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Superoxide dismutase [Fe] 1, chloroplastic (EC 1.15.1.1) (Protein FE SUPEROXIDE DISMUTASE 1)

 SODF1_ARATH             Reviewed;         212 AA.
P21276; Q9FE21; Q9SW16;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
15-DEC-2003, sequence version 4.
12-SEP-2018, entry version 161.
RecName: Full=Superoxide dismutase [Fe] 1, chloroplastic;
EC=1.15.1.1;
AltName: Full=Protein FE SUPEROXIDE DISMUTASE 1;
Flags: Precursor;
Name=FSD1; Synonyms=SODB; OrderedLocusNames=At4g25100;
ORFNames=F13M23.240;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. C24;
PubMed=2263641; DOI=10.1073/pnas.87.24.9903;
van Camp W., Bowler C., Villarroel R., Tsang E.W.T., van Montagu M.,
Inze D.;
"Characterization of iron superoxide dismutase cDNAs from plants
obtained by genetic complementation in Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 87:9903-9907(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
INDUCTION BY LIGHT AND OZONE, AND GENE FAMILY.
PubMed=9765550; DOI=10.1104/pp.118.2.637;
Kliebenstein D.J., Monde R.A., Last R.L.;
"Superoxide dismutase in Arabidopsis: an eclectic enzyme family with
disparate regulation and protein localization.";
Plant Physiol. 118:637-650(1998).
[7]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
PubMed=15060130; DOI=10.1074/mcp.M400001-MCP200;
Marmagne A., Rouet M.-A., Ferro M., Rolland N., Alcon C., Joyard J.,
Garin J., Barbier-Brygoo H., Ephritikhine G.;
"Identification of new intrinsic proteins in Arabidopsis plasma
membrane proteome.";
Mol. Cell. Proteomics 3:675-691(2004).
[8]
SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=18996978; DOI=10.1105/tpc.108.061341;
Myouga F., Hosoda C., Umezawa T., Iizumi H., Kuromori T.,
Motohashi R., Shono Y., Nagata N., Ikeuchi M., Shinozaki K.;
"A heterocomplex of iron superoxide dismutases defends chloroplast
nucleoids against oxidative stress and is essential for chloroplast
development in Arabidopsis.";
Plant Cell 20:3148-3162(2008).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[10]
SUBCELLULAR LOCATION, COFACTOR, INTERACTION WITH CPN20/CPN21, AND
ACTIVITY REGULATION.
PubMed=23057508; DOI=10.1111/j.1469-8137.2012.04369.x;
Kuo W.Y., Huang C.H., Liu A.C., Cheng C.P., Li S.H., Chang W.C.,
Weiss C., Azem A., Jinn T.L.;
"CHAPERONIN 20 mediates iron superoxide dismutase (FeSOD) activity
independent of its co-chaperonin role in Arabidopsis chloroplasts.";
New Phytol. 197:99-110(2013).
-!- FUNCTION: Destroys superoxide anion radicals which are normally
produced within the cells and which are toxic to biological
systems.
-!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875;
Evidence={ECO:0000269|PubMed:23057508};
Note=Binds 1 Fe cation per subunit. {ECO:0000269|PubMed:23057508};
-!- ACTIVITY REGULATION: Activated by cpn20/cpn21.
{ECO:0000269|PubMed:23057508}.
-!- SUBUNIT: Homodimer. Interacts with cpn20/cpn21.
{ECO:0000269|PubMed:18996978, ECO:0000269|PubMed:23057508}.
-!- INTERACTION:
O65282:CPN20; NbExp=2; IntAct=EBI-4466816, EBI-4435709;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15060130}.
Plastid, chloroplast membrane. Plastid, chloroplast stroma.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=P21276-1; Sequence=Displayed;
-!- INDUCTION: Circadian-regulation. Down-regulated upon
photosynthetically active radiation (PAR) (e.g. light fluence)
increase and in response to ozone fumigation.
{ECO:0000269|PubMed:9765550}.
-!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA32791.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAB36752.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAB79419.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M55910; AAA32791.1; ALT_INIT; mRNA.
EMBL; AL035523; CAB36752.1; ALT_SEQ; Genomic_DNA.
EMBL; AL161562; CAB79419.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002687; AEE85007.1; -; Genomic_DNA.
EMBL; CP002687; AEE85008.1; -; Genomic_DNA.
EMBL; CP002687; AEE85009.1; -; Genomic_DNA.
EMBL; CP002687; AEE85011.1; -; Genomic_DNA.
EMBL; AF326862; AAG41444.1; -; mRNA.
EMBL; AF324711; AAG40062.1; -; mRNA.
EMBL; AF339685; AAK00367.1; -; mRNA.
EMBL; AY039560; AAK62615.1; -; mRNA.
EMBL; AY129470; AAM91056.1; -; mRNA.
