CP2_ARATH
ID CP2_ARATH Reviewed; 394 AA.
AC P0DO23; Q9LV19;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-APR-2020, sequence version 1.
DT 03-AUG-2022, entry version 10.
DE RecName: Full=2-oxoglutarate and iron-dependent oxygenase domain-containing protein CP2 {ECO:0000305};
DE EC=1.14.11.- {ECO:0000255|PROSITE-ProRule:PRU00805};
DE AltName: Full=Protein CUPULIFORMIS 2 {ECO:0000303|PubMed:29915151};
GN Name=CP2 {ECO:0000303|PubMed:29915151};
GN OrderedLocusNames=At3g18210 {ECO:0000312|Araport:AT3G18210};
GN ORFNames=MRC8.20 {ECO:0000312|EMBL:BAB02034.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=29915151; DOI=10.1105/tpc.18.00300;
RA Mateo-Bonmati E., Esteve-Bruna D., Juan-Vicente L., Nadi R., Candela H.,
RA Lozano F.M., Ponce M.R., Perez-Perez J.M., Micol J.L.;
RT "INCURVATA11 and CUPULIFORMIS2 are redundant genes that encode epigenetic
RT machinery components in Arabidopsis.";
RL Plant Cell 30:1596-1616(2018).
CC -!- FUNCTION: Participates in the epigenetic repression of flowering genes
CC in association with ICU11 (PubMed:29915151). Functions in the
CC repression of several members of the MADS-box transcription factors
CC family, including SEP3, during vegetative development via histone
CC modification (PubMed:29915151). {ECO:0000269|PubMed:29915151}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000250|UniProtKB:Q02809};
CC -!- INTERACTION:
CC P0DO23; Q8H1P9: MYB3R3; NbExp=3; IntAct=EBI-4428219, EBI-4448936;
CC P0DO23; O23160: MYB73; NbExp=3; IntAct=EBI-4428219, EBI-25506855;
CC P0DO23; Q39234: TGA3; NbExp=3; IntAct=EBI-4428219, EBI-541366;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:29915151}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons, rosette leaves,
CC cauline leaves, inflorescences and siliques.
CC {ECO:0000269|PubMed:29915151}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:29915151). The double mutant seedlings icu11 and cp2
CC skip the vegetative phase, flower immediatly after germination and then
CC die (PubMed:29915151). {ECO:0000269|PubMed:29915151}.
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DR EMBL; AB020749; BAB02034.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76064.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76065.1; -; Genomic_DNA.
DR EMBL; AF386971; AAK62416.1; -; mRNA.
DR EMBL; BT008485; AAP37844.1; -; mRNA.
DR RefSeq; NP_001078177.1; NM_001084708.1.
DR RefSeq; NP_566600.1; NM_112704.3.
DR AlphaFoldDB; P0DO23; -.
DR SMR; P0DO23; -.
DR IntAct; P0DO23; 5.
DR STRING; 3702.AT3G18210.1; -.
DR ProteomicsDB; 189930; -.
DR EnsemblPlants; AT3G18210.1; AT3G18210.1; AT3G18210.
DR EnsemblPlants; AT3G18210.2; AT3G18210.2; AT3G18210.
DR GeneID; 821348; -.
DR Gramene; AT3G18210.1; AT3G18210.1; AT3G18210.
DR Gramene; AT3G18210.2; AT3G18210.2; AT3G18210.
DR KEGG; ath:AT3G18210; -.
DR Araport; AT3G18210; -.
DR TAIR; locus:2092727; AT3G18210.
DR eggNOG; KOG1971; Eukaryota.
DR HOGENOM; CLU_045835_0_0_1; -.
DR OMA; KHRDYRQ; -.
DR OrthoDB; 756511at2759; -.
DR PRO; PR:P0DO23; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P0DO23; baseline and differential.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase;
KW Reference proteome; Vitamin C.
FT CHAIN 1..394
FT /note="2-oxoglutarate and iron-dependent oxygenase domain-
FT containing protein CP2"
FT /id="PRO_0000449522"
FT DOMAIN 248..347
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 268
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 270
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 328
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 338
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 394 AA; 45179 MW; 65DE0E3FD6ACD16A CRC64;
MSSEQREGSQ ETTTTTVEGN GTIAGQNSHS AAPTTLRATS TMVSCQRLRL NPNNEHRPDS
YEDLQLDFPN SVYSSLEKYL PPNMLVSNRD EKIKFMTDIM LRHLPHGERS RAQRHSDYRL
KITTNYQPLH KELYTLVPTV CFVPAFLKAI NENTEESFRN IISEPSPGVF VFDMLQPSFC
EMMLAEIDNF ERWVGETKFR IMRPNTMNKY GAVLDDFGLD TMLDKLMEGF IRPISKVFFS
DVGGATLDSH HGFVVEYGKD RDVDLGFHVD DSEVTLNVCL GNQFVGGELF FRGTRCEKHV
NTATKADETY DYCHIPGQAV LHRGRHRHGA RATTCGHRVN MLLWCRSSVF RELKTHHKDF
SSWCGECFCE KRDEKVRSID ALRKKLFKPR QTQA
