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Protein

Superoxide dismutase [Mn] 2, mitochondrial

Gene

MSD2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi60 – 601ManganeseBy similarity
Metal bindingi108 – 1081ManganeseBy similarity
Metal bindingi197 – 1971ManganeseBy similarity
Metal bindingi201 – 2011ManganeseBy similarity

GO - Molecular functioni

GO - Biological processi

  • floral organ abscission Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT3G56350-MONOMER.
ReactomeiR-ATH-3299685. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Mn] 2, mitochondrial (EC:1.15.1.1)
Alternative name(s):
Protein MANGANESE SUPEROXIDE DISMUTASE 2
Short name:
AtMSD2
Gene namesi
Name:MSD2
Ordered Locus Names:At3g56350
ORF Names:F18O21_310
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G56350.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 241Superoxide dismutase [Mn] 2, mitochondrialSequence analysisPRO_5000237373
Transit peptidei1 – ?MitochondrionBy similarity

Proteomic databases

PaxDbiQ9LYK8.
PRIDEiQ9LYK8.
ProMEXiQ9LYK8.

Expressioni

Gene expression databases

GenevisibleiQ9LYK8. AT.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

BioGridi10118. 1 interaction.
STRINGi3702.AT3G56350.1.

Structurei

3D structure databases

ProteinModelPortaliQ9LYK8.
SMRiQ9LYK8. Positions 35-233.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0876. Eukaryota.
COG0605. LUCA.
HOGENOMiHOG000013583.
InParanoidiQ9LYK8.
KOiK04564.
OMAiSGWVWFG.
PhylomeDBiQ9LYK8.

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.

Q9LYK8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTTVIIIIF VAIFATTLHD ARGATMEPCL ESMKTASLPD LPYAYDALEP
60 70 80 90 100
AISEEIMRLH HQKHHQTYVT QYNKALNSLR SAMADGDHSS VVKLQSLIKF
110 120 130 140 150
NGGGHVNHAI FWKNLAPVHE GGGKPPHDPL ASAIDAHFGS LEGLIQKMNA
160 170 180 190 200
EGAAVQGSGW VWFGLDRELK RLVVETTANQ DPLVTKGSHL VPLIGIDVWE
210 220 230 240
HAYYPQYKNA RAEYLKNIWT VINWKYAADV FEKHTRDLDI N
Length:241
Mass (Da):26,892
Last modified:October 1, 2000 - v1
Checksum:i22E5F2FB84DD99D4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY151395 mRNA. Translation: AAN46857.1.
AL163763 Genomic DNA. Translation: CAB87434.1.
CP002686 Genomic DNA. Translation: AEE79512.1.
BT004168 mRNA. Translation: AAO42188.1.
PIRiT47752.
RefSeqiNP_191194.1. NM_115493.3.
UniGeneiAt.34942.

Genome annotation databases

EnsemblPlantsiAT3G56350.1; AT3G56350.1; AT3G56350.
GeneIDi824802.
GrameneiAT3G56350.1; AT3G56350.1; AT3G56350.
KEGGiath:AT3G56350.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY151395 mRNA. Translation: AAN46857.1.
AL163763 Genomic DNA. Translation: CAB87434.1.
CP002686 Genomic DNA. Translation: AEE79512.1.
BT004168 mRNA. Translation: AAO42188.1.
PIRiT47752.
RefSeqiNP_191194.1. NM_115493.3.
UniGeneiAt.34942.

3D structure databases

ProteinModelPortaliQ9LYK8.
SMRiQ9LYK8. Positions 35-233.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi10118. 1 interaction.
STRINGi3702.AT3G56350.1.

Proteomic databases

PaxDbiQ9LYK8.
PRIDEiQ9LYK8.
ProMEXiQ9LYK8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G56350.1; AT3G56350.1; AT3G56350.
GeneIDi824802.
GrameneiAT3G56350.1; AT3G56350.1; AT3G56350.
KEGGiath:AT3G56350.

Organism-specific databases

TAIRiAT3G56350.

Phylogenomic databases

eggNOGiKOG0876. Eukaryota.
COG0605. LUCA.
HOGENOMiHOG000013583.
InParanoidiQ9LYK8.
KOiK04564.
OMAiSGWVWFG.
PhylomeDBiQ9LYK8.

Enzyme and pathway databases

BioCyciARA:AT3G56350-MONOMER.
ReactomeiR-ATH-3299685. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

PROiQ9LYK8.

Gene expression databases

GenevisibleiQ9LYK8. 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. "The character of manganese superoxide dismutases in Arabidopsis."
    Pan S.-M., Chung M.-H.
    Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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] OF 8-241.
    Strain: cv. Columbia.
  5. "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: GENE FAMILY.

Entry informationi

Entry nameiSODM2_ARATH
AccessioniPrimary (citable) accession number: Q9LYK8
Secondary accession number(s): Q84W70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: October 1, 2000
Last modified: February 17, 2016
This is version 116 of the entry and version 1 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.