SODC2_OLEEU
ID SODC2_OLEEU Reviewed; 152 AA.
AC Q8L5E0; A9LNF9;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Superoxide dismutase [Cu-Zn] 2;
DE EC=1.15.1.1;
DE AltName: Full=Allergen Ole e V;
DE AltName: Allergen=Ole e 5;
GN Name=OLE5; Synonyms=O5;
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 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP ALLERGEN.
RC TISSUE=Pollen;
RX PubMed=15785077; DOI=10.1159/000084608;
RA Butteroni C., Afferni C., Barletta B., Iacovacci P., Corinti S.,
RA Brunetto B., Tinghino R., Ariano R., Panzani R.C., Pini C., Di Felice G.;
RT "Cloning and Expression of the Olea europaea allergen Ole e 5, the pollen
RT Cu/Zn superoxide dismutase.";
RL Int. Arch. Allergy Immunol. 137:9-17(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Soleimani A., Jimenez-Lopez J.C., Rodriguez-Garcia M.I., Alche J.D.;
RT "Isoforms of pollen allergens in two widespread olive cultivars from
RT Iran.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Leaf;
RA Zafra A., Jimenez-Lopez J.C., Rodriguez-Garcia M.I., Alche J.D.;
RT "CuZn-SOD polymorphism in olive pollen from different cultivars.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND ACTIVITY
RP REGULATION.
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 [5]
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 [6]
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 [7]
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|PubMed:15785077, ECO:0000269|Ref.4}.
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 Evidence={ECO:0000269|PubMed:15785077};
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.4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|Ref.4}. Endoplasmic
CC reticulum {ECO:0000269|Ref.4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8L5E0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8L5E0-2; Sequence=VSP_045094;
CC -!- TISSUE SPECIFICITY: Expressed in fruits, leaves and pollen grains.
CC {ECO:0000269|PubMed:16766574, ECO:0000269|PubMed:21995844,
CC ECO:0000269|Ref.4}.
CC -!- POLYMORPHISM: Several isoforms of the allergen exist due to
CC polymorphism. {ECO:0000305|PubMed:22385802}.
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:0000269|PubMed:15785077}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; AJ428575; CAD21706.2; -; mRNA.
DR EMBL; EF541380; ABP58626.1; -; mRNA.
DR EMBL; EF541382; ABP58628.1; -; mRNA.
DR EMBL; EF541383; ABP58629.1; -; mRNA.
DR EMBL; EF541384; ABP58630.1; -; mRNA.
DR EMBL; EF541385; ABP58631.1; -; mRNA.
DR EMBL; EU247080; ABX26133.1; -; Genomic_DNA.
DR EMBL; EU247082; ABX26135.1; -; Genomic_DNA.
DR EMBL; EU247083; ABX26136.1; -; Genomic_DNA.
DR EMBL; EU247084; ABX26137.1; -; Genomic_DNA.
DR EMBL; EU247089; ABX26142.1; -; Genomic_DNA.
DR EMBL; EU247091; ABX26144.1; -; Genomic_DNA.
DR EMBL; EU247093; ABX26146.1; -; Genomic_DNA.
DR EMBL; EU247095; ABX26148.1; -; Genomic_DNA.
DR EMBL; EU247096; ABX26149.1; -; Genomic_DNA.
DR EMBL; EU250757; ABX54839.1; -; mRNA.
DR EMBL; EU250758; ABX54840.1; -; mRNA.
DR EMBL; EU250759; ABX54841.1; -; mRNA.
DR EMBL; EU250761; ABX54843.1; -; mRNA.
DR EMBL; EU250764; ABX54846.1; -; mRNA.
DR EMBL; EU250765; ABX54847.1; -; mRNA.
DR EMBL; EU250766; ABX54848.1; -; mRNA.
DR EMBL; EU250768; ABX54850.1; -; mRNA.
DR EMBL; EU250769; ABX54851.1; -; mRNA.
DR EMBL; EU250770; ABX54852.1; -; mRNA.
DR EMBL; EU250771; ABX54853.1; -; mRNA.
DR EMBL; EU250774; ABX54856.1; -; mRNA.
DR EMBL; EU250775; ABX54857.1; -; mRNA.
DR EMBL; EU250776; ABX54858.1; -; mRNA.
DR EMBL; EU250778; ABX54860.1; -; mRNA.
DR EMBL; EU250779; ABX54861.1; -; mRNA.
DR EMBL; EU250781; ABX54863.1; -; mRNA.
DR EMBL; EU250783; ABX54865.1; -; mRNA.
DR EMBL; EU250785; ABX54867.1; -; mRNA.
DR EMBL; EU250786; ABX54868.1; -; mRNA.
DR EMBL; EU250788; ABX54870.1; -; mRNA.
DR EMBL; EU250789; ABX54871.1; -; mRNA.
DR EMBL; EU250790; ABX54872.1; -; mRNA.
DR EMBL; EU250791; ABX54873.1; -; mRNA.
DR EMBL; EU250793; ABX54875.1; -; mRNA.
DR EMBL; EU250797; ABX54879.1; -; mRNA.
DR AlphaFoldDB; Q8L5E0; -.
DR SMR; Q8L5E0; -.
DR Allergome; 493; Ole e 5.
DR EnsemblPlants; OE9A103554T1; OE9A103554C1; OE9A103554.
DR EnsemblPlants; Oeu044798.1; Oeu044798.1; Oeu044798.
DR Gramene; OE9A103554T1; OE9A103554C1; OE9A103554.
DR Gramene; Oeu044798.1; Oeu044798.1; Oeu044798.
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.
DR CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR Gene3D; 2.60.40.200; -; 1.
DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR InterPro; IPR018152; SOD_Cu/Zn_BS.
DR InterPro; IPR001424; SOD_Cu_Zn_dom.
DR PANTHER; PTHR10003; PTHR10003; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR PRINTS; PR00068; CUZNDISMTASE.
DR SUPFAM; SSF49329; SSF49329; 1.
DR PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE 1: Evidence at protein level;
KW Allergen; Alternative splicing; Antioxidant; Copper; Cytoplasm;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Metal-binding;
KW Oxidoreductase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..152
FT /note="Superoxide dismutase [Cu-Zn] 2"
FT /id="PRO_0000421080"
FT BINDING 45
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 56..145
FT /evidence="ECO:0000250"
FT VAR_SEQ 84..91
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_045094"
SQ SEQUENCE 152 AA; 15307 MW; 7DD474BCD86AC888 CRC64;
MVKAVTVLNS SEGVTGTVYF TQEGDGPTTV TGNLSGLKPG LHGFHVHALG DTTNGCMSTG
PHFNPVGKEH GAPGDENRHA GDLGNITVGE DGTAAINIVD KQIPLTGPHS IIGRAVVVHS
DPDDLGRGGH ELSKSTGNAG GRVACGIIGL QG
