PCO2_ARATH
ID PCO2_ARATH Reviewed; 276 AA.
AC Q8LGJ5; Q9FLE5;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Plant cysteine oxidase 2 {ECO:0000303|PubMed:24599061};
DE Short=AtPCO2 {ECO:0000303|PubMed:33207269};
DE EC=1.13.11.20 {ECO:0000269|PubMed:24599061, ECO:0000269|PubMed:29848548, ECO:0000269|PubMed:33207269};
DE AltName: Full=Hypoxia-responsive unknown protein 43 {ECO:0000303|PubMed:20097791};
GN Name=PCO2 {ECO:0000303|PubMed:24599061};
GN Synonyms=HUP43 {ECO:0000303|PubMed:20097791};
GN OrderedLocusNames=At5g39890 {ECO:0000312|Araport:AT5G39890};
GN ORFNames=MYH19.8 {ECO:0000312|EMBL:BAB10214.1};
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [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).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 48-276 IN COMPLEX WITH IRON IONS,
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=33207269; DOI=10.1016/j.jsb.2020.107663;
RA Chen Z., Guo Q., Wu G., Wen J., Liao S., Xu C.;
RT "Molecular basis for cysteine oxidation by plant cysteine oxidases from
RT Arabidopsis thaliana.";
RL J. Struct. Biol. 213:107663-107663(2020).
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, PubMed:33207269). Controls
CC the preparation of the group VII ethylene response factor (ERF-VII)
CC proteins for degradation via the 26S proteasome N-end rule pathway
CC (PubMed:24599061, PubMed:29848548, PubMed:33207269). Acts as an oxygen
CC sensor that controls the stability of ERF-VII proteins, which are
CC stabilized in flooding-induced hypoxia, and regulate transcriptional
CC adaptation to these adverse conditions (Probable) (PubMed:29848548).
CC Not active on Cys located inside or at the C-terminus of a peptide
CC (PubMed:24599061). Acts redundantly with PCO1 to repress the anaerobic
CC response (PubMed:24599061). {ECO:0000269|PubMed:24599061,
CC ECO:0000269|PubMed:29848548, ECO:0000269|PubMed:33207269,
CC ECO:0000305|PubMed:24599061}.
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 ECO:0000269|PubMed:33207269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20442;
CC Evidence={ECO:0000269|PubMed:24599061, ECO:0000269|PubMed:29848548,
CC ECO:0000269|PubMed:33207269};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:33207269};
CC Note=Binds 1 Fe(2+) cation per subunit. {ECO:0000269|PubMed:33207269};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.09 mM for CGGAIISDFIPPPR peptide {ECO:0000269|PubMed:29848548};
CC Vmax=3.45 umol/min/mg enzyme with CGGAIISDFIPPPR peptide as substrate
CC {ECO:0000269|PubMed:29848548};
CC Note=kcat is 1.98 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 {ECO:0000269|PubMed:20097791, ECO:0000269|PubMed:24599061}.
CC -!- SIMILARITY: Belongs to the cysteine dioxygenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10214.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB010077; BAB10214.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED94488.1; -; Genomic_DNA.
DR EMBL; BT003127; AAO24559.1; -; mRNA.
DR EMBL; AK228134; BAF00091.1; -; mRNA.
DR EMBL; AY084237; AAM60834.1; -; mRNA.
DR RefSeq; NP_198805.1; NM_123352.3.
DR PDB; 7CXZ; X-ray; 1.56 A; A=48-276.
DR PDBsum; 7CXZ; -.
DR AlphaFoldDB; Q8LGJ5; -.
DR SMR; Q8LGJ5; -.
DR STRING; 3702.AT5G39890.1; -.
DR PaxDb; Q8LGJ5; -.
DR PRIDE; Q8LGJ5; -.
DR ProteomicsDB; 236362; -.
DR EnsemblPlants; AT5G39890.1; AT5G39890.1; AT5G39890.
DR GeneID; 833986; -.
DR Gramene; AT5G39890.1; AT5G39890.1; AT5G39890.
DR KEGG; ath:AT5G39890; -.
DR Araport; AT5G39890; -.
DR TAIR; locus:2178032; AT5G39890.
DR eggNOG; KOG4281; Eukaryota.
DR HOGENOM; CLU_061320_4_1_1; -.
DR InParanoid; Q8LGJ5; -.
DR OrthoDB; 929927at2759; -.
DR PhylomeDB; Q8LGJ5; -.
DR SABIO-RK; Q8LGJ5; -.
DR PRO; PR:Q8LGJ5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LGJ5; baseline and differential.
DR Genevisible; Q8LGJ5; 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; IDA:UniProtKB.
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 3D-structure; Cytoplasm; Iron; Metal-binding; Nucleus; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..276
FT /note="Plant cysteine oxidase 2"
FT /id="PRO_0000432450"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 134
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:33207269,
FT ECO:0007744|PDB:7CXZ"
FT BINDING 136
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:33207269,
FT ECO:0007744|PDB:7CXZ"
FT BINDING 197
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:33207269,
FT ECO:0007744|PDB:7CXZ"
FT HELIX 48..57
FT /evidence="ECO:0007829|PDB:7CXZ"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:7CXZ"
FT HELIX 69..80
FT /evidence="ECO:0007829|PDB:7CXZ"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:7CXZ"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:7CXZ"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:7CXZ"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:7CXZ"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:7CXZ"
FT STRAND 140..157
FT /evidence="ECO:0007829|PDB:7CXZ"
FT STRAND 168..182
FT /evidence="ECO:0007829|PDB:7CXZ"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:7CXZ"
FT STRAND 195..203
FT /evidence="ECO:0007829|PDB:7CXZ"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:7CXZ"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:7CXZ"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:7CXZ"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:7CXZ"
FT HELIX 243..248
FT /evidence="ECO:0007829|PDB:7CXZ"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:7CXZ"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:7CXZ"
SQ SEQUENCE 276 AA; 30820 MW; 7EDDEE9322BA3E73 CRC64;
MGTDTVMSGR VRKDLSKTNP NGNIPENRSN SRKKIQRRSK KTLICPVQKL FDTCKKVFAD
GKSGTVPSQE NIEMLRAVLD EIKPEDVGVN PKMSYFRSTV TGRSPLVTYL HIYACHRFSI
CIFCLPPSGV IPLHNHPEMT VFSKLLFGTM HIKSYDWVPD SPQPSSDTRL AKVKVDSDFT
APCDTSILYP ADGGNMHCFT AKTACAVLDV IGPPYSDPAG RHCTYYFDYP FSSFSVDGVV
VAEEEKEGYA WLKEREEKPE DLTVTALMYS GPTIKE
