SODF2_ARATH
ID SODF2_ARATH Reviewed; 305 AA.
AC Q9LU64; O04879;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Superoxide dismutase [Fe] 2, chloroplastic;
DE EC=1.15.1.1 {ECO:0000269|PubMed:18996978};
DE AltName: Full=Protein ALBINO OR PALE GREEN 8;
DE AltName: Full=Protein FE SUPEROXIDE DISMUTASE 2;
DE Flags: Precursor;
GN Name=FSD2; Synonyms=APG8; OrderedLocusNames=At5g51100; ORFNames=MWD22.4;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 152-305.
RC STRAIN=cv. Columbia;
RA Van Breusegem F., Villaroel R., Van Montagu M., Inze D.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INDUCTION BY UV-B, AND GENE FAMILY.
RX PubMed=9765550; DOI=10.1104/pp.118.2.637;
RA Kliebenstein D.J., Monde R.A., Last R.L.;
RT "Superoxide dismutase in Arabidopsis: an eclectic enzyme family with
RT disparate regulation and protein localization.";
RL Plant Physiol. 118:637-650(1998).
RN [8]
RP INDUCTION BY SALT.
RX PubMed=18275461; DOI=10.1111/j.1399-3054.2007.01009.x;
RA Attia H., Arnaud N., Karray N., Lachaal M.;
RT "Long-term effects of mild salt stress on growth, ion accumulation and
RT superoxide dismutase expression of Arabidopsis rosette leaves.";
RL Physiol. Plantarum 132:293-305(2008).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=18996978; DOI=10.1105/tpc.108.061341;
RA Myouga F., Hosoda C., Umezawa T., Iizumi H., Kuromori T., Motohashi R.,
RA Shono Y., Nagata N., Ikeuchi M., Shinozaki K.;
RT "A heterocomplex of iron superoxide dismutases defends chloroplast
RT nucleoids against oxidative stress and is essential for chloroplast
RT development in Arabidopsis.";
RL Plant Cell 20:3148-3162(2008).
RN [10]
RP ACTIVITY REGULATION.
RX PubMed=23057508; DOI=10.1111/j.1469-8137.2012.04369.x;
RA Kuo W.Y., Huang C.H., Liu A.C., Cheng C.P., Li S.H., Chang W.C., Weiss C.,
RA Azem A., Jinn T.L.;
RT "CHAPERONIN 20 mediates iron superoxide dismutase (FeSOD) activity
RT independent of its co-chaperonin role in Arabidopsis chloroplasts.";
RL New Phytol. 197:99-110(2013).
RN [11]
RP INTERACTION WITH MRL7 AND PRDA1.
RX PubMed=24132784; DOI=10.1093/pcp/pct148;
RA Qiao J., Li J., Chu W., Luo M.;
RT "PRDA1, a novel chloroplast nucleoid protein, is required for early
RT chloroplast development and is involved in the regulation of plastid gene
RT expression in Arabidopsis.";
RL Plant Cell Physiol. 54:2071-2084(2013).
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems (By
CC similarity). Plays important role in chloroplast development,
CC particularly in the maintenance of thylakoids membranes. Seems to act
CC as a heterodimer with FSD3. {ECO:0000250, ECO:0000269|PubMed:18996978}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:18421; EC=1.15.1.1;
CC Evidence={ECO:0000269|PubMed:18996978};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by cpn20/cpn21 (in vitro).
CC {ECO:0000269|PubMed:23057508}.
CC -!- SUBUNIT: Heterodimer with FSD3 (PubMed:18996978). Interacts with MRL7
CC and PRDA1 (PubMed:24132784). {ECO:0000269|PubMed:18996978,
CC ECO:0000269|PubMed:24132784}.
CC -!- INTERACTION:
CC Q9LU64; Q9FMX0: FSD3; NbExp=7; IntAct=EBI-4424866, EBI-4430441;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid
CC {ECO:0000269|PubMed:18996978}.
CC -!- INDUCTION: By UV-B treatment. Induced by salt stress.
CC {ECO:0000269|PubMed:18275461, ECO:0000269|PubMed:9765550}.
CC -!- DISRUPTION PHENOTYPE: Pale green phenotype. Abnormal plastids, highly
CC vacuolated and without internal membrane structures like thylakoids.
CC {ECO:0000269|PubMed:18996978}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; AB023044; BAA97372.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96034.1; -; Genomic_DNA.
DR EMBL; BT004073; AAO42100.1; -; mRNA.
DR EMBL; BT005116; AAO50649.1; -; mRNA.
