GenomeNet

Database: UniProt
Entry: Q9LU64
LinkDB: Q9LU64
Original site: Q9LU64 
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   16-JAN-2019, entry version 125.
DE   RecName: Full=Superoxide dismutase [Fe] 2, chloroplastic;
DE            EC=1.15.1.1;
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;
GN   ORFNames=MWD22.4;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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
RT   reference 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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.,
RA   Hayashizaki Y., 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, DISRUPTION PHENOTYPE, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=18996978; DOI=10.1105/tpc.108.061341;
RA   Myouga F., Hosoda C., Umezawa T., Iizumi H., Kuromori T.,
RA   Motohashi R., 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.,
RA   Weiss C., 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
RT   gene 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
CC       systems (By similarity). Plays important role in chloroplast
CC       development, particularly in the maintenance of thylakoids
CC       membranes. Seems to act as a heterodimer with FSD3. {ECO:0000250,
CC       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   -!- 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
CC       MRL7 and PRDA1 (PubMed:24132784). {ECO:0000269|PubMed:18996978,
CC       ECO:0000269|PubMed:24132784}.
CC   -!- INTERACTION:
CC       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,
CC       highly vacuolated and without internal membrane structures like
CC       thylakoids. {ECO:0000269|PubMed:18996978}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
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   UniGene; At.212; -.
DR   ProteinModelPortal; Q9LU64; -.
DR   SMR; Q9LU64; -.
DR   BioGrid; 20428; 9.
DR   IntAct; Q9LU64; 8.
DR   STRING; 3702.AT5G51100.1; -.
DR   iPTMnet; Q9LU64; -.
DR   PaxDb; Q9LU64; -.
DR   PRIDE; Q9LU64; -.
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   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013584; -.
DR   InParanoid; Q9LU64; -.
DR   KO; K04564; -.
DR   OMA; FGTGWVW; -.
DR   OrthoDB; 1353361at2759; -.
DR   PhylomeDB; Q9LU64; -.
DR   BioCyc; MetaCyc:AT5G51100-MONOMER; -.
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:0009295; C:nucleoid; IDA:TAIR.
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:0055114; P:oxidation-reduction process; IDA:UniProtKB.
DR   GO; GO:0009411; P:response to UV; IEP:TAIR.
DR   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 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   Chloroplast; Complete proteome; Iron; Metal-binding; Oxidoreductase;
KW   Plastid; Reference proteome; Repeat; Thylakoid; Transit peptide.
FT   TRANSIT       1     46       Chloroplast. {ECO:0000255}.
FT   CHAIN        47    305       Superoxide dismutase [Fe] 2,
FT                                chloroplastic.
FT                                /FTId=PRO_0000421265.
FT   METAL        77     77       Iron. {ECO:0000250}.
FT   METAL       129    129       Iron. {ECO:0000250}.
FT   METAL       228    228       Iron. {ECO:0000250}.
FT   METAL       232    232       Iron. {ECO:0000250}.
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
//
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