EMBL; AY087220; AAM64776.1; -; mRNA.
PIR; B39267; B39267.
PIR; G85289; G85289.
PIR; T05531; T05531.
RefSeq; NP_001190834.1; NM_001203905.1. [P21276-1]
RefSeq; NP_194240.1; NM_118642.2. [P21276-1]
RefSeq; NP_849440.1; NM_179109.3. [P21276-1]
RefSeq; NP_849441.1; NM_179110.2. [P21276-1]
UniGene; At.22638; -.
UniGene; At.47521; -.
UniGene; At.486; -.
ProteinModelPortal; P21276; -.
SMR; P21276; -.
BioGrid; 13900; 7.
IntAct; P21276; 2.
STRING; 3702.AT4G25100.1; -.
iPTMnet; P21276; -.
PaxDb; P21276; -.
PRIDE; P21276; -.
EnsemblPlants; AT4G25100.1; AT4G25100.1; AT4G25100. [P21276-1]
EnsemblPlants; AT4G25100.2; AT4G25100.2; AT4G25100. [P21276-1]
EnsemblPlants; AT4G25100.3; AT4G25100.3; AT4G25100. [P21276-1]
EnsemblPlants; AT4G25100.5; AT4G25100.5; AT4G25100. [P21276-1]
GeneID; 828613; -.
Gramene; AT4G25100.1; AT4G25100.1; AT4G25100. [P21276-1]
Gramene; AT4G25100.2; AT4G25100.2; AT4G25100. [P21276-1]
Gramene; AT4G25100.3; AT4G25100.3; AT4G25100. [P21276-1]
Gramene; AT4G25100.5; AT4G25100.5; AT4G25100. [P21276-1]
KEGG; ath:AT4G25100; -.
Araport; AT4G25100; -.
TAIR; locus:2117273; AT4G25100.
eggNOG; KOG0876; Eukaryota.
eggNOG; COG0605; LUCA.
HOGENOM; HOG000013584; -.
InParanoid; P21276; -.
KO; K04564; -.
OMA; YIKYWEN; -.
OrthoDB; EOG09360IDF; -.
PhylomeDB; P21276; -.
PRO; PR:P21276; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; P21276; baseline and differential.
Genevisible; P21276; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009579; C:thylakoid; IDA:TAIR.
GO; GO:0005507; F:copper ion binding; IDA:TAIR.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:0004784; F:superoxide dismutase activity; IMP:TAIR.
GO; GO:0007623; P:circadian rhythm; IEP:TAIR.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0046688; P:response to copper ion; IEP:TAIR.
GO; GO:0009642; P:response to light intensity; IEP:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; IDA:TAIR.
GO; GO:0010193; P:response to ozone; IEP:UniProtKB.
Gene3D; 1.10.287.990; -; 1.
Gene3D; 2.40.500.20; -; 1.
InterPro; IPR001189; Mn/Fe_SOD.
InterPro; IPR019833; Mn/Fe_SOD_BS.
InterPro; IPR019832; Mn/Fe_SOD_C.
InterPro; IPR019831; Mn/Fe_SOD_N.
InterPro; IPR036324; Mn/Fe_SOD_N_sf.
InterPro; IPR036314; SOD_C_sf.
Pfam; PF02777; Sod_Fe_C; 1.
Pfam; PF00081; Sod_Fe_N; 1.
PIRSF; PIRSF000349; SODismutase; 1.
PRINTS; PR01703; MNSODISMTASE.
SUPFAM; SSF46609; SSF46609; 1.
SUPFAM; SSF54719; SSF54719; 1.
PROSITE; PS00088; SOD_MN; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell membrane; Chloroplast;
Complete proteome; Iron; Membrane; Metal-binding; Oxidoreductase;
Plastid; Reference proteome; Transit peptide.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
TRANSIT 2 ? Chloroplast. {ECO:0000255}.
CHAIN ? 212 Superoxide dismutase [Fe] 1,
chloroplastic.
/FTId=PRO_0000032889.
METAL 35 35 Iron. {ECO:0000250}.
METAL 87 87 Iron. {ECO:0000250}.
METAL 169 169 Iron. {ECO:0000250}.
METAL 173 173 Iron. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895}.
SEQUENCE 212 AA; 23791 MW; BCFDA057F040F9DD CRC64;
MAASSAVTAN YVLKPPPFAL DALEPHMSKQ TLEFHWGKHH RAYVDNLKKQ VLGTELEGKP
LEHIIHSTYN NGDLLPAFNN AAQAWNHEFF WESMKPGGGG KPSGELLALL ERDFTSYEKF
YEEFNAAAAT QFGAGWAWLA YSNEKLKVVK TPNAVNPLVL GSFPLLTIDV WEHAYYLDFQ
NRRPDYIKTF MTNLVSWEAV SARLEAAKAA SA


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