DR EMBL; AK228538; BAF00460.1; -; mRNA.
DR EMBL; AY085077; AAM61633.1; -; mRNA.
DR EMBL; Y12641; CAA73188.1; -; mRNA.
DR RefSeq; NP_199923.1; NM_124489.3.
DR PDB; 7BJK; X-ray; 2.25 A; A/B/C/D/E=47-305.
DR PDBsum; 7BJK; -.
DR AlphaFoldDB; Q9LU64; -.
DR SMR; Q9LU64; -.
DR BioGRID; 20428; 10.
DR IntAct; Q9LU64; 8.
DR STRING; 3702.AT5G51100.1; -.
DR iPTMnet; Q9LU64; -.
DR PaxDb; Q9LU64; -.
DR PRIDE; Q9LU64; -.
DR ProteomicsDB; 234478; -.
DR EnsemblPlants; AT5G51100.1; AT5G51100.1; AT5G51100.
DR GeneID; 835183; -.
DR Gramene; AT5G51100.1; AT5G51100.1; AT5G51100.
DR KEGG; ath:AT5G51100; -.
DR Araport; AT5G51100; -.
DR TAIR; locus:2176167; AT5G51100.
DR eggNOG; KOG0876; Eukaryota.
DR HOGENOM; CLU_031625_0_0_1; -.
DR InParanoid; Q9LU64; -.
DR OMA; HNQFWEM; -.
DR OrthoDB; 1353361at2759; -.
DR PhylomeDB; Q9LU64; -.
DR BioCyc; MetaCyc:AT5G51100-MON; -.
DR PRO; PR:Q9LU64; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LU64; baseline and differential.
DR Genevisible; Q9LU64; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0042644; C:chloroplast nucleoid; IDA:UniProtKB.
DR GO; GO:0009534; C:chloroplast thylakoid; IEA:UniProtKB-SubCell.
DR GO; GO:0009579; C:thylakoid; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004784; F:superoxide dismutase activity; IDA:UniProtKB.
DR GO; GO:0009411; P:response to UV; IEP:TAIR.
DR Gene3D; 1.10.287.990; -; 1.
DR Gene3D; 3.55.40.20; -; 1.
DR InterPro; IPR001189; Mn/Fe_SOD.
DR InterPro; IPR019833; Mn/Fe_SOD_BS.
DR InterPro; IPR019832; Mn/Fe_SOD_C.
DR InterPro; IPR019831; Mn/Fe_SOD_N.
DR InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR InterPro; IPR036314; SOD_C_sf.
DR Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 1.
DR PRINTS; PR01703; MNSODISMTASE.
DR SUPFAM; SSF46609; SSF46609; 1.
DR SUPFAM; SSF54719; SSF54719; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Iron; Metal-binding; Oxidoreductase; Plastid;
KW Reference proteome; Repeat; Thylakoid; Transit peptide.
FT TRANSIT 1..46
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 47..305
FT /note="Superoxide dismutase [Fe] 2, chloroplastic"
FT /id="PRO_0000421265"
FT REGION 270..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..305
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 77
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT TURN 62..68
FT /evidence="ECO:0007829|PDB:7BJK"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:7BJK"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:7BJK"
FT HELIX 81..93
FT /evidence="ECO:0007829|PDB:7BJK"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:7BJK"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:7BJK"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:7BJK"
FT HELIX 120..134
FT /evidence="ECO:0007829|PDB:7BJK"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:7BJK"
FT HELIX 159..172
FT /evidence="ECO:0007829|PDB:7BJK"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:7BJK"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:7BJK"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:7BJK"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:7BJK"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:7BJK"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:7BJK"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:7BJK"
FT HELIX 256..274
FT /evidence="ECO:0007829|PDB:7BJK"
SQ SEQUENCE 305 AA; 34664 MW; 6A68EAF701EA5AC2 CRC64;
MMNVAVTATP SSLLYSPLLL PSQGPNRRMQ WKRNGKRRLG TKVAVSGVIT AGFELKPPPY
PLDALEPHMS RETLDYHWGK HHKTYVENLN KQILGTDLDA LSLEEVVLLS YNKGNMLPAF
NNAAQAWNHE FFWESIQPGG GGKPTGELLR LIERDFGSFE EFLERFKSAA ASNFGSGWTW
LAYKANRLDV ANAVNPLPKE EDKKLVIVKT PNAVNPLVWD YSPLLTIDTW EHAYYLDFEN
RRAEYINTFM EKLVSWETVS TRLESAIARA VQREQEGTET EDEENPDDEV PEVYLDSDID
VSEVD
