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Protein

Superoxide dismutase [Cu-Zn] 1

Gene
N/A
Organism
Olea europaea (Common olive)
Status
Reviewed-Annotation score: Annotation score: 4 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. Probably involved in the protection against oxidative stress during pollen development.1 Publication

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

Enzyme regulationi

Inhibited by KCN and H2O2.1 Publication

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] 1 (EC:1.15.1.1)
Alternative name(s):
Allergen Ole e V
Allergen: Ole e 5
OrganismiOlea europaea (Common olive)
Taxonomic identifieri4146 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsLamialesOleaceaeOleeaeOlea

Subcellular locationi

  • Cytoplasm 1 Publication
  • Endoplasmic reticulum 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human. Allergen from olive pollen. Important in Mediterranean countries and California. Its prevalence is related to the geographic area.1 Publication

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei3386. Ole e 5.0101.
493. Ole e 5.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – ›30›29Superoxide dismutase [Cu-Zn] 1PRO_0000164147Add
BLAST

Expressioni

Tissue specificityi

Expressed in fruits, leaves and pollen grains.3 Publications

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Sequencei

Sequence statusi: Fragment.

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

P80740-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30
MVKAVTVLNS SEGPHGIVYF AQEGDGPTTV
Length:30
Mass (Da):3,104
Last modified:January 23, 2007 - v2
Checksum:i836C7A193E930383
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei30 – 301

Polymorphismi

Several isoforms of the allergen exist due to polymorphism.

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei3386. Ole e 5.0101.
493. Ole e 5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "Purification, characterization, and partial sequencing of two new allergens of Olea europaea."
    Boluda L., Alonso C., Fernandez-Caldas E.
    J. Allergy Clin. Immunol. 101:210-216(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-30.
    Tissue: Pollen.
  2. "Identification and immunolocalization of superoxide dismutase isoenzymes of olive pollen."
    Alche J.D., Corpas F.J., Rodriguez-Garcia M.I., del Rio L.A.
    Physiol. Plantarum 104:772-776(1998)
    Cited for: FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, TISSUE SPECIFICITY.
  3. "The expression of different superoxide dismutase forms is cell-type dependent in olive (Olea europaea L.) leaves."
    Corpas F.J., Fernandez-Ocana A., Carreras A., Valderrama R., Luque F., Esteban F.J., Rodriguez-Serrano M., Chaki M., Pedrajas J.R., Sandalio L.M., del Rio L.A., Barroso J.B.
    Plant Cell Physiol. 47:984-994(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  4. "Identification of olive (Olea europaea) pulp proteins by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and nano-liquid chromatography tandem mass spectrometry."
    Esteve C., Canas B., Moreno-Gordaliza E., Del Rio C., Garcia M.C., Marina M.L.
    J. Agric. Food Chem. 59:12093-12101(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
  5. Cited for: REVIEW, NOMENCLATURE.

Entry informationi

Entry nameiALL5A_OLEEU
AccessioniPrimary (citable) accession number: P80740
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: January 20, 2016
This is version 65 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

Direct protein sequencing

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  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.