DIN11_ARATH
ID DIN11_ARATH Reviewed; 357 AA.
AC Q8H113; Q8RXJ6; Q9FVM1; Q9SCJ7;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Probable 2-oxoglutarate-dependent dioxygenase DIN11;
DE EC=1.14.11.-;
DE AltName: Full=Protein DARK-INDUCIBLE 11;
GN Name=DIN11; OrderedLocusNames=At3g49620; ORFNames=T9C5.210;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 [MRNA] OF 1-148, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11240919; DOI=10.1034/j.1399-3054.2001.1110312.x;
RA Fujiki Y., Yoshikawa Y., Sato T., Inada N., Ito M., Nishida I.,
RA Watanabe A.;
RT "Dark-inducible genes from Arabidopsis thaliana are associated with leaf
RT senescence and repressed by sugars.";
RL Physiol. Plantarum 111:345-352(2001).
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 -!- TISSUE SPECIFICITY: Expressed in senescent leaves.
CC {ECO:0000269|PubMed:11240919}.
CC -!- INDUCTION: By dark. {ECO:0000269|PubMed:11240919}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB62466.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL132964; CAB62466.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE78567.1; -; Genomic_DNA.
DR EMBL; AY080850; AAL87324.1; -; mRNA.
DR EMBL; BT000898; AAN41298.1; -; mRNA.
DR EMBL; AF159379; AAG23722.1; -; mRNA.
DR PIR; T46239; T46239.
DR RefSeq; NP_190531.2; NM_114822.5.
DR AlphaFoldDB; Q8H113; -.
DR SMR; Q8H113; -.
DR STRING; 3702.AT3G49620.1; -.
DR PaxDb; Q8H113; -.
DR PRIDE; Q8H113; -.
DR ProteomicsDB; 241226; -.
DR EnsemblPlants; AT3G49620.1; AT3G49620.1; AT3G49620.
DR GeneID; 824124; -.
DR Gramene; AT3G49620.1; AT3G49620.1; AT3G49620.
DR KEGG; ath:AT3G49620; -.
DR Araport; AT3G49620; -.
DR TAIR; locus:2114683; AT3G49620.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_6_0_1; -.
DR InParanoid; Q8H113; -.
DR OMA; YRISVPF; -.
DR OrthoDB; 1005149at2759; -.
DR PhylomeDB; Q8H113; -.
DR BioCyc; ARA:AT3G49620-MON; -.
DR PRO; PR:Q8H113; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8H113; baseline and differential.
DR Genevisible; Q8H113; AT.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 2: Evidence at transcript level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..357
FT /note="Probable 2-oxoglutarate-dependent dioxygenase DIN11"
FT /id="PRO_0000428721"
FT DOMAIN 208..308
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 231
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 233
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 289
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 299
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 357 AA; 40697 MW; C81712BBD4AA07BE CRC64;
MVIYHRKVVF TYVRAKRFYH FLNIEMVTDF KSLLPVIDIS PLLAKCDDFD MAEDAGVVEV
VGKLDRACRD VGFFYVIGHG ISDDLINKVK EMTHQFFELP YEEKLKIKIT PTAGYRGYQR
IGVNFTSGKQ DMHEAIDCYR EFKQGKHGDI GKVLEGPNQW PGNPQEYKDL MEKYIKLCTD
LSRNILRGIS LALGGSPYEF EGKMLRDPFW VMRIIGYPGV NQENVIGCGA HTDYGLLTLI
NQDDDKTALQ VKNVDGDWIP AIPIPGSFIC NIGDMLTILS NGVYQSTLHK VINNSPKYRV
CVAFFYETNF EAEVEPLDIF KEKHPRKETS QVAKRVVYGQ HLINKVLTTF ANLVENS
