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Reviewed, UniProtKB/Swiss-Prot O78310 (SODCP_ARATH)

Last modified November 3, 2009. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Superoxide dismutase [Cu-Zn], chloroplastic
    EC=1.15.1.1
Gene names
Name: SODCP
Synonyms: CSD2
Ordered Locus Names: At2g28190
ORF Names: F24D13.2
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length216 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

Homotetramer By similarity.

Subcellular location

Plastidchloroplast.

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6262Chloroplast
Chain63 – 216154Superoxide dismutase [Cu-Zn], chloroplastic
PRO_0000032844

Sites

Metal binding1081Copper; catalytic By similarity
Metal binding1101Copper; catalytic By similarity
Metal binding1251Copper; catalytic By similarity
Metal binding1251Zinc; structural By similarity
Metal binding1331Zinc; structural By similarity
Metal binding1421Zinc; structural By similarity
Metal binding1451Zinc; structural By similarity
Metal binding1821Copper; catalytic By similarity

Amino acid modifications

Disulfide bond119 ↔ 208 By similarity

Experimental info

Sequence conflict321R → S in AAD10208. Ref.1
Sequence conflict321R → S in AAM65492. Ref.5

Sequences

Sequence LengthMass (Da)Tools
O78310-1 [UniParc].

Last modified June 20, 2002. Version 2.
Checksum: 5F0E4333E1C1581C

FASTA21622,244
        10         20         30         40         50         60 
MAATNTILAF SSPSRLLIPP SSNPSTLRSS FRGVSLNNNN LHRLQSVSFA VKAPSKALTV 

        70         80         90        100        110        120 
VSAAKKAVAV LKGTSDVEGV VTLTQDDSGP TTVNVRITGL TPGPHGFHLH EFGDTTNGCI 

       130        140        150        160        170        180 
STGPHFNPNN MTHGAPEDEC RHAGDLGNIN ANADGVAETT IVDNQIPLTG PNSVVGRAFV 

       190        200        210 
VHELKDDLGK GGHELSLTTG NAGGRLACGV IGLTPL 

« 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: 9765550] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"Two genomic sequences encoding chloroplastic Cu/Zn superoxide dismutases from Arabidopsis thaliana ecotypes Ler and Cvi."
Abarca D., Martin M., Sabater B.
Plant Gene Register PGR99-089
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Landsberg erecta.
[3]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed: 10617197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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

AF061519 mRNA. Translation: AAD10208.1.
AJ238521 Genomic DNA. Translation: CAB51839.1.
AC005851 Genomic DNA. Translation: AAM15088.1.
AY064050 mRNA. Translation: AAL36406.1.
AY133756 mRNA. Translation: AAM91690.1.
AY087944 mRNA. Translation: AAM65492.1.
IPIIPI00520632.
PIRT51730.
RefSeqNP_565666.1.
UniGeneAt.20409

3D structure databases

HSSPHSSP built from PDB template 1SRD based on UniProtKB P07505.
SMRO78310. Positions 63-216.
ModBaseSearch...

Protein-protein interaction databases

STRINGO78310.

Proteomic databases

PRIDEO78310.
ProMEXO78310.

Genome annotation databases

GeneID817365.
GenomeReviewsGene locus AT2G28190 in contig CT485783_GR.
KEGGath:AT2G28190.

Organism-specific databases

TAIRAt2g28190.

Phylogenomic databases

OMAGPHFNPN.

Enzyme and pathway databases

BRENDA1.15.1.1. 302.

Gene expression databases

ArrayExpressO78310.
GenevestigatorO78310.
GermOnlineAT2G28190. Arabidopsis thaliana.

Family and domain databases

InterProIPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn.
[Graphical view]
Gene3DG3DSA:2.60.40.200. SOD_Cu_Zn. 1 hit.
PANTHERPTHR10003. SOD_Cu_Zn. 1 hit.
PfamPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSPR00068. CUZNDISMTASE.
ProDomPD000469. SOD_CU_ZN. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSODCP_ARATH
AccessionPrimary (citable) accession number: O78310
Secondary accession number(s): Q541D5, Q9SUJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: June 20, 2002
Last modified: November 3, 2009
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents