CAOA2_ARATH
ID CAOA2_ARATH Reviewed; 677 AA.
AC F4IAX0; Q9C6V8; Q9C6V9;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Amine oxidase [copper-containing] alpha 2, peroxisomal {ECO:0000303|PubMed:31862580};
DE Short=AtCuAO8 {ECO:0000303|PubMed:28383668};
DE Short=AtCuAOalpha2 {ECO:0000303|PubMed:31862580};
DE EC=1.4.3.21 {ECO:0000269|PubMed:28383668};
GN Name=CuAOalpha2 {ECO:0000303|PubMed:31862580};
GN Synonyms=CuAO8 {ECO:0000303|PubMed:28383668};
GN OrderedLocusNames=At1g31690 {ECO:0000312|Araport:AT1G31690};
GN ORFNames=F27M3.11 {ECO:0000312|EMBL:AAG60148.1},
GN F27M3.12 {ECO:0000312|EMBL:AAG60151.1};
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 FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=cv. Columbia;
RX PubMed=28383668; DOI=10.1093/jxb/erx105;
RA Gross F., Rudolf E.-E., Thiele B., Durner J., Astier J.;
RT "Copper amine oxidase 8 regulates arginine-dependent nitric oxide
RT production in Arabidopsis thaliana.";
RL J. Exp. Bot. 68:2149-2162(2017).
RN [4]
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:28383668). Involved in putrescine catabolism in
CC peroxisomes in response to salt stress (PubMed:28383668). Regulates
CC arginine-dependent nitric oxide (NO) production, a key signaling
CC molecule regulating a wide range of physiological processes including
CC responses to salt stress, by influencing arginine bioavailability
CC (PubMed:28383668). Modulates primary root growth (PubMed:28383668).
CC {ECO:0000269|PubMed:28383668}.
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:28383668};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16154;
CC Evidence={ECO:0000269|PubMed:28383668};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P46883};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P12807};
CC Note=Binds 1 copper ion per subunit (By similarity). Can also use zinc
CC ion as cofactor (By similarity). {ECO:0000250|UniProtKB:P12807,
CC ECO:0000250|UniProtKB:P46883};
CC -!- COFACTOR:
CC Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
CC Evidence={ECO:0000250|UniProtKB:P46883};
CC Note=Contains 1 topaquinone per subunit.
CC {ECO:0000250|UniProtKB:P46883};
CC -!- PATHWAY: Amine and polyamine degradation; putrescine degradation.
CC {ECO:0000269|PubMed:28383668}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A0A1S4BDC4}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:F4IAX1}.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in leaves.
CC {ECO:0000269|PubMed:31862580}.
CC -!- DEVELOPMENTAL STAGE: In young seedlings, first observed in hydathodes
CC and borders of new emerging cotyledons and in leaf primordia
CC (PubMed:31862580). Accumulates in expanding leaves (PubMed:31862580).
CC {ECO:0000269|PubMed:31862580}.
CC -!- INDUCTION: Induced transiently by auxin (IAA) (PubMed:31862580).
CC Accumulates during dehydration recovery, wounding and treatment with
CC putrescine (Put) and jasmonic acid (MeJA) (PubMed:31862580). Repressed
CC by abscisic acid (ABA) and salicylic acid (SA) (PubMed:31862580).
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 -!- DISRUPTION PHENOTYPE: Decreased nitric oxide (NO) production in
CC seedlings after elicitor treatment with 2,6-dichloroisonicotinic acid
CC (INA) in root tips and salt stress associated with a reduced arginine
CC availability but with a normal nitrate reductase activity in plants
CC (PubMed:28383668). Reduced primary root length (PubMed:28383668).
CC {ECO:0000269|PubMed:28383668}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG60148.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG60151.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC074360; AAG60148.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC074360; AAG60151.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31383.1; -; Genomic_DNA.
DR RefSeq; NP_174450.2; NM_102904.3.
DR SMR; F4IAX0; -.
DR STRING; 3702.AT1G31690.1; -.
DR PaxDb; F4IAX0; -.
DR PRIDE; F4IAX0; -.
DR ProteomicsDB; 197390; -.
DR EnsemblPlants; AT1G31690.1; AT1G31690.1; AT1G31690.
DR GeneID; 840056; -.
DR Gramene; AT1G31690.1; AT1G31690.1; AT1G31690.
DR KEGG; ath:AT1G31690; -.
DR Araport; AT1G31690; -.
DR TAIR; locus:2028636; AT1G31690.
DR eggNOG; KOG1186; Eukaryota.
DR HOGENOM; CLU_011500_5_4_1; -.
DR InParanoid; F4IAX0; -.
DR OMA; PVVWSVF; -.
DR OrthoDB; 1320015at2759; -.
DR BioCyc; ARA:AT1G31690-MON; -.
DR BRENDA; 1.4.3.21; 399.
DR UniPathway; UPA00188; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4IAX0; baseline and differential.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
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:0090465; P:arginine homeostasis; IMP:UniProtKB.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IMP:UniProtKB.
DR GO; GO:0080022; P:primary root development; IMP:UniProtKB.
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:0009651; P:response to salt stress; IMP: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 Copper; Disulfide bond; Manganese; Metal-binding; Oxidoreductase;
KW Peroxisome; Reference proteome; TPQ.
FT CHAIN 1..677
FT /note="Amine oxidase [copper-containing] alpha 2,
FT peroxisomal"
FT /id="PRO_5003309597"
FT ACT_SITE 322
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT ACT_SITE 410
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 320..331
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 407..412
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 466
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 468
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 477
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 617
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 618
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 628
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT MOD_RES 410
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT DISULFID 341..367
FT /evidence="ECO:0000250|UniProtKB:Q43077"
SQ SEQUENCE 677 AA; 76674 MW; A4A45980995368DC CRC64;
MAQVHLTIFI FSSIFVISSS SFIPPPHPFD PLTETELKLV RNIINKSYPI GHNHKFTFQY
VGLNEPEKSL VLSWHSSPDR NVKPPPRQAF VIARDKGMSR EIVIDFSTRA IVSNKIHVGN
GNPMLTIDEQ QAATAVVQKY KPFCDSIIKR GLNLSEVVVT SSTMGWFGET KTKRFIRTIP
FYLNGSVNTY LRPIEGMTII VNLDQMKVTG FKDRFTGPMP KANGREYRIS KLKPPFGPSL
RSAVVFQPDG PGFKIDGHVV RWANWEFHMS FDVRAGLVIS LASIFDMDMN RYRQVLYKGH
LSEMFVPYMD PNDDWYFISY LDCGEFGCGQ TAVSLEPYTD CPPNAAFMDG IFPGQDGTPT
KISNVMCIFE KYAGDIMWRH TEAEVPGLKI TEVRPDVSLV ARMVTTVGNY DYIIEYEFKP
SGSIKMGVGL TGVLEVKPVE YVHTSEIKED DIYGTIVADN TVGVNHDHFV TFRLDLDIDG
TENSFVRTEL VTKRTPKSVN TPRKSYWTTK RNTAKTEADA RVKLGLRAEE LVVVNPTKKT
KHGNEVGYRL LPGPASSPLL VQDDYPQIRA AFTNYNVWIT PYNKSEVWAS GLYADRSQGD
DTLAVWSQRD REIENKDIVM WYTVGFHHVP CQEDFPTMPT MFGGFELRPT NFFEQNPVLK
AKPFNLTTIP KCTTKNE
