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Protein

Superoxide dismutase [Cu-Zn] 2, chloroplastic

Gene

CSD2

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

Functioni

Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Mediates tolerance to stress, including photo-oxidative stress.3 Publications

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Protein has several cofactor binding sites:
  • Cu cationBy similarityNote: Binds 1 copper ion per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi108 – 1081Copper; catalyticBy similarity
Metal bindingi110 – 1101Copper; catalyticBy similarity
Metal bindingi125 – 1251Copper; catalyticBy similarity
Metal bindingi125 – 1251Zinc; structuralBy similarity
Metal bindingi133 – 1331Zinc; structuralBy similarity
Metal bindingi142 – 1421Zinc; structuralBy similarity
Metal bindingi145 – 1451Zinc; structuralBy similarity
Metal bindingi182 – 1821Copper; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

  • cellular response to high light intensity Source: InterPro
  • cellular response to light intensity Source: UniProtKB
  • cellular response to oxidative stress Source: UniProtKB
  • cellular response to ozone Source: UniProtKB
  • cellular response to salt stress Source: UniProtKB
  • cellular response to sucrose stimulus Source: UniProtKB
  • cellular response to UV-B Source: UniProtKB
  • gene silencing by miRNA Source: UniProtKB
  • response to copper ion Source: TAIR
  • response to iron ion Source: TAIR
  • response to oxidative stress Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Cu-Zn] 2, chloroplastic (EC:1.15.1.1)
Alternative name(s):
Copper/zinc superoxide dismutase 2
Gene namesi
Name:CSD2
Synonyms:KD-SOD, SODCP
Ordered Locus Names:At2g28190
ORF Names:F24D13.2
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G28190.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: TAIR
  • chloroplast Source: UniProtKB
  • chloroplast stroma Source: TAIR
  • thylakoid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

Growth retardation (e.g. delayed flowering) and abnormal chloroplasts (e.g. less organized with fewer stacks). This phenotype is reversed under very low light conditions. Enhanced tolerance to oxidative stress.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6262ChloroplastAdd
BLAST
Chaini63 – 216154Superoxide dismutase [Cu-Zn] 2, chloroplasticPRO_0000032844Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi119 ↔ 208By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiO78310.
PRIDEiO78310.

PTM databases

iPTMnetiO78310.

Expressioni

Tissue specificityi

Expressed in leaves (at protein level). The spatial localization is regulated by miR398-mediated silencing. Mostly present in flowers, old rosette leaves and inflorescence, and, to a lower extent, in cauline leaves, stems and roots.2 Publications

Inductioni

Upon photosynthetically active radiation (PAR) (e.g. light fluence) increase and UV-B treatment. Accumulates in response to ozone fumigation, during recovery. Induced in response to oxidative stress, via a reduction of miR398-mediated silencing. Repressed by sucrose in a miR398-mediated silencing-dependent manner. Repressed by salt stress. Down-regulated by aconitase.4 Publications

Gene expression databases

GenevisibleiO78310. AT.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

BioGridi2715. 2 interactions.
IntActiO78310. 1 interaction.
STRINGi3702.AT2G28190.1.

Structurei

3D structure databases

ProteinModelPortaliO78310.
SMRiO78310. Positions 63-216.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0441. Eukaryota.
COG2032. LUCA.
HOGENOMiHOG000263447.
InParanoidiO78310.
KOiK04565.
OMAiDKAGMND.
OrthoDBiEOG09360OJH.
PhylomeDBiO78310.

