ID   SODC1_OLEEU             Reviewed;          30 AA.
AC   P80740;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] 1;
DE            EC=1.15.1.1;
DE   AltName: Full=Allergen Ole e V;
DE   AltName: Allergen=Ole e 5;
DE   Flags: Fragment;
OS   Olea europaea (Common olive).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Oleaceae; Oleeae; Olea.
OX   NCBI_TaxID=4146;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-30.
RC   TISSUE=Pollen;
RX   PubMed=9500754; DOI=10.1016/s0091-6749(98)70385-9;
RA   Boluda L., Alonso C., Fernandez-Caldas E.;
RT   "Purification, characterization, and partial sequencing of two new
RT   allergens of Olea europaea.";
RL   J. Allergy Clin. Immunol. 101:210-216(1998).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND TISSUE
RP   SPECIFICITY.
RA   Alche J.D., Corpas F.J., Rodriguez-Garcia M.I., del Rio L.A.;
RT   "Identification and immunolocalization of superoxide dismutase isoenzymes
RT   of olive pollen.";
RL   Physiol. Plantarum 104:772-776(1998).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=16766574; DOI=10.1093/pcp/pcj071;
RA   Corpas F.J., Fernandez-Ocana A., Carreras A., Valderrama R., Luque F.,
RA   Esteban F.J., Rodriguez-Serrano M., Chaki M., Pedrajas J.R., Sandalio L.M.,
RA   del Rio L.A., Barroso J.B.;
RT   "The expression of different superoxide dismutase forms is cell-type
RT   dependent in olive (Olea europaea L.) leaves.";
RL   Plant Cell Physiol. 47:984-994(2006).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX   PubMed=21995844; DOI=10.1021/jf203363q;
RA   Esteve C., Canas B., Moreno-Gordaliza E., Del Rio C., Garcia M.C.,
RA   Marina M.L.;
RT   "Identification of olive (Olea europaea) pulp proteins by matrix-assisted
RT   laser desorption/ionization time-of-flight mass spectrometry and nano-
RT   liquid chromatography tandem mass spectrometry.";
RL   J. Agric. Food Chem. 59:12093-12101(2011).
RN   [5]
RP   REVIEW, AND NOMENCLATURE.
RX   PubMed=22385802; DOI=10.1016/j.talanta.2012.01.016;
RA   Esteve C., Montealegre C., Marina M.L., Garcia M.C.;
RT   "Analysis of olive allergens.";
RL   Talanta 92:1-14(2012).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems. Probably involved in
CC       the protection against oxidative stress during pollen development.
CC       {ECO:0000269|Ref.2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Inhibited by KCN and H(2)O(2).
CC       {ECO:0000269|Ref.2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|Ref.2}. Endoplasmic
CC       reticulum {ECO:0000269|Ref.2}.
CC   -!- TISSUE SPECIFICITY: Expressed in fruits, leaves and pollen grains.
CC       {ECO:0000269|PubMed:16766574, ECO:0000269|PubMed:21995844,
CC       ECO:0000269|Ref.2}.
CC   -!- POLYMORPHISM: Several isoforms of the allergen exist due to
CC       polymorphism.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Allergen from olive
CC       pollen. Important in Mediterranean countries and California. Its
CC       prevalence is related to the geographic area.
CC       {ECO:0000305|PubMed:22385802}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P80740; -.
DR   SMR; P80740; -.
DR   Allergome; 3386; Ole e 5.0101.
DR   Allergome; 493; Ole e 5.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   Allergen; Antioxidant; Copper; Cytoplasm; Direct protein sequencing;
KW   Endoplasmic reticulum; Metal-binding; Oxidoreductase; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9500754"
FT   CHAIN           2..>30
FT                   /note="Superoxide dismutase [Cu-Zn] 1"
FT                   /id="PRO_0000164147"
FT   NON_TER         30
SQ   SEQUENCE   30 AA;  3104 MW;  836C7A193E930383 CRC64;
     MVKAVTVLNS SEGPHGIVYF AQEGDGPTTV