CAOG1_ARATH
ID CAOG1_ARATH Reviewed; 712 AA.
AC Q8H1H9; Q84W14; Q9SI68;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Amine oxidase [copper-containing] gamma 1 {ECO:0000303|PubMed:31862580};
DE Short=AtCuAO1 {ECO:0000303|PubMed:21471330, ECO:0000303|PubMed:23915037};
DE Short=AtCuAOgamma1 {ECO:0000303|PubMed:31862580};
DE Short=Copper amine oxidase 1 {ECO:0000303|PubMed:21471330};
DE EC=1.4.3.21 {ECO:0000269|PubMed:23915037};
DE AltName: Full=Primary amine oxidase 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=CuAOgamma1 {ECO:0000303|PubMed:31862580};
GN Synonyms=CuAO1 {ECO:0000303|PubMed:21471330, ECO:0000303|PubMed:23915037};
GN OrderedLocusNames=At1g62810 {ECO:0000312|Araport:AT1G62810};
GN ORFNames=F23N19.18 {ECO:0000312|EMBL:AAF19542.1};
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].
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, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND INDUCTION BY ABSCISIC ACID.
RC STRAIN=cv. Columbia, and cv. No-0;
RX PubMed=21471330; DOI=10.1093/mp/ssr023;
RA Wimalasekera R., Villar C., Begum T., Scherer G.F.E.;
RT "COPPER AMINE OXIDASE1 (CuAO1) of Arabidopsis thaliana contributes to
RT abscisic acid- and polyamine-induced nitric oxide biosynthesis and abscisic
RT acid signal transduction.";
RL Mol. Plant 4:663-678(2011).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION BY SALICYLIC ACID; JASMONATE;
RP FLAGELLIN AND ABCISIC ACID, GENE FAMILY, AND 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; WOUNDING; DEHYDRATION RECOVERY; 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). Required for abscisic acid- (ABA) and
CC polyamine- (PA) and H(2)O(2)-dependent induced nitric oxide (NO)
CC biosynthesis (PubMed:21471330). Involved in ABA signal transduction and
CC in responses to osmotic stress (PubMed:21471330).
CC {ECO:0000269|PubMed:21471330, 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 -!- 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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q43077};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:Q43077};
CC -!- PATHWAY: Amine and polyamine degradation; putrescine degradation.
CC {ECO:0000269|PubMed:23915037}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P46883}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:23915037}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, stems and flowers, and,
CC at lower levels, in leaves and cotyledons.
CC {ECO:0000269|PubMed:21471330, ECO:0000269|PubMed:23915037,
CC ECO:0000269|PubMed:31862580}.
CC -!- DEVELOPMENTAL STAGE: Accumulates during aging (PubMed:23915037,
CC PubMed:21471330). In young seedlings, expressed in hydathodes of new
CC emerging leaves and cotyledons as well as in vascular tissues of new
CC emerging leaves and in cortical root cells at the division/elongation
CC transition zone (PubMed:31862580). Observed in shoot apex, in
CC hypocotyls and hypocotyl/root junction (PubMed:31862580).
CC {ECO:0000269|PubMed:21471330, ECO:0000269|PubMed:23915037,
CC ECO:0000269|PubMed:31862580}.
CC -!- INDUCTION: Induced transiently by auxin (IAA) (PubMed:31862580).
CC Strongly induced by salicylic acid (SA), and, to a lower extent, by
CC jasmonic acid (MeJA) and flagellin 22 (fgl22) (PubMed:23915037,
CC PubMed:31862580). Triggered by abcisic acid (ABA) (PubMed:23915037,
CC PubMed:21471330, PubMed:31862580). Induced during wounding, dehydration
CC recovery, and treatment with putrescine (Put) (PubMed:31862580).
CC {ECO:0000269|PubMed:21471330, 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 -!- DISRUPTION PHENOTYPE: Impaired in nitric oxide (NO) production in
CC response to polyamines (PA) and abscisic acid (ABA) associated with
CC reduced levels of hydrogen preroxide (H(2)O(2)) (PubMed:21471330).
CC Reduced sensibility to ABA leading to a lower induction of ABA-
CC responsive genes in response to ABA as well as abnormal growth
CC regulation (PubMed:21471330). Altered responses to osmotic stress
CC (PubMed:21471330). {ECO:0000269|PubMed:21471330}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF19542.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 3 genes: At1g62810, At1g62820 and At1g62830.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC007190; AAF19542.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34008.1; -; Genomic_DNA.
DR EMBL; AY149440; AAN12916.1; -; mRNA.
DR EMBL; BT004539; AAO42785.1; -; mRNA.
DR RefSeq; NP_176469.1; NM_104959.4.
DR AlphaFoldDB; Q8H1H9; -.
DR SMR; Q8H1H9; -.
DR BioGRID; 27801; 1.
DR STRING; 3702.AT1G62810.1; -.
DR PaxDb; Q8H1H9; -.
DR PRIDE; Q8H1H9; -.
DR ProteomicsDB; 244972; -.
DR EnsemblPlants; AT1G62810.1; AT1G62810.1; AT1G62810.
DR GeneID; 842580; -.
DR Gramene; AT1G62810.1; AT1G62810.1; AT1G62810.
DR KEGG; ath:AT1G62810; -.
DR Araport; AT1G62810; -.
DR TAIR; locus:2026267; AT1G62810.
DR eggNOG; KOG1186; Eukaryota.
DR HOGENOM; CLU_011500_5_4_1; -.
DR InParanoid; Q8H1H9; -.
DR OMA; RVIRVQC; -.
DR OrthoDB; 1320015at2759; -.
DR PhylomeDB; Q8H1H9; -.
DR BioCyc; ARA:AT1G62810-MON; -.
DR BRENDA; 1.4.3.21; 399.
DR UniPathway; UPA00188; -.
DR PRO; PR:Q8H1H9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8H1H9; baseline and differential.
DR Genevisible; Q8H1H9; AT.
DR GO; GO:0005615; C:extracellular space; 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:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0009308; P:amine metabolic process; IBA:GO_Central.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IMP:TAIR.
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:0002237; P:response to molecule of bacterial origin; 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 Abscisic acid signaling pathway; Apoplast; Copper; Disulfide bond;
KW Glycoprotein; Metal-binding; Oxidoreductase; Reference proteome; Secreted;
KW Signal; TPQ.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..712
FT /note="Amine oxidase [copper-containing] gamma 1"
FT /id="PRO_0000342892"
FT ACT_SITE 354
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT ACT_SITE 442
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 352..363
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 439..444
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 499
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 501
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 508
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 509
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 510
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 651
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 652
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 662
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT MOD_RES 442
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 188..210
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT DISULFID 373..399
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT CONFLICT 201
FT /note="E -> K (in Ref. 3; AAO42785)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 712 AA; 80138 MW; 451908CE887D1F64 CRC64;
MAEPSFARLF LLFFSFLLIF ATYSWVFGPD SGFLFGTRVR KTLGSNRQVH VDHSLEKPHH
PLDPLTVREI NRVRTILSNH DPGFGSGSAT IHSMALDEPE KSRVVQWKKG NKLLSRRAAV
VAYWGGQTHE ITVDLDSGRV VSDVINRTSG YPILTLNDVF AASQVPLKSL EFNRSIEARG
VKFSDLACIT PFAGWFGSEE EGRRVIRVQC FTLQGTTNYF MRPLEGLYVT VDLDKLEVIK
IIDKGPIPIP KASGTEYRFG VQNKPVHMDR INPISMEQPD GPSFRVEDGH LVKWANWVFH
VKADQRAGMI ISQATVRDSE TGEPRSVMYK GFPSELFVPY MDPEEGWYYK GYMDAGELGL
GPTAMPLVPL NDCPRNSYYI DGVFASPDGK PIVQPNMICL FERYAGDISW RHSEILFANA
DIRESRPKVT LVARMATSVG NYDYIFDWEF QTDGLIRVTV AASGMLMVKG TPYDNVDDLG
DREDDAGPLI SENVIGVVHD HFITFHLDMD IDGPMNNSLV KVHLEKQRVP TGKSPRKSYL
KVKKYIAKTE KDAQIKLSLY DPYEFHIVNP NRKSRVGNPA GYRIVPGGNA ASLLDHDDPP
QIRGAFTNNQ IWVTPYNRSE QYAGGVLIYQ SQGDDTLQVW SDRDRSIENK DIVLWYTLGF
HHVPCQEDYP VMPTVAASFE LKPANFFESN PILGSAPFFE KDLPVCRPFA SS
