CHAIN 1..681
FT /note="Amine oxidase [copper-containing] alpha 3,
FT peroxisomal"
FT /id="PRO_5003311420"
FT ACT_SITE 325
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT ACT_SITE 413
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 323..334
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 410..415
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 470
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 472
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 481
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 621
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 622
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 632
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT MOD_RES 413
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT DISULFID 344..370
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT VAR_SEQ 265..681
FT /note="Missing (in isoform 2)"
FT /id="VSP_061527"
FT CONFLICT 407
FT /note="V -> A (in Ref. 4; BAC41866)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="K -> E (in Ref. 4; BAC41866)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 681 AA; 76711 MW; 32AF204CCC0A7CBF CRC64;
MAPLHFTILI LFSFVIVVSS SSFTPPRHPF DPLTETELKL VRTIINKSYP VGPNHKFTFQ
YVGLNEPNKS LVLSWYSSPN HTIKPPPRQA FVIARDNGKT REIVLDFSSR AIVSDKIHVG
NGYPMLSNDE QEASTELVVK FKPFIDSVAK RGLNVSEIVF TTSTIGWYGE TKAEAERVIR
LMPFYLDGTV NMYLRPIEGM TIIVNLDEMK VSEFKDRSVV TMPIANGTEY RISKLNPPFG
PTLHNAVLLQ PDGPGFKVDG HIVRWANWEF HISFDVRAGI VISLASLFDT DVNKYRQVLY
KGHLSEMFIP YMDPSDDWYF ITYLDCGDFG CGQCAVSLQP YTDCPAGAVF MDGIFAGQDG
TPAKIPKVMC IFEKYAGDIM WRHTEAEIPN LEITEVRPDV SLVARIVTTV GNYDYIVDYE
FKPSGSIKMG VGLTGVLEVK PVEYIHTSEI KLGEDIHGTI VADNTVGVNH DHFVTFRLHL
DIDGTENSFV RNELVTTRSP KSVNTPRKTY WTTKPKTAKT EAEARVKLGL KAEELVVVNP
NRKTKHGNEV GYRLLHGSAA GPLLAQDDFP QIRAAFTNYN VWITPYNRSE VWAGGLYADR
SQGDDTLAVW SQRNRKIEKE DIVMWYTVGF HHVPSQEDYP TMPTLSGGFE LRPTNFFERN
PVLKTKPVKV TTARKCTPKN D
