ICU11_ARATH
ID ICU11_ARATH Reviewed; 397 AA.
AC Q3ED68; O23127;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=2-oxoglutarate and iron-dependent oxygenase domain-containing protein ICU11 {ECO:0000305};
DE EC=1.14.11.-;
DE AltName: Full=Protein INCURVATA 11 {ECO:0000303|PubMed:29915151};
GN Name=ICU11 {ECO:0000303|PubMed:29915151};
GN OrderedLocusNames=At1g22950 {ECO:0000312|Araport:AT1G22950};
GN ORFNames=F19G10.24 {ECO:0000312|EMBL:AAB72163.1};
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=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 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 CP2 (PubMed:29915151). Functions in the repression
CC of several members of the MADS-box transcription factors family,
CC including SEP3, during vegetative development via histone modification
CC (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 -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:29915151}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons, rosette leaves,
CC cauline leaves and inflorescences. {ECO:0000269|PubMed:29915151}.
CC -!- DISRUPTION PHENOTYPE: Altered plant morphology, including epinastic
CC (curved downward) cotyledons, hyponastic (curved up) leaves, and
CC reduced palisade mesophyll cell size (PubMed:29915151). Reduced number
CC of leaves at bolting and early flowering (PubMed:29915151). The double
CC mutant seedlings icu11 and cp2 skip the vegetative phase, flower
CC immediatly after germination and then die (PubMed:29915151).
CC {ECO:0000269|PubMed:29915151}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB72163.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At1g22950 and At1g22960.; Evidence={ECO:0000305};
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DR EMBL; AF000657; AAB72163.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30314.1; -; Genomic_DNA.
DR PIR; F86363; F86363.
DR RefSeq; NP_173708.3; NM_102142.5.
DR AlphaFoldDB; Q3ED68; -.
DR SMR; Q3ED68; -.
DR STRING; 3702.AT1G22950.1; -.
DR PaxDb; Q3ED68; -.
DR PRIDE; Q3ED68; -.
DR ProteomicsDB; 242386; -.
DR EnsemblPlants; AT1G22950.1; AT1G22950.1; AT1G22950.
DR GeneID; 838902; -.
DR Gramene; AT1G22950.1; AT1G22950.1; AT1G22950.
DR KEGG; ath:AT1G22950; -.
DR Araport; AT1G22950; -.
DR TAIR; locus:2017774; AT1G22950.
DR eggNOG; KOG1971; Eukaryota.
DR HOGENOM; CLU_045835_0_0_1; -.
DR InParanoid; Q3ED68; -.
DR OMA; IPNEEHE; -.
DR OrthoDB; 756511at2759; -.
DR PhylomeDB; Q3ED68; -.
DR PRO; PR:Q3ED68; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q3ED68; 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 GO; GO:0016571; P:histone methylation; IMP:TAIR.
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 2: Evidence at transcript level;
KW Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase;
KW Reference proteome; Vitamin C.
FT CHAIN 1..397
FT /note="2-oxoglutarate and iron-dependent oxygenase domain-
FT containing protein ICU11"
FT /id="PRO_0000342737"
FT DOMAIN 238..339
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 260
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 262
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 320
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 330
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 397 AA; 45751 MW; 670EAAFF9C023848 CRC64;
MCNQTPLRSM ALDSSGKQPE QQQQQQPRAS SGNGEARLKL RRTPNEEHEP ENYEDLPLDY
SPSLFTSLER YLPEQLLNST RIDKASFMRD LLLRYSPDTE RVRVLRHKEY RDKIMSSYQR
LHGEIYTLDP SSFFAPSFLG AFSRKSEPNF RSSMVESYPG IFTFEMFKPQ FCEMLLAEVE
HMEKWVYDSR STIMRPNTMN NFGVVLDDFG FDSMLQKLVD DFISPIAQVL FPEVCGTSLD
SHHGYIVEYG KDRDVDLGFH VDDSEVSLNV CLGKQFSGGE LYFRGVRCDK HVNSDSTEKE
VYDYSHVPGH AILHRGRHRH GARATTSGHR ANLILWCRSS TFREMKNYQR DFSGWCGGCK
LDKQRRQRDS INATKEILAR KAAEKTLVEL ASKSCAE
