Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Superoxide dismutase [Cu-Zn]

Gene

SOD1

Organism
Capra hircus (Goat)
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
OrganismiCapra hircus (Goat)
Taxonomic identifieri9925 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeCapra

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_0000164052Add
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 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

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ5FB29.
SMRiQ5FB29. Positions 2-151.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Phylogenomic databases

HOVERGENiHBG000062.
KOiK04565.
OrthoDBiEOG091G0OG2.

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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q5FB29-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATKAVCVLK GDGPVQGTIH FEAKGDKVVV TGSITGLTEG DHGFHVHQFG
60 70 80 90 100
DNTQGCTSAG PHFNPLSKKH GGPKDEERHV GDLGNVKADK NGVAIVDIVD
110 120 130 140 150
PLISLSGEYS IIGRTMVVHE KPDDLGRGGN EESTKTGNAG SCLACGVIGI

AP
Length:152
Mass (Da):15,653
Last modified:January 23, 2007 - v3
Checksum:iB0257980664C1CD2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB201469 mRNA. Translation: BAD89543.1.
RefSeqiNP_001272479.1. NM_001285550.1.
UniGeneiChi.235.

Genome annotation databases

GeneIDi100861196.
KEGGichx:100861196.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB201469 mRNA. Translation: BAD89543.1.
RefSeqiNP_001272479.1. NM_001285550.1.
UniGeneiChi.235.

3D structure databases

ProteinModelPortaliQ5FB29.
SMRiQ5FB29. Positions 2-151.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100861196.
KEGGichx:100861196.

Organism-specific databases

CTDi6647.

Phylogenomic databases

HOVERGENiHBG000062.
KOiK04565.
OrthoDBiEOG091G0OG2.

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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSODC_CAPHI
AccessioniPrimary (citable) accession number: Q5FB29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 69 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.