SODF1_ARATH
ID SODF1_ARATH Reviewed; 212 AA.
AC P21276; Q9FE21; Q9SW16;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 4.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Superoxide dismutase [Fe] 1, chloroplastic;
DE EC=1.15.1.1 {ECO:0000305|PubMed:23057508};
DE AltName: Full=Protein FE SUPEROXIDE DISMUTASE 1;
DE Short=FeSOD {ECO:0000303|PubMed:23057508};
DE Flags: Precursor;
GN Name=FSD1; Synonyms=SODB; OrderedLocusNames=At4g25100; ORFNames=F13M23.240;
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 [MRNA].
RC STRAIN=cv. C24;
RX PubMed=2263641; DOI=10.1073/pnas.87.24.9903;
RA van Camp W., Bowler C., Villarroel R., Tsang E.W.T., van Montagu M.,
RA Inze D.;
RT "Characterization of iron superoxide dismutase cDNAs from plants obtained
RT by genetic complementation in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:9903-9907(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
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 [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 INDUCTION BY LIGHT AND OZONE, 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=15060130; DOI=10.1074/mcp.m400001-mcp200;
RA Marmagne A., Rouet M.-A., Ferro M., Rolland N., Alcon C., Joyard J.,
RA Garin J., Barbier-Brygoo H., Ephritikhine G.;
RT "Identification of new intrinsic proteins in Arabidopsis plasma membrane
RT proteome.";
RL Mol. Cell. Proteomics 3:675-691(2004).
RN [8]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10]
RP SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP AND INTERACTION WITH CPN20/CPN21.
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).
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
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:0000305|PubMed:23057508};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:23057508};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000269|PubMed:23057508};
CC -!- ACTIVITY REGULATION: Activated by cpn20/cpn21.
CC {ECO:0000269|PubMed:23057508}.
CC -!- SUBUNIT: Homodimer. Interacts with cpn20/cpn21.
CC {ECO:0000269|PubMed:18996978, ECO:0000269|PubMed:23057508}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15060130}.
CC Plastid, chloroplast membrane. Plastid, chloroplast stroma.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P21276-1; Sequence=Displayed;
CC -!- INDUCTION: Circadian-regulation. Down-regulated upon photosynthetically
CC active radiation (PAR) (e.g. light fluence) increase and in response to
CC ozone fumigation. {ECO:0000269|PubMed:9765550}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA32791.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB36752.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79419.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M55910; AAA32791.1; ALT_INIT; mRNA.
DR EMBL; AL035523; CAB36752.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161562; CAB79419.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85007.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85008.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85009.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85011.1; -; Genomic_DNA.
DR EMBL; AF326862; AAG41444.1; -; mRNA.
DR EMBL; AF324711; AAG40062.1; -; mRNA.
DR EMBL; AF339685; AAK00367.1; -; mRNA.
DR EMBL; AY039560; AAK62615.1; -; mRNA.
DR EMBL; AY129470; AAM91056.1; -; mRNA.
DR EMBL; AY087220; AAM64776.1; -; mRNA.
DR PIR; B39267; B39267.
DR PIR; G85289; G85289.
DR PIR; T05531; T05531.
DR RefSeq; NP_001190834.1; NM_001203905.1. [P21276-1]
DR RefSeq; NP_194240.1; NM_118642.2. [P21276-1]
DR RefSeq; NP_849440.1; NM_179109.3. [P21276-1]
DR RefSeq; NP_849441.1; NM_179110.2. [P21276-1]
DR AlphaFoldDB; P21276; -.
DR SMR; P21276; -.
DR BioGRID; 13900; 9.
DR IntAct; P21276; 2.
DR STRING; 3702.AT4G25100.1; -.
DR iPTMnet; P21276; -.
DR PaxDb; P21276; -.
DR PRIDE; P21276; -.
DR ProteomicsDB; 228227; -. [P21276-1]
DR EnsemblPlants; AT4G25100.1; AT4G25100.1; AT4G25100. [P21276-1]
DR EnsemblPlants; AT4G25100.2; AT4G25100.2; AT4G25100. [P21276-1]
DR EnsemblPlants; AT4G25100.3; AT4G25100.3; AT4G25100. [P21276-1]
DR EnsemblPlants; AT4G25100.5; AT4G25100.5; AT4G25100. [P21276-1]
DR GeneID; 828613; -.
DR Gramene; AT4G25100.1; AT4G25100.1; AT4G25100. [P21276-1]
DR Gramene; AT4G25100.2; AT4G25100.2; AT4G25100. [P21276-1]
DR Gramene; AT4G25100.3; AT4G25100.3; AT4G25100. [P21276-1]
DR Gramene; AT4G25100.5; AT4G25100.5; AT4G25100. [P21276-1]
DR KEGG; ath:AT4G25100; -.
DR Araport; AT4G25100; -.
DR TAIR; locus:2117273; AT4G25100.
DR eggNOG; KOG0876; Eukaryota.
DR InParanoid; P21276; -.
DR OMA; TLDIWEH; -.
DR OrthoDB; 1353361at2759; -.
DR PhylomeDB; P21276; -.
DR PRO; PR:P21276; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P21276; baseline and differential.
DR Genevisible; P21276; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042644; C:chloroplast nucleoid; IBA:GO_Central.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0004784; F:superoxide dismutase activity; IMP:TAIR.
DR GO; GO:0007623; P:circadian rhythm; IEP:TAIR.
DR GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
DR GO; GO:0046688; P:response to copper ion; IEP:TAIR.
DR GO; GO:0009642; P:response to light intensity; IEP:UniProtKB.
DR GO; GO:0010193; P:response to ozone; IEP:UniProtKB.
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 PIRSF; PIRSF000349; SODismutase; 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 Acetylation; Alternative splicing; Cell membrane; Chloroplast; Iron;
KW Membrane; Metal-binding; Oxidoreductase; Plastid; Reference proteome;
KW Transit peptide.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT TRANSIT 2..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..212
FT /note="Superoxide dismutase [Fe] 1, chloroplastic"
FT /id="PRO_0000032889"
FT BINDING 35
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ 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
