GenomeNet

Database: UniProt
Entry: P21276
LinkDB: P21276
Original site: P21276 
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   16-JAN-2019, entry version 164.
DE   RecName: Full=Superoxide dismutase [Fe] 1, chloroplastic;
DE            EC=1.15.1.1;
DE   AltName: Full=Protein FE SUPEROXIDE DISMUTASE 1;
DE   Flags: Precursor;
GN   Name=FSD1; Synonyms=SODB; OrderedLocusNames=At4g25100;
GN   ORFNames=F13M23.240;
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 [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
RT   obtained 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.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   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.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   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
RT   reference 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.,
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   [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
RP   SCALE 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
RT   membrane 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.,
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   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.M111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
RA   Meinnel T., 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, COFACTOR, INTERACTION WITH CPN20/CPN21, AND
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).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       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   -!- 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   -!- INTERACTION:
CC       O65282:CPN20; NbExp=2; IntAct=EBI-4466816, EBI-4435709;
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
CC       photosynthetically active radiation (PAR) (e.g. light fluence)
CC       increase and in response to ozone fumigation.
CC       {ECO:0000269|PubMed:9765550}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA32791.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; 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};
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   UniGene; At.22638; -.
DR   UniGene; At.47521; -.
DR   UniGene; At.486; -.
DR   ProteinModelPortal; P21276; -.
DR   SMR; P21276; -.
DR   BioGrid; 13900; 7.
DR   IntAct; P21276; 2.
DR   STRING; 3702.AT4G25100.1; -.
DR   iPTMnet; P21276; -.
DR   PaxDb; P21276; -.
DR   PRIDE; P21276; -.
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   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013584; -.
DR   InParanoid; P21276; -.
DR   KO; K04564; -.
DR   OMA; YSKHHAT; -.
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; IDA: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; IDA:TAIR.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0009579; C:thylakoid; IDA:TAIR.
DR   GO; GO:0005507; F:copper ion binding; IDA: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:0006979; P:response to oxidative stress; IDA:TAIR.
DR   GO; GO:0010193; P:response to ozone; IEP:UniProtKB.
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   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;
KW   Complete proteome; Iron; Membrane; Metal-binding; Oxidoreductase;
KW   Plastid; Reference proteome; Transit peptide.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:22223895}.
FT   TRANSIT       2      ?       Chloroplast. {ECO:0000255}.
FT   CHAIN         ?    212       Superoxide dismutase [Fe] 1,
FT                                chloroplastic.
FT                                /FTId=PRO_0000032889.
FT   METAL        35     35       Iron. {ECO:0000250}.
FT   METAL        87     87       Iron. {ECO:0000250}.
FT   METAL       169    169       Iron. {ECO:0000250}.
FT   METAL       173    173       Iron. {ECO:0000250}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000244|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
//
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