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Protein

Superoxide dismutase [Cu-Zn] 2

Gene

SODCC.1

Organism
Zea mays (Maize)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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

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)DescriptionActionsGraphical viewLength
Metal bindingi44Copper; catalyticBy similarity1
Metal bindingi46Copper; catalyticBy similarity1
Metal bindingi61Copper; catalyticBy similarity1
Metal bindingi61Zinc; structuralBy similarity1
Metal bindingi69Zinc; structuralBy similarity1
Metal bindingi78Zinc; structuralBy similarity1
Metal bindingi81Zinc; structuralBy similarity1
Metal bindingi118Copper; catalyticBy similarity1

GO - Molecular functioni

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 (EC:1.15.1.1)
Gene namesi
Name:SODCC.1
Synonyms:SOD2
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogonodaeAndropogoneaeTripsacinaeZea
Proteomesi
  • UP000007305 Componenti: Unplaced

Organism-specific databases

MaizeGDBi47586.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001641412 – 151Superoxide dismutase [Cu-Zn] 2Add BLAST150

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi55 ↔ 144By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP11428.
PRIDEiP11428.

Expressioni

Gene expression databases

ExpressionAtlasiP11428. baseline and differential.
GenevisibleiP11428. ZM.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi4577.GRMZM2G025992_P01.

Structurei

3D structure databases

ProteinModelPortaliP11428.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Phylogenomic databases

eggNOGiKOG0441. Eukaryota.
COG2032. LUCA.
HOGENOMiHOG000263447.
KOiK04565.

Family and domain databases

CDDicd00305. Cu-Zn_Superoxide_Dismutase. 1 hit.
Gene3Di2.60.40.200. 1 hit.
InterProiIPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 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.

P11428-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKAVAVLAG TDVKGTIFFS QEGDGPTTVT GSISGLKPGL HGFHVHALGD
60 70 80 90 100
TTNGCMSTGP HFNPVGKEHG APEDEDRHAG DLGNVTAGED GVVNVNITDS
110 120 130 140 150
QIPLAGPHSI IGRAVVVHAD PDDLGKGGHE LSKSTGNAGG RVACGIIGLQ

G
Length:151
Mass (Da):15,104
Last modified:January 23, 2007 - v2
Checksum:i6B1E8C703B17D216
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15175 mRNA. Translation: AAA33511.1.
M54936 mRNA. Translation: AAA33510.1.
PIRiA29077.
RefSeqiNP_001105335.1. NM_001111865.1.
XP_008651856.1. XM_008653634.1.
UniGeneiZm.25.

Genome annotation databases

EnsemblPlantsiZm00001d022505_T003; Zm00001d022505_T003; Zm00001d022505.
Zm00001d022505_T005; Zm00001d022505_T005; Zm00001d022505.
Zm00001d022505_T006; Zm00001d022505_T006; Zm00001d022505.
Zm00001d022505_T007; Zm00001d022505_T007; Zm00001d022505.
Zm00001d022505_T010; Zm00001d022505_T010; Zm00001d022505.
GeneIDi542260.
GrameneiZm00001d022505_T003; Zm00001d022505_T003; Zm00001d022505.
Zm00001d022505_T005; Zm00001d022505_T005; Zm00001d022505.
Zm00001d022505_T006; Zm00001d022505_T006; Zm00001d022505.
Zm00001d022505_T007; Zm00001d022505_T007; Zm00001d022505.
Zm00001d022505_T010; Zm00001d022505_T010; Zm00001d022505.
KEGGizma:542260.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15175 mRNA. Translation: AAA33511.1.
M54936 mRNA. Translation: AAA33510.1.
PIRiA29077.
RefSeqiNP_001105335.1. NM_001111865.1.
XP_008651856.1. XM_008653634.1.
UniGeneiZm.25.

3D structure databases

ProteinModelPortaliP11428.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4577.GRMZM2G025992_P01.

Proteomic databases

PaxDbiP11428.
PRIDEiP11428.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiZm00001d022505_T003; Zm00001d022505_T003; Zm00001d022505.
Zm00001d022505_T005; Zm00001d022505_T005; Zm00001d022505.
Zm00001d022505_T006; Zm00001d022505_T006; Zm00001d022505.
Zm00001d022505_T007; Zm00001d022505_T007; Zm00001d022505.
Zm00001d022505_T010; Zm00001d022505_T010; Zm00001d022505.
GeneIDi542260.
GrameneiZm00001d022505_T003; Zm00001d022505_T003; Zm00001d022505.
Zm00001d022505_T005; Zm00001d022505_T005; Zm00001d022505.
Zm00001d022505_T006; Zm00001d022505_T006; Zm00001d022505.
Zm00001d022505_T007; Zm00001d022505_T007; Zm00001d022505.
Zm00001d022505_T010; Zm00001d022505_T010; Zm00001d022505.
KEGGizma:542260.

Organism-specific databases

MaizeGDBi47586.

Phylogenomic databases

eggNOGiKOG0441. Eukaryota.
COG2032. LUCA.
HOGENOMiHOG000263447.
KOiK04565.

Gene expression databases

ExpressionAtlasiP11428. baseline and differential.
GenevisibleiP11428. ZM.

Family and domain databases

CDDicd00305. Cu-Zn_Superoxide_Dismutase. 1 hit.
Gene3Di2.60.40.200. 1 hit.
InterProiIPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 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_MAIZE
AccessioniPrimary (citable) accession number: P11428
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 122 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. 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.