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O81235 (SODM1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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 names
Name:MSD1
Synonyms:MEE3, SODA
Ordered Locus Names:At3g10920
ORF Names:F9F8.26
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length231 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

2 superoxide + 2 H+ = O2 + H2O2.

Cofactor

Binds 1 manganese ion per subunit By similarity.

Enzyme regulation

Activated by MTM1. Ref.7

Subunit structure

Homotetramer By similarity.

Subcellular location

Mitochondrion matrix.

Induction

Induced by salt stress. Ref.7 Ref.8

Sequence similarities

Belongs to the iron/manganese superoxide dismutase family.

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: O81235-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2929Mitochondrion By similarity
Chain30 – 231202Superoxide dismutase [Mn] 1, mitochondrial
PRO_0000032891

Sites

Metal binding551Manganese By similarity
Metal binding1031Manganese By similarity
Metal binding1921Manganese By similarity
Metal binding1961Manganese By similarity

Experimental info

Sequence conflict1691V → F in AAC24832. Ref.1
Sequence conflict2301N → S in AAM62550. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 20, 2002. Version 2.
Checksum: 2DBD5560A9E8AD7D

FASTA23125,444
        10         20         30         40         50         60 
MAIRCVASRK TLAGLKETSS RLLRIRGIQT FTLPDLPYDY GALEPAISGE IMQIHHQKHH 

        70         80         90        100        110        120 
QAYVTNYNNA LEQLDQAVNK GDASTVVKLQ SAIKFNGGGH VNHSIFWKNL APSSEGGGEP 

       130        140        150        160        170        180 
PKGSLGSAID AHFGSLEGLV KKMSAEGAAV QGSGWVWLGL DKELKKLVVD TTANQDPLVT 

       190        200        210        220        230 
KGGSLVPLVG IDVWEHAYYL QYKNVRPEYL KNVWKVINWK YASEVYEKEN N 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
IPIIPI00546447.
PIRPA0012.
T50827.
RefSeqNP_187703.1. NM_111929.3.
UniGeneAt.11023.

3D structure databases

ProteinModelPortalO81235.
SMRO81235. Positions 32-228.
ModBaseSearch...

Proteomic databases

PaxDbO81235.
PRIDEO81235.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G10920.1; AT3G10920.1; AT3G10920.
GeneID820263.
KEGGath:AT3G10920.

Organism-specific databases

GeneFarm1987.
TAIRAt3g10920.

Phylogenomic databases

eggNOGCOG0605.
HOGENOMHOG000013583.
InParanoidO81235.
KOK04564.
OMAWTVMAPN.
PhylomeDBO81235.
ProtClustDBPLN02471.

Gene expression databases

ArrayExpressO81235.
GenevestigatorO81235.

Family and domain databases

InterProIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERPTHR11404. PTHR11404. 1 hit.
PfamPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFPIRSF000349. SODismutase. 1 hit.
PRINTSPR01703. MNSODISMTASE.
SUPFAMSSF46609. SODismutase. 1 hit.
SSF54719. SODismutase. 1 hit.
PROSITEPS00088. SOD_MN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSODM1_ARATH
AccessionPrimary (citable) accession number: O81235
Secondary accession number(s): Q8LEP0, Q9SRK3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: June 20, 2002
Last modified: May 1, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families