NEET_ARATH
ID NEET_ARATH Reviewed; 108 AA.
AC Q9FLI7; Q8LCD5;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=CDGSH iron-sulfur domain-containing protein NEET;
DE Short=At-NEET;
GN Name=NEET; OrderedLocusNames=At5g51720; ORFNames=MIO24.14;
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].
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 X-RAY CRYSTALLOGRAPHY (1.14 ANGSTROMS) OF 30-108 IN COMPLEX WITH 2FE-2S
RP CLUSTER, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF HIS-89.
RX PubMed=22562611; DOI=10.1105/tpc.112.097634;
RA Nechushtai R., Conlan A.R., Harir Y., Song L., Yogev O.,
RA Eisenberg-Domovich Y., Livnah O., Michaeli D., Rosen R., Ma V., Luo Y.,
RA Zuris J.A., Paddock M.L., Cabantchik Z.I., Jennings P.A., Mittler R.;
RT "Characterization of Arabidopsis NEET reveals an ancient role for NEET
RT proteins in iron metabolism.";
RL Plant Cell 24:2139-2154(2012).
CC -!- FUNCTION: Plays an important role in plant development, senescence,
CC reactive oxygen homeostasis, and iron metabolism. Acts as an iron-
CC sulfur transfer protein. {ECO:0000269|PubMed:22562611}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Note=Binds 1 [2Fe-2S] cluster per subunit.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22562611}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:22562611}. Mitochondrion
CC {ECO:0000269|PubMed:22562611}.
CC -!- DISRUPTION PHENOTYPE: Late bolting, early senescence and increased
CC tolerance to abiotic stress. {ECO:0000269|PubMed:22562611}.
CC -!- SIMILARITY: Belongs to the CISD protein family. {ECO:0000305}.
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DR EMBL; AB010074; BAB11241.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96119.1; -; Genomic_DNA.
DR EMBL; AF372888; AAK49604.1; -; mRNA.
DR EMBL; AY057716; AAL15346.1; -; mRNA.
DR EMBL; AY086662; AAM63719.1; -; mRNA.
DR RefSeq; NP_568764.1; NM_124551.5.
DR PDB; 3S2Q; X-ray; 1.75 A; A/B=30-108.
DR PDB; 3S2R; X-ray; 1.14 A; A/B=30-108.
DR PDBsum; 3S2Q; -.
DR PDBsum; 3S2R; -.
DR AlphaFoldDB; Q9FLI7; -.
DR SMR; Q9FLI7; -.
DR STRING; 3702.AT5G51720.1; -.
DR PaxDb; Q9FLI7; -.
DR PRIDE; Q9FLI7; -.
DR ProteomicsDB; 250822; -.
DR DNASU; 835246; -.
DR EnsemblPlants; AT5G51720.1; AT5G51720.1; AT5G51720.
DR GeneID; 835246; -.
DR Gramene; AT5G51720.1; AT5G51720.1; AT5G51720.
DR KEGG; ath:AT5G51720; -.
DR Araport; AT5G51720; -.
DR TAIR; locus:2165336; AT5G51720.
DR eggNOG; KOG3461; Eukaryota.
DR HOGENOM; CLU_132293_0_0_1; -.
DR InParanoid; Q9FLI7; -.
DR OMA; VVSTHFK; -.
DR OrthoDB; 1393750at2759; -.
DR PhylomeDB; Q9FLI7; -.
DR PRO; PR:Q9FLI7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLI7; baseline and differential.
DR Genevisible; Q9FLI7; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IPI:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IMP:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:TAIR.
DR GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR Gene3D; 3.40.5.90; -; 1.
DR InterPro; IPR045131; CISD1/2.
DR InterPro; IPR018967; FeS-contain_CDGSH-typ.
DR InterPro; IPR042216; MitoNEET_CISD.
DR PANTHER; PTHR13680; PTHR13680; 1.
DR Pfam; PF09360; zf-CDGSH; 1.
DR SMART; SM00704; ZnF_CDGSH; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Chloroplast; Iron; Iron-sulfur; Metal-binding;
KW Mitochondrion; Plastid; Reference proteome.
FT CHAIN 1..108
FT /note="CDGSH iron-sulfur domain-containing protein NEET"
FT /id="PRO_0000424630"
FT BINDING 74
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 76
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 85
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 89
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT MUTAGEN 89
FT /note="H->C: Increases 2Fe-2S cluster stability 10 fold.
FT Loss of iron-sulfur transfer activity."
FT /evidence="ECO:0000269|PubMed:22562611"
FT CONFLICT 77
FT /note="W -> R (in Ref. 4; AAM63719)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="Q -> L (in Ref. 4; AAM63719)"
FT /evidence="ECO:0000305"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:3S2R"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:3S2R"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:3S2R"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:3S2R"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:3S2R"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:3S2R"
FT TURN 80..83
FT /evidence="ECO:0007829|PDB:3S2R"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:3S2R"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:3S2R"
SQ SEQUENCE 108 AA; 11626 MW; 1750CEEB1A4EC08D CRC64;
MAIIASTFGT GLSYAGELPF KPVTGGEVGR KQQRMVVVRA EGGGGINPEI RKNEDKVVDS
VVVTELSKNI TPYCRCWRSG TFPLCDGSHV KHNKANGDNV GPLLLKKQ
