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Protein

Superoxide dismutase [Mn] 1, mitochondrial

Gene

MSD1

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

Mn2+By similarityNote: Binds 1 Mn2+ ion per subunit.By similarity

Enzyme regulationi

Activated by MTM1.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi55 – 551ManganeseBy similarity
Metal bindingi103 – 1031ManganeseBy similarity
Metal bindingi192 – 1921ManganeseBy similarity
Metal bindingi196 – 1961ManganeseBy similarity

GO - Molecular functioni

  • copper ion binding Source: TAIR
  • metal ion binding Source: TAIR
  • superoxide dismutase activity Source: UniProtKB-EC

GO - Biological processi

  • defense response to bacterium Source: TAIR
  • embryo development ending in seed dormancy Source: TAIR
  • response to salt stress Source: TAIR
  • response to zinc ion Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciARA:GQT-1754-MONOMER.
ReactomeiR-ATH-3299685. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Mn] 1, mitochondrial (EC:1.15.1.1)
Alternative name(s):
Protein MANGANESE SUPEROXIDE DISMUTASE 1
Short name:
AtMSD1
Protein MATERNAL EFFECT EMBRYO ARREST 33
Gene namesi
Name:MSD1
Synonyms:MEE3, SODA
Ordered Locus Names:At3g10920
ORF Names:F9F8.26
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G10920.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2929MitochondrionBy similarityAdd
BLAST
Chaini30 – 231202Superoxide dismutase [Mn] 1, mitochondrialPRO_0000032891Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei124 – 1241PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO81235.
PRIDEiO81235.

PTM databases

iPTMnetiO81235.

Expressioni

Inductioni

Induced by salt stress.1 Publication

Gene expression databases

ExpressionAtlasiO81235. baseline and differential.
GenevisibleiO81235. AT.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi3702.AT3G10920.1.

Structurei

Secondary structure

1
231
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi40 – 434Combined sources
Turni44 – 463Combined sources
Helixi49 – 579Combined sources
Helixi59 – 8022Combined sources
Helixi83 – 886Combined sources
Helixi90 – 10819Combined sources
Helixi113 – 1153Combined sources
Turni116 – 1183Combined sources
Helixi123 – 13311Combined sources
Helixi136 – 14914Combined sources
Beta strandi152 – 16110Combined sources
Turni162 – 1654Combined sources
Beta strandi166 – 1738Combined sources
Helixi178 – 1814Combined sources
Beta strandi185 – 1928Combined sources
Helixi195 – 1973Combined sources
Helixi199 – 2024Combined sources
Helixi206 – 2127Combined sources
Helixi213 – 2164Combined sources
Helixi219 – 22810Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C7UX-ray1.95A/B/C/D/E/F/G/H30-231[»]
ProteinModelPortaliO81235.
SMRiO81235. Positions 30-231.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0876. Eukaryota.
COG0605. LUCA.
HOGENOMiHOG000013583.
InParanoidiO81235.
OMAiVIDWVEV.
PhylomeDBiO81235.

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: O81235-1) [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
MAIRCVASRK TLAGLKETSS RLLRIRGIQT FTLPDLPYDY GALEPAISGE
60 70 80 90 100
IMQIHHQKHH QAYVTNYNNA LEQLDQAVNK GDASTVVKLQ SAIKFNGGGH
110 120 130 140 150
VNHSIFWKNL APSSEGGGEP PKGSLGSAID AHFGSLEGLV KKMSAEGAAV
160 170 180 190 200
QGSGWVWLGL DKELKKLVVD TTANQDPLVT KGGSLVPLVG IDVWEHAYYL
210 220 230
QYKNVRPEYL KNVWKVINWK YASEVYEKEN N
Length:231
Mass (Da):25,444
Last modified:June 20, 2002 - v2
Checksum:i2DBD5560A9E8AD7D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti169 – 1691V → F in AAC24832 (PubMed:9765550).Curated
Sequence conflicti230 – 2301N → S in AAM62550 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061518 mRNA. Translation: AAC24832.1.
AC009991 Genomic DNA. Translation: AAF01529.1.
CP002686 Genomic DNA. Translation: AEE74977.1.
AY072495 mRNA. Translation: AAL66910.1.
AY059807 mRNA. Translation: AAL24289.1.
AY085319 mRNA. Translation: AAM62550.1.
PIRiPA0012.
T50827.
RefSeqiNP_187703.1. NM_111929.3. [O81235-1]
UniGeneiAt.11023.

Genome annotation databases

EnsemblPlantsiAT3G10920.1; AT3G10920.1; AT3G10920. [O81235-1]
GeneIDi820263.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061518 mRNA. Translation: AAC24832.1.
AC009991 Genomic DNA. Translation: AAF01529.1.
CP002686 Genomic DNA. Translation: AEE74977.1.
AY072495 mRNA. Translation: AAL66910.1.
AY059807 mRNA. Translation: AAL24289.1.
AY085319 mRNA. Translation: AAM62550.1.
PIRiPA0012.
T50827.
RefSeqiNP_187703.1. NM_111929.3. [O81235-1]
UniGeneiAt.11023.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C7UX-ray1.95A/B/C/D/E/F/G/H30-231[»]
ProteinModelPortaliO81235.
SMRiO81235. Positions 30-231.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT3G10920.1.

PTM databases

iPTMnetiO81235.

Proteomic databases

PaxDbiO81235.
PRIDEiO81235.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G10920.1; AT3G10920.1; AT3G10920. [O81235-1]
GeneIDi820263.

Organism-specific databases

TAIRiAT3G10920.

Phylogenomic databases

eggNOGiKOG0876. Eukaryota.
COG0605. LUCA.
HOGENOMiHOG000013583.
InParanoidiO81235.
OMAiVIDWVEV.
PhylomeDBiO81235.

Enzyme and pathway databases

BioCyciARA:GQT-1754-MONOMER.
ReactomeiR-ATH-3299685. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

PROiO81235.

Gene expression databases

ExpressionAtlasiO81235. baseline and differential.
GenevisibleiO81235. 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. "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: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY.
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [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. "Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins."
    Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.
    Plant Cell 16:241-256(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Landsberg erecta.
  7. "AtMTM1, a novel mitochondrial protein, may be involved in activation of the manganese-containing superoxide dismutase in Arabidopsis."
    Su Z., Chai M.F., Lu P.L., An R., Chen J., Wang X.C.
    Planta 226:1031-1039(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  8. "Long-term effects of mild salt stress on growth, ion accumulation and superoxide dismutase expression of Arabidopsis rosette leaves."
    Attia H., Arnaud N., Karray N., Lachaal M.
    Physiol. Plantarum 132:293-305(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY SALT.
  9. "Identification of phosphoproteins in Arabidopsis thaliana leaves using polyethylene glycol fractionation, immobilized metal-ion affinity chromatography, two-dimensional gel electrophoresis and mass spectrometry."
    Aryal U.K., Krochko J.E., Ross A.R.
    J. Proteome Res. 11:425-437(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSODM1_ARATH
AccessioniPrimary (citable) accession number: O81235
Secondary accession number(s): Q8LEP0, Q9SRK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: June 20, 2002
Last modified: February 17, 2016
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.