PCO3_ARATH
ID PCO3_ARATH Reviewed; 282 AA.
AC Q1G3U6; Q8L8X2; Q940G4;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Plant cysteine oxidase 3 {ECO:0000303|PubMed:24599061};
DE Short=AtPCO3 {ECO:0000303|PubMed:29848548};
DE EC=1.13.11.20 {ECO:0000269|PubMed:29848548, ECO:0000305|PubMed:24599061};
DE AltName: Full=NIFS-like protein 2 {ECO:0000303|PubMed:18978034};
DE Short=NifS2;
GN Name=PCO3 {ECO:0000303|PubMed:24599061};
GN Synonyms=CpNIFS2 {ECO:0000303|PubMed:18978034};
GN OrderedLocusNames=At1g18490 {ECO:0000312|Araport:AT1G18490};
GN ORFNames=F15H18.26 {ECO:0000312|EMBL:AC013354};
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-282 (ISOFORM 2).
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 [6]
RP IDENTIFICATION.
RX PubMed=18978034; DOI=10.1105/tpc.107.056341;
RA Schippers J.H., Nunes-Nesi A., Apetrei R., Hille J., Fernie A.R.,
RA Dijkwel P.P.;
RT "The Arabidopsis onset of leaf death5 mutation of quinolinate synthase
RT affects nicotinamide adenine dinucleotide biosynthesis and causes early
RT ageing.";
RL Plant Cell 20:2909-2925(2008).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, GENE FAMILY, NOMENCLATURE, AND SUBCELLULAR
RP LOCATION.
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).
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 (Probable) (PubMed:29848548). Controls the preparation of the
CC group VII ethylene response factor (ERF-VII) proteins for degradation
CC via the 26S proteasome N-end rule pathway (Probable) (PubMed:29848548).
CC Acts as an oxygen sensor that controls the stability of ERF-VII
CC proteins, which are stabilized in flooding-induced hypoxia, and
CC regulate transcriptional adaptation to these adverse conditions
CC (Probable) (PubMed:29848548). {ECO:0000269|PubMed:29848548,
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:29848548, ECO:0000305|PubMed:24599061};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20442;
CC Evidence={ECO:0000269|PubMed:29848548, ECO:0000305|PubMed:24599061};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q9SJI9};
CC Note=Binds 1 Fe(2+) cation per subunit. {ECO:0000250|UniProtKB:Q9SJI9};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.56 mM for CGGAIISDFIPPPR peptide {ECO:0000269|PubMed:29848548};
CC Vmax=8.43 umol/min/mg enzyme with CGGAIISDFIPPPR peptide as substrate
CC {ECO:0000269|PubMed:29848548};
CC Note=kcat is 4.7 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:0000305|PubMed:24599061}. Cytoplasm
CC {ECO:0000305|PubMed:24599061}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q1G3U6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q1G3U6-2; Sequence=VSP_057518;
CC -!- SIMILARITY: Belongs to the cysteine dioxygenase family. {ECO:0000305}.
CC -!- CAUTION: Was originally identified as a putative plastidic SufS-like
CC protein and thus called CpNifS2. {ECO:0000303|PubMed:18978034}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK96846.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM67070.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC013354; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE29722.1; -; Genomic_DNA.
DR EMBL; DQ487488; ABF59200.1; -; mRNA.
DR EMBL; AY088754; AAM67070.1; ALT_INIT; mRNA.
DR EMBL; AY054655; AAK96846.1; ALT_INIT; mRNA.
DR EMBL; AY072501; AAL66916.1; -; mRNA.
DR RefSeq; NP_564055.1; NM_101707.4. [Q1G3U6-1]
DR AlphaFoldDB; Q1G3U6; -.
DR SMR; Q1G3U6; -.
DR IntAct; Q1G3U6; 1.
DR STRING; 3702.AT1G18490.1; -.
DR PaxDb; Q1G3U6; -.
DR PRIDE; Q1G3U6; -.
DR ProteomicsDB; 236444; -. [Q1G3U6-1]
DR EnsemblPlants; AT1G18490.1; AT1G18490.1; AT1G18490. [Q1G3U6-1]
DR GeneID; 838430; -.
DR Gramene; AT1G18490.1; AT1G18490.1; AT1G18490. [Q1G3U6-1]
DR KEGG; ath:AT1G18490; -.
DR Araport; AT1G18490; -.
DR TAIR; locus:2014169; AT1G18490.
DR eggNOG; KOG4281; Eukaryota.
DR HOGENOM; CLU_061320_3_2_1; -.
DR InParanoid; Q1G3U6; -.
DR OMA; KCTYYRD; -.
DR PhylomeDB; Q1G3U6; -.
DR SABIO-RK; Q1G3U6; -.
DR PRO; PR:Q1G3U6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q1G3U6; baseline and differential.
DR Genevisible; Q1G3U6; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0017172; F:cysteine dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
DR GO; GO:0070483; P:detection of hypoxia; IDA:UniProtKB.
DR GO; GO:0018171; P:peptidyl-cysteine oxidation; IDA:UniProtKB.
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 Alternative splicing; Cytoplasm; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..282
FT /note="Plant cysteine oxidase 3"
FT /id="PRO_0000432451"
FT BINDING 131
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9SJI9"
FT BINDING 133
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9SJI9"
FT BINDING 202
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9SJI9"
FT VAR_SEQ 173
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_057518"
FT CONFLICT 198
FT /note="G -> V (in Ref. 4; AAM67070)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 282 AA; 31291 MW; 342F69567E6136F6 CRC64;
MLSRLFKAGE KVLSNLVSKK DIYMASRNQE KSPKVQELYD LCKETFTGKA PSPASMAIQK
LCSVLDSVSP ADVGLEEVSQ DDDRGYGVSG VSRFNRVGRW AQPITFLDIH ECDTFTMCIF
CFPTSSVIPL HDHPEMAVFS KILYGSLHVK AYDWVEPPCI ITQDKGVPGS LPARLAKLVS
DKVITPQSEI PALYPKTGGN LHCFTALTPC AVLDILSPPY KESVGRSCSY YMDYPFSTFA
LENGMKKVDE GKEDEYAWLV QIDTPDDLHM RPGSYTGPTI RV
