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Protein

Superoxide dismutase [Cu-Zn]

Gene

SOD1

Organism
Cervus elaphus (Red deer)
Status
Reviewed-Annotation score: Annotation score: 4 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi45 – 451Copper; catalyticBy similarity
Metal bindingi47 – 471Copper; catalyticBy similarity
Metal bindingi62 – 621Copper; catalyticBy similarity
Metal bindingi62 – 621Zinc; structuralBy similarity
Metal bindingi70 – 701Zinc; structuralBy similarity
Metal bindingi79 – 791Zinc; structuralBy similarity
Metal bindingi82 – 821Zinc; structuralBy similarity
Metal bindingi119 – 1191Copper; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Cu-Zn] (EC:1.15.1.1)
Gene namesi
Name:SOD1
OrganismiCervus elaphus (Red deer)
Taxonomic identifieri9860 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraCervidaeCervinaeCervus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 152151Superoxide dismutase [Cu-Zn]PRO_0000164055Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei4 – 41N6-succinyllysineBy similarity
Lipidationi7 – 71S-palmitoyl cysteineBy similarity
Modified residuei10 – 101N6-succinyllysineBy similarity
Disulfide bondi56 ↔ 145By similarity
Modified residuei90 – 901N6-succinyllysineBy similarity
Modified residuei101 – 1011PhosphoserineBy similarity
Modified residuei104 – 1041PhosphoserineBy similarity
Modified residuei106 – 1061PhosphoserineBy similarity
Modified residuei121 – 1211N6-acetyllysine; alternateBy similarity
Modified residuei121 – 1211N6-succinyllysine; alternateBy similarity
Modified residuei135 – 1351N6-acetyllysine; alternateBy similarity
Modified residuei135 – 1351N6-succinyllysine; alternateBy similarity

Post-translational modificationi

Palmitoylation helps nuclear targeting and decreases catalytic activity.By similarity
Succinylation, adjacent to copper catalytic site probably inhibit activity. Desuccinylated by SIRT5, enhancing activity (By similarity).By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PRIDEiO46412.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO46412.
SMRiO46412. Positions 2-152.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Phylogenomic databases

HOVERGENiHBG000062.

Family and domain databases

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.

O46412-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATKAVCVLK GDGPVQGTIR FEAKGHTVVV TGSITGLTEG DHGFHVHQFG
60 70 80 90 100
DNTQGCTSAG PHFNPLSKKH GGPKDEERHV GDLGNVTADK NGVAKVDIVD
110 120 130 140 150
SLISLSGEHS IIGRTMVVHE KPDDLGRGGN EESTKTGNAR NRLACGVIGI

AQ
Length:152
Mass (Da):15,829
Last modified:January 23, 2007 - v3
Checksum:iBAC5F0E9D3EBFFFD
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91L → M in European red deer.
Natural varianti26 – 261H → N in European red deer.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U93268 mRNA. Translation: AAB88115.1.
U93269 mRNA. Translation: AAB88116.1.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U93268 mRNA. Translation: AAB88115.1.
U93269 mRNA. Translation: AAB88116.1.

3D structure databases

ProteinModelPortaliO46412.
SMRiO46412. Positions 2-152.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO46412.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG000062.

Family and domain databases

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...

Publicationsi

  1. "Characterization of the erythrocyte superoxide dismutase allozymes in the deer Cervus elaphus."
    He K., Wilton S.D., Tate M.L., Murphy M.P.
    Anim. Genet. 28:299-301(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: European red deer and North American wapiti.

Entry informationi

Entry nameiSODC_CEREL
AccessioniPrimary (citable) accession number: O46412
Secondary accession number(s): O46413
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 23, 2007
Last modified: December 9, 2015
This is version 94 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.