ID J3JYL1_DENPD Unreviewed; 153 AA.
AC J3JYL1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN Name=109538429 {ECO:0000313|EnsemblMetazoa:ENN76399};
GN ORFNames=D910_11395 {ECO:0000313|EMBL:ERL94113.1}, YQE_07060
GN {ECO:0000313|EMBL:ENN76399.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:AEE63298.1};
RN [1] {ECO:0000313|EMBL:AEE63298.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Midgut and adhering fatbody of emerged adults of both sexes
RC after feeding on lodgepole pine for up to 64 h
RC {ECO:0000313|EMBL:AEE63298.1};
RX PubMed=22516182; DOI=10.1016/j.ibmb.2012.03.010;
RA Keeling C.I., Henderson H., Li M., Yuen M., Clark E.L., Fraser J.D.,
RA Huber D.P., Liao N.Y., Roderick Docking T., Birol I., Chan S.K.,
RA Taylor G.A., Palmquist D., Jones S.J., Bohlmann J.;
RT "Transcriptome and full-length cDNA resources for the mountain pine beetle,
RT Dendroctonus ponderosae Hopkins, a major insect pest of pine forests.";
RL Insect Biochem. Mol. Biol. 42:525-536(2012).
RN [2] {ECO:0000313|Proteomes:UP000019118, ECO:0000313|Proteomes:UP000030742}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:ENN76399}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JAN-2017) to UniProtKB.
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
CC {ECO:0000256|RuleBase:RU000393}.
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:0000256|ARBA:ARBA00001605,
CC ECO:0000256|RuleBase:RU000393};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|RuleBase:RU000393};
CC Note=Binds 1 copper ion per subunit. {ECO:0000256|RuleBase:RU000393};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU000393};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU000393};
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000256|RuleBase:RU000393}.
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DR EMBL; APGK01040371; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BT128340; AEE63298.1; -; mRNA.
DR EMBL; KB740979; ENN76399.1; -; Genomic_DNA.
DR EMBL; KB632379; ERL94113.1; -; Genomic_DNA.
DR RefSeq; XP_019761213.1; XM_019905654.1.
DR AlphaFoldDB; J3JYL1; -.
DR SMR; J3JYL1; -.
DR STRING; 77166.J3JYL1; -.
DR EnsemblMetazoa; ENN76399; ENN76399; YQE_07060.
DR GeneