CAOG2_ARATH
ID CAOG2_ARATH Reviewed; 687 AA.
AC Q9M2B9;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Amine oxidase [copper-containing] gamma 2 {ECO:0000303|PubMed:31862580};
DE Short=AtCuAOgamma2 {ECO:0000303|PubMed:31862580};
DE EC=1.4.3.21 {ECO:0000250|UniProtKB:Q8H1H9};
DE Flags: Precursor;
GN Name=CuAOgamma2 {ECO:0000303|PubMed:31862580};
GN OrderedLocusNames=At3g43670 {ECO:0000312|Araport:AT3G43670};
GN ORFNames=F23N14.50 {ECO:0000312|EMBL:CAB83068.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 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. {ECO:0000250|UniProtKB:Q8H1H9}.
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:0000250|UniProtKB:Q8H1H9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16154;
CC Evidence={ECO:0000250|UniProtKB:Q8H1H9};
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:0000250|UniProtKB:Q8H1H9}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P46883}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000250|UniProtKB:Q8H1H9}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and cotyledons.
CC {ECO:0000269|PubMed:31862580}.
CC -!- DEVELOPMENTAL STAGE: In young seedlings, expressed in hydathodes of new
CC emerging leaves and cotyledons as well as in columella cells
CC (PubMed:31862580). Also observed in hypocotyl/root junction, hypocotyls
CC and in root apex (PubMed:31862580). {ECO:0000269|PubMed:31862580}.
CC -!- INDUCTION: Induced transiently by auxin (IAA) (PubMed:31862580).
CC Induced during wounding, dehydration recovery, and treatment with
CC putrescine (Put) (PubMed:31862580). Slightly and transiently repressed
CC by jasmonic acid (MeJA), abscisic acid (ABA) and salicylic acid (SA),
CC and drought (PubMed:31862580). {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}.
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DR EMBL; AL138638; CAB83068.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77817.1; -; Genomic_DNA.
DR EMBL; AY095989; AAM19946.1; -; mRNA.
DR EMBL; BT005817; AAO64752.1; -; mRNA.
DR PIR; T47403; T47403.
DR RefSeq; NP_189953.1; NM_114235.4.
DR SMR; Q9M2B9; -.
DR STRING; 3702.AT3G43670.1; -.
DR PRIDE; Q9M2B9; -.
DR ProteomicsDB; 177325; -.
DR EnsemblPlants; AT3G43670.1; AT3G43670.1; AT3G43670.
DR GeneID; 823469; -.
DR Gramene; AT3G43670.1; AT3G43670.1; AT3G43670.
DR KEGG; ath:AT3G43670; -.
DR Araport; AT3G43670; -.
DR TAIR; locus:2080173; AT3G43670.
DR eggNOG; KOG1186; Eukaryota.
DR HOGENOM; CLU_011500_5_4_1; -.
DR OMA; SKQDTVN; -.
DR OrthoDB; 1320015at2759; -.
DR BioCyc; ARA:AT3G43670-MON; -.
DR UniPathway; UPA00188; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M2B9; baseline and differential.
DR GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:UniProtKB-EC.
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 2: Evidence at transcript level;
KW Apoplast; Copper; Disulfide bond; Glycoprotein; Manganese; Metal-binding;
KW Oxidoreductase; Reference proteome; Secreted; Signal; TPQ.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..687
FT /note="Amine oxidase [copper-containing] gamma 2"
FT /id="PRO_5015099887"
FT ACT_SITE 335
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT ACT_SITE 423
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 333..344
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 420..425
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 480
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 482
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 489
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 490
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 491
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 632
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 633
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 643
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT MOD_RES 423
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 598
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 169..191
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT DISULFID 354..380
FT /evidence="ECO:0000250|UniProtKB:P12807"
SQ SEQUENCE 687 AA; 77533 MW; 15AFC49DB0823146 CRC64;
MVELSFSQLL VLLLSLLFLF TTLASSSKTP RFKYSLEKPH HPLDPLTTPE IKRVQTILSG
HDPGFGSGST IIHAMALDEP DKQRVIRWKK GDRLPPRRAE ILAMSNGESH VLTVDLKSGR
VVSDLVNPTF GYPILTMKDI IAVSQVPYKS VEFNRSIEAR GIPFSGLICI TPFAGWYGPD
EEGRRVIKIQ CFSKQDTVNF YMRPIEGLYL TVDMDKLEII KIVDNGPVPV PKSTGTEYRY
GFLNETVYMD RVNPMSMEQP DGPSFQVEDG YLVKWANWKF HIKPDQRAGM IISQATVRDS
KTGEARSVMY KGFASELFVP NMDPGEGWYS KAYMDAGEFG LGPSSMPLVP LNDCPRNAYY
IDGFFASPEG IPILQPNMIC LFERYAGDTS WRHSEILLPG VDIRESRAKV TLVARMACSV
GNYDYIFDWE FQMDGVIRVT VAASGMLMVK GTAYENVEDL GEKEDDSGPL ISENVIGVVH
DHFISFHLDM DIDGSANNSF VKVHLEKQRL PPGESRRKSY LKVKKYVAKT EKDAQIKMSL
YDPYEFHLVN PNRLSRLGNP AGYKLVPGGN AASLLDHDDP PQMRGAFTNN QIWVTRYNRS
EQWAGGLLMY QSRGEDTLQV WSDRDRSIEN KDIVLWYTLG FHHVPCQEDF PVMPTIASSF
ELKPVNFFES NPVLGISPFF EKDLPVC