Family and domain databases

CDDicd00305. Cu-Zn_Superoxide_Dismutase. 1 hit.
Gene3Di2.60.40.200. 1 hit.
InterProiIPR031074. CSD2_chloroplastic.
IPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 1 hit.
PTHR10003:SF34. PTHR10003:SF34. 1 hit.
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O78310-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATNTILAF SSPSRLLIPP SSNPSTLRSS FRGVSLNNNN LHRLQSVSFA
60 70 80 90 100
VKAPSKALTV VSAAKKAVAV LKGTSDVEGV VTLTQDDSGP TTVNVRITGL
110 120 130 140 150
TPGPHGFHLH EFGDTTNGCI STGPHFNPNN MTHGAPEDEC RHAGDLGNIN
160 170 180 190 200
ANADGVAETT IVDNQIPLTG PNSVVGRAFV VHELKDDLGK GGHELSLTTG
210
NAGGRLACGV IGLTPL
Length:216
Mass (Da):22,244
Last modified:June 20, 2002 - v2
Checksum:i5F0E4333E1C1581C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321R → S in AAD10208 (PubMed:9765550).Curated
Sequence conflicti32 – 321R → S in AAM65492 (Ref. 7) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231N → Y in strain: cv. Cvi-1; enhanced stability and better tolerance to photo-oxidative stress conditions; when associated with S-39, A-101 and K-164. 1 Publication
Natural varianti39 – 391N → S in strain: cv. Cvi-1; enhanced stability and better tolerance to photo-oxidative stress conditions; when associated with Y-23, A-101 and K-164. 1 Publication
Natural varianti101 – 1011T → A in strain: cv. Cvi-1; enhanced stability and better tolerance to photo-oxidative stress conditions; when associated with Y-23, S-39 and K-164. 1 Publication
Natural varianti164 – 1641N → K in strain: cv. Cvi-1; enhanced stability and better tolerance to photo-oxidative stress conditions; when associated with Y-23, S-39 and A-101. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061519 mRNA. Translation: AAD10208.1.
AJ238521 Genomic DNA. Translation: CAB51839.1.
AJ238522 Genomic DNA. Translation: CAB51840.1.
AC005851 Genomic DNA. Translation: AAM15088.1.
CP002685 Genomic DNA. Translation: AEC08089.1.
AY064050 mRNA. Translation: AAL36406.1.
AY133756 mRNA. Translation: AAM91690.1.
AK227096 mRNA. Translation: BAE99148.1.
AY087944 mRNA. Translation: AAM65492.1.
PIRiT51730.
RefSeqiNP_565666.1. NM_128379.3.
UniGeneiAt.20409.

Genome annotation databases

EnsemblPlantsiAT2G28190.1; AT2G28190.1; AT2G28190.
GeneIDi817365.
GrameneiAT2G28190.1; AT2G28190.1; AT2G28190.
KEGGiath:AT2G28190.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061519 mRNA. Translation: AAD10208.1.
AJ238521 Genomic DNA. Translation: CAB51839.1.
AJ238522 Genomic DNA. Translation: CAB51840.1.
AC005851 Genomic DNA. Translation: AAM15088.1.
CP002685 Genomic DNA. Translation: AEC08089.1.
AY064050 mRNA. Translation: AAL36406.1.
AY133756 mRNA. Translation: AAM91690.1.
AK227096 mRNA. Translation: BAE99148.1.
AY087944 mRNA. Translation: AAM65492.1.
PIRiT51730.
RefSeqiNP_565666.1. NM_128379.3.
UniGeneiAt.20409.

3D structure databases

ProteinModelPortaliO78310.
SMRiO78310. Positions 63-216.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi2715. 2 interactions.
IntActiO78310. 1 interaction.
STRINGi3702.AT2G28190.1.

PTM databases

iPTMnetiO78310.

Proteomic databases

PaxDbiO78310.
PRIDEiO78310.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G28190.1; AT2G28190.1; AT2G28190.
GeneIDi817365.
GrameneiAT2G28190.1; AT2G28190.1; AT2G28190.
KEGGiath:AT2G28190.

Organism-specific databases

TAIRiAT2G28190.

Phylogenomic databases

eggNOGiKOG0441. Eukaryota.
COG2032. LUCA.
HOGENOMiHOG000263447.
InParanoidiO78310.
KOiK04565.
OMAiDKAGMND.
OrthoDBiEOG09360OJH.
PhylomeDBiO78310.

Miscellaneous databases

PROiO78310.

Gene expression databases

GenevisibleiO78310. AT.

Family and domain databases

CDDicd00305. Cu-Zn_Superoxide_Dismutase. 1 hit.
Gene3Di2.60.40.200. 1 hit.
InterProiIPR031074. CSD2_chloroplastic.
IPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 1 hit.
PTHR10003:SF34. PTHR10003:SF34. 1 hit.
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSODC2_ARATH
AccessioniPrimary (citable) accession number: O78310
Secondary accession number(s): Q0WUQ0
, Q541D5, Q9SUJ7, Q9SUJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: June 20, 2002
Last modified: September 7, 2016
This is version 136 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

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.