PCO1_ARATH
ID PCO1_ARATH Reviewed; 293 AA.
AC Q9LXG9;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Plant cysteine oxidase 1 {ECO:0000303|PubMed:24599061};
DE Short=AtPCO1 {ECO:0000303|PubMed:29848548};
DE EC=1.13.11.20 {ECO:0000269|PubMed:24599061, ECO:0000269|PubMed:29848548};
DE AltName: Full=Hypoxia-responsive unknown protein 29 {ECO:0000303|PubMed:20097791};
GN Name=PCO1 {ECO:0000303|PubMed:24599061};
GN Synonyms=HUP29 {ECO:0000303|PubMed:20097791};
GN OrderedLocusNames=At5g15120 {ECO:0000312|Araport:AT5G15120};
GN ORFNames=F8M21.10 {ECO:0000312|EMBL:CAB89322.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INDUCTION BY HYPOXIA.
RX PubMed=20097791; DOI=10.1104/pp.109.151845;
RA Mustroph A., Lee S.C., Oosumi T., Zanetti M.E., Yang H., Ma K.,
RA Yaghoubi-Masihi A., Fukao T., Bailey-Serres J.;
RT "Cross-kingdom comparison of transcriptomic adjustments to low-oxygen
RT stress highlights conserved and plant-specific responses.";
RL Plant Physiol. 152:1484-1500(2010).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, GENE FAMILY, NOMENCLATURE,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=24599061; DOI=10.1038/ncomms4425;
RA Weits D.A., Giuntoli B., Kosmacz M., Parlanti S., Hubberten H.M.,
RA Riegler H., Hoefgen R., Perata P., van Dongen J.T., Licausi F.;
RT "Plant cysteine oxidases control the oxygen-dependent branch of the N-end-
RT rule pathway.";
RL Nat. Commun. 5:3425-3425(2014).
RN [7]
RP FUNCTION.
RX PubMed=28332493; DOI=10.1038/ncomms14690;
RA White M.D., Klecker M., Hopkinson R.J., Weits D.A., Mueller C., Naumann C.,
RA O'Neill R., Wickens J., Yang J., Brooks-Bartlett J.C., Garman E.F.,
RA Grossmann T.N., Dissmeyer N., Flashman E.;
RT "Plant cysteine oxidases are dioxygenases that directly enable arginyl
RT transferase-catalysed arginylation of N-end rule targets.";
RL Nat. Commun. 8:14690-14690(2017).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=29848548; DOI=10.1074/jbc.ra118.003496;
RA White M.D., Kamps J.J.A.G., East S., Taylor Kearney L.J., Flashman E.;
RT "The plant cysteine oxidases from Arabidopsis thaliana are kinetically
RT tailored to act as oxygen sensors.";
RL J. Biol. Chem. 293:11786-11795(2018).
CC -!- FUNCTION: Catalyzes the oxidation of N-terminal cysteine residues (N-
CC Cys), thus preparing the protein for N-end rule pathway-mediated
CC proteasomal degradation, upstream of the N-end rule enzymes ATE1, ATE2
CC and PRT6 (PubMed:24599061, PubMed:29848548). Controls the preparation
CC of the group VII ethylene response factor (ERF-VII) proteins for
CC degradation via the 26S proteasome N-end rule pathway (PubMed:24599061,
CC PubMed:29848548). Acts as an oxygen sensor that controls the stability
CC of ERF-VII proteins, which are stabilized in flooding-induced hypoxia,
CC and regulate transcriptional adaptation to these adverse conditions
CC (PubMed:28332493, PubMed:29848548). Not active on Cys located inside or
CC at the C-terminus of a peptide (PubMed:24599061). Acts redundantly with
CC PCO2 to repress the anaerobic response (PubMed:24599061).
CC {ECO:0000269|PubMed:24599061, ECO:0000269|PubMed:28332493,
CC ECO:0000269|PubMed:29848548}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteine + O2 = 3-sulfino-L-alanine + H(+);
CC Xref=Rhea:RHEA:20441, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:61085; EC=1.13.11.20;
CC Evidence={ECO:0000269|PubMed:24599061, ECO:0000269|PubMed:29848548};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20442;
CC Evidence={ECO:0000269|PubMed:24599061, ECO:0000269|PubMed:29848548};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q8LGJ5};
CC Note=Binds 1 Fe(2+) cation per subunit. {ECO:0000250|UniProtKB:Q8LGJ5};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.24 mM for CGGAIISDFIPPPR peptide {ECO:0000269|PubMed:29848548};
CC Vmax=7.14 umol/min/mg enzyme with CGGAIISDFIPPPR peptide as substrate
CC {ECO:0000269|PubMed:29848548};
CC Note=kcat is 4.18 sec(-1) with CGGAIISDFIPPPR peptide as substrate.
CC {ECO:0000269|PubMed:29848548};
CC pH dependence:
CC Optimum pH is 8.5 with CGGAIISDFIPPPR peptide as substrate.
CC {ECO:0000269|PubMed:29848548};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24599061}. Cytoplasm
CC {ECO:0000269|PubMed:24599061}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development, with the highest
CC expression in mature siliques and during seed germination.
CC {ECO:0000269|PubMed:24599061}.
CC -!- INDUCTION: Up-regulated by hypoxia (PubMed:20097791). Up-regulated by
CC the ERF-VII transcription factor RAP2-12 during hypoxia
CC (PubMed:24599061). {ECO:0000269|PubMed:20097791,
CC ECO:0000269|PubMed:24599061}.
CC -!- SIMILARITY: Belongs to the cysteine dioxygenase family. {ECO:0000305}.
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DR EMBL; AL353993; CAB89322.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92119.1; -; Genomic_DNA.
DR EMBL; BT008337; AAP37696.1; -; mRNA.
DR EMBL; AK228354; BAF00293.1; -; mRNA.
DR PIR; T49947; T49947.
DR RefSeq; NP_197016.1; NM_121516.4.
DR AlphaFoldDB; Q9LXG9; -.
DR SMR; Q9LXG9; -.
DR STRING; 3702.AT5G15120.1; -.
DR iPTMnet; Q9LXG9; -.
DR PaxDb; Q9LXG9; -.
DR PRIDE; Q9LXG9; -.
DR ProteomicsDB; 236361; -.
DR EnsemblPlants; AT5G15120.1; AT5G15120.1; AT5G15120.
DR GeneID; 831364; -.
DR Gramene; AT5G15120.1; AT5G15120.1; AT5G15120.
DR KEGG; ath:AT5G15120; -.
DR Araport; AT5G15120; -.
DR TAIR; locus:2150866; AT5G15120.
DR eggNOG; KOG4281; Eukaryota.
DR HOGENOM; CLU_061320_4_1_1; -.
DR InParanoid; Q9LXG9; -.
DR OMA; DWADNIL; -.
DR OrthoDB; 929927at2759; -.
DR PhylomeDB; Q9LXG9; -.
DR SABIO-RK; Q9LXG9; -.
DR PRO; PR:Q9LXG9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LXG9; baseline and differential.
DR Genevisible; Q9LXG9; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0017172; F:cysteine dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0009061; P:anaerobic respiration; IMP:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0070483; P:detection of hypoxia; IMP:TAIR.
DR GO; GO:0018171; P:peptidyl-cysteine oxidation; IDA:TAIR.
DR GO; GO:0001666; P:response to hypoxia; IMP:TAIR.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR012864; PCO/ADO.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR22966; PTHR22966; 1.
DR Pfam; PF07847; PCO_ADO; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Iron; Metal-binding; Nucleus; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..293
FT /note="Plant cysteine oxidase 1"
FT /id="PRO_0000432449"
FT REGION 250..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 148
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8LGJ5"
FT BINDING 150
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8LGJ5"
FT BINDING 211
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8LGJ5"
SQ SEQUENCE 293 AA; 33014 MW; EF8037CEABA5E9AC CRC64;
MGFEMKPEKE VLELISSKNQ CKSNPNSVKK KNKNKNKKMM MTWRRKKIDS PADGITAVRR
LFNTCKEVFS NGGPGVIPSE DKIQQLREIL DDMKPEDVGL TPTMPYFRPN SGVEARSSPP
ITYLHLHQCD QFSIGIFCLP PSGVIPLHNH PGMTVFSKLL FGTMHIKSYD WVVDAPMRDS
KTRLAKLKVD STFTAPCNAS ILYPEDGGNM HRFTAITACA VLDVLGPPYC NPEGRHCTYF
LEFPLDKLSS EDDDVLSSEE EKEGYAWLQE RDDNPEDHTN VVGALYRGPK VED
