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P24704 (SODC_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 106. 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 [Cu-Zn]

EC=1.15.1.1
Alternative name(s):
Copper/zinc superoxide dismutase 1
Gene names
Name:CSD1
Synonyms:SODCC
Ordered Locus Names:At1g08830
ORF Names:F22O13.32
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Destroys 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 copper ion per subunit By similarity.

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Sequence caution

The sequence AAF99769.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 152151Superoxide dismutase [Cu-Zn]
PRO_0000164131

Sites

Metal binding451Copper; catalytic By similarity
Metal binding471Copper; catalytic By similarity
Metal binding621Copper; catalytic By similarity
Metal binding621Zinc; structural By similarity
Metal binding701Zinc; structural By similarity
Metal binding791Zinc; structural By similarity
Metal binding821Zinc; structural By similarity
Metal binding1191Copper; catalytic By similarity

Amino acid modifications

Disulfide bond56 ↔ 145 By similarity

Sequences

Sequence LengthMass (Da)Tools
P24704 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 59E01FF9794F34BD

FASTA15215,098
        10         20         30         40         50         60 
MAKGVAVLNS SEGVTGTIFF TQEGDGVTTV SGTVSGLKPG LHGFHVHALG DTTNGCMSTG 

        70         80         90        100        110        120 
PHFNPDGKTH GAPEDANRHA GDLGNITVGD DGTATFTITD CQIPLTGPNS IVGRAVVVHA 

       130        140        150 
DPDDLGKGGH ELSLATGNAG GRVACGIIGL QG 

« Hide

References

« Hide 'large scale' references
[1]"cDNA and derived amino acid sequence of a cytosolic Cu,Zn superoxide dismutase from Arabidopsis thaliana (L.) Heyhn."
Hindges R., Slusarenko A.J.
Plant Mol. Biol. 18:123-125(1992) [PubMed: 1731963] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
Tissue: Leaf and Stem.
[2]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed: 11130712] [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: 14593172] [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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X60935 mRNA. Translation: CAA43270.1.
AC003981 Genomic DNA. Translation: AAF99769.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE28354.1.
CP002684 Genomic DNA. Translation: AEE28355.1.
AY091168 mRNA. Translation: AAM14107.1.
AY050932 mRNA. Translation: AAK93609.1.
AY087273 mRNA. Translation: AAM64826.1.
IPIIPI00545223.
PIRDSMUZ. S19117.
RefSeqNP_001077494.1. NM_001084025.1.
NP_172360.1. NM_100757.3.
UniGeneAt.25177.

3D structure databases

ProteinModelPortalP24704.
SMRP24704. Positions 1-152.
ModBaseSearch...

Protein-protein interaction databases

IntActP24704. 1 interaction.
STRINGP24704.

Proteomic databases

PRIDEP24704.
ProMEXP24704.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G08830.1; AT1G08830.1; AT1G08830.
AT1G08830.2; AT1G08830.2; AT1G08830.
GeneID837405.
GenomeReviewsGene locus AT1G08830 in contig CT485782_GR.
KEGGath:AT1G08830.
NMPDRfig|3702.1.peg.1097.

Organism-specific databases

TAIRAt1g08830.

Phylogenomic databases

GeneTreeEPGT00070000028650.
HOGENOMHBG609879.
InParanoidP24704.
OMATQEGDGP.
PhylomeDBP24704.
ProtClustDBPLN02386.

Enzyme and pathway databases

BioCycARA:AT1G08830-MONOMER.
MetaCyc:AT1G08830-MONOMER.

Gene expression databases

ArrayExpressP24704.
GenevestigatorP24704.
GermOnlineAT1G08830. Arabidopsis thaliana.

Family and domain databases

InterProIPR024134. SOD_Cu/Zn_/chaperones.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
Gene3DG3DSA:2.60.40.200. SOD_Cu_Zn. 1 hit.
KOK04565.
PANTHERPTHR10003. SOD_Cu_Zn. 1 hit.
PfamPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSPR00068. CUZNDISMTASE.
SUPFAMSSF49329. SOD_Cu_Zn. 1 hit.
PROSITEPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSODC_ARATH
AccessionPrimary (citable) accession number: P24704
Secondary accession number(s): Q9FRQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: December 14, 2011
This is version 106 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