Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Superoxide dismutase [Fe] 1, chloroplastic

Gene

FSD1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Fe cation1 PublicationNote: Binds 1 Fe cation per subunit.1 Publication

Enzyme regulationi

Activated by cpn20/cpn21.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi35 – 351IronBy similarity
Metal bindingi87 – 871IronBy similarity
Metal bindingi169 – 1691IronBy similarity
Metal bindingi173 – 1731IronBy similarity

GO - Molecular functioni

  • copper ion binding Source: TAIR
  • superoxide dismutase activity Source: TAIR

GO - Biological processi

  • circadian rhythm Source: TAIR
  • removal of superoxide radicals Source: GOC
  • response to cadmium ion Source: TAIR
  • response to copper ion Source: TAIR
  • response to light intensity Source: UniProtKB
  • response to oxidative stress Source: TAIR
  • response to ozone Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciARA:GQT-1863-MONOMER.
ARA:GQT-1864-MONOMER.
ARA:GQT-1865-MONOMER.
ARA:GQT-1866-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Fe] 1, chloroplastic (EC:1.15.1.1)
Alternative name(s):
Protein FE SUPEROXIDE DISMUTASE 1
Gene namesi
Name:FSD1
Synonyms:SODB
Ordered Locus Names:At4g25100
ORF Names:F13M23.240
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G25100.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast envelope Source: TAIR
  • chloroplast membrane Source: UniProtKB-SubCell
  • chloroplast stroma Source: TAIR
  • cytoplasm Source: UniProtKB
  • mitochondrion Source: TAIR
  • plasma membrane Source: TAIR
  • thylakoid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 212Superoxide dismutase [Fe] 1, chloroplasticPRO_0000032889
Initiator methionineiRemovedCombined sources
Transit peptidei2 – ?ChloroplastSequence analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP21276.
PRIDEiP21276.

Expressioni

Inductioni

Circadian-regulation. Down-regulated upon photosynthetically active radiation (PAR) (e.g. light fluence) increase and in response to ozone fumigation.1 Publication

Gene expression databases

ExpressionAtlasiP21276. baseline and differential.
GenevisibleiP21276. AT.

Interactioni

Subunit structurei

Homodimer. Interacts with cpn20/cpn21.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CPN21O652822EBI-4466816,EBI-4435709

Protein-protein interaction databases

BioGridi13900. 7 interactions.
IntActiP21276. 2 interactions.
STRINGi3702.AT4G25100.1.

Structurei

3D structure databases

ProteinModelPortaliP21276.
SMRiP21276. Positions 7-212.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0876. Eukaryota.
COG0605. LUCA.
HOGENOMiHOG000013584.
InParanoidiP21276.
OMAiTANYVLK.
PhylomeDBiP21276.

Family and domain databases

InterProiIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERiPTHR11404. PTHR11404. 1 hit.
PfamiPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000349. SODismutase. 1 hit.
PRINTSiPR01703. MNSODISMTASE.
SUPFAMiSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEiPS00088. SOD_MN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: P21276-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAASSAVTAN YVLKPPPFAL DALEPHMSKQ TLEFHWGKHH RAYVDNLKKQ
60 70 80 90 100
VLGTELEGKP LEHIIHSTYN NGDLLPAFNN AAQAWNHEFF WESMKPGGGG
110 120 130 140 150
KPSGELLALL ERDFTSYEKF YEEFNAAAAT QFGAGWAWLA YSNEKLKVVK
160 170 180 190 200
TPNAVNPLVL GSFPLLTIDV WEHAYYLDFQ NRRPDYIKTF MTNLVSWEAV
210
SARLEAAKAA SA
Length:212
Mass (Da):23,791
Last modified:December 15, 2003 - v4
Checksum:iBCFDA057F040F9DD
GO

Sequence cautioni

The sequence AAA32791.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAB36752.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB79419.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55910 mRNA. Translation: AAA32791.1. Different initiation.
AL035523 Genomic DNA. Translation: CAB36752.1. Sequence problems.
AL161562 Genomic DNA. Translation: CAB79419.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE85007.1.
CP002687 Genomic DNA. Translation: AEE85008.1.
CP002687 Genomic DNA. Translation: AEE85009.1.
CP002687 Genomic DNA. Translation: AEE85011.1.
AF326862 mRNA. Translation: AAG41444.1.
AF324711 mRNA. Translation: AAG40062.1.
AF339685 mRNA. Translation: AAK00367.1.
AY039560 mRNA. Translation: AAK62615.1.
AY129470 mRNA. Translation: AAM91056.1.
AY087220 mRNA. Translation: AAM64776.1.
PIRiB39267.
G85289.
T05531.
RefSeqiNP_001190834.1. NM_001203905.1. [P21276-1]
NP_194240.1. NM_118642.2. [P21276-1]
NP_849440.1. NM_179109.2. [P21276-1]
NP_849441.1. NM_179110.2. [P21276-1]
UniGeneiAt.22638.
At.47521.
At.486.

Genome annotation databases

EnsemblPlantsiAT4G25100.1; AT4G25100.1; AT4G25100. [P21276-1]
AT4G25100.2; AT4G25100.2; AT4G25100. [P21276-1]
AT4G25100.3; AT4G25100.3; AT4G25100. [P21276-1]
AT4G25100.5; AT4G25100.5; AT4G25100. [P21276-1]
GeneIDi828613.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55910 mRNA. Translation: AAA32791.1. Different initiation.
AL035523 Genomic DNA. Translation: CAB36752.1. Sequence problems.
AL161562 Genomic DNA. Translation: CAB79419.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE85007.1.
CP002687 Genomic DNA. Translation: AEE85008.1.
CP002687 Genomic DNA. Translation: AEE85009.1.
CP002687 Genomic DNA. Translation: AEE85011.1.
AF326862 mRNA. Translation: AAG41444.1.
AF324711 mRNA. Translation: AAG40062.1.
AF339685 mRNA. Translation: AAK00367.1.
AY039560 mRNA. Translation: AAK62615.1.
AY129470 mRNA. Translation: AAM91056.1.
AY087220 mRNA. Translation: AAM64776.1.
PIRiB39267.
G85289.
T05531.
RefSeqiNP_001190834.1. NM_001203905.1. [P21276-1]
NP_194240.1. NM_118642.2. [P21276-1]
NP_849440.1. NM_179109.2. [P21276-1]
NP_849441.1. NM_179110.2. [P21276-1]
UniGeneiAt.22638.
At.47521.
At.486.

3D structure databases

ProteinModelPortaliP21276.
SMRiP21276. Positions 7-212.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi13900. 7 interactions.
IntActiP21276. 2 interactions.
STRINGi3702.AT4G25100.1.

Proteomic databases

PaxDbiP21276.
PRIDEiP21276.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G25100.1; AT4G25100.1; AT4G25100. [P21276-1]
AT4G25100.2; AT4G25100.2; AT4G25100. [P21276-1]
AT4G25100.3; AT4G25100.3; AT4G25100. [P21276-1]
AT4G25100.5; AT4G25100.5; AT4G25100. [P21276-1]
GeneIDi828613.

Organism-specific databases

TAIRiAT4G25100.

Phylogenomic databases

eggNOGiKOG0876. Eukaryota.
COG0605. LUCA.
HOGENOMiHOG000013584.
InParanoidiP21276.
OMAiTANYVLK.
PhylomeDBiP21276.

Enzyme and pathway databases

BioCyciARA:GQT-1863-MONOMER.
ARA:GQT-1864-MONOMER.
ARA:GQT-1865-MONOMER.
ARA:GQT-1866-MONOMER.

Miscellaneous databases

PROiP21276.

Gene expression databases

ExpressionAtlasiP21276. baseline and differential.
GenevisibleiP21276. AT.

Family and domain databases

InterProiIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERiPTHR11404. PTHR11404. 1 hit.
PfamiPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000349. SODismutase. 1 hit.
PRINTSiPR01703. MNSODISMTASE.
SUPFAMiSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEiPS00088. SOD_MN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of iron superoxide dismutase cDNAs from plants obtained by genetic complementation in Escherichia coli."
    van Camp W., Bowler C., Villarroel R., Tsang E.W.T., van Montagu M., Inze D.
    Proc. Natl. Acad. Sci. U.S.A. 87:9903-9907(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. C24.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    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.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    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.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Superoxide dismutase in Arabidopsis: an eclectic enzyme family with disparate regulation and protein localization."
    Kliebenstein D.J., Monde R.A., Last R.L.
    Plant Physiol. 118:637-650(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY LIGHT AND OZONE, GENE FAMILY.
  7. "Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana."
    Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M., Garin J., Joyard J., Rolland N.
    Mol. Cell. Proteomics 2:325-345(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Wassilewskija.
  8. "The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions."
    Kleffmann T., Russenberger D., von Zychlinski A., Christopher W., Sjoelander K., Gruissem W., Baginsky S.
    Curr. Biol. 14:354-362(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  10. "A heterocomplex of iron superoxide dismutases defends chloroplast nucleoids against oxidative stress and is essential for chloroplast development in Arabidopsis."
    Myouga F., Hosoda C., Umezawa T., Iizumi H., Kuromori T., Motohashi R., Shono Y., Nagata N., Ikeuchi M., Shinozaki K.
    Plant Cell 20:3148-3162(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUBUNIT.
  11. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "CHAPERONIN 20 mediates iron superoxide dismutase (FeSOD) activity independent of its co-chaperonin role in Arabidopsis chloroplasts."
    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.
    New Phytol. 197:99-110(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, COFACTOR, INTERACTION WITH CPN20/CPN21, ENZYME REGULATION.

Entry informationi

Entry nameiSODF1_ARATH
AccessioniPrimary (citable) accession number: P21276
Secondary accession number(s): Q9FE21, Q9SW16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: December 15, 2003
Last modified: November 11, 2015
This is version 140 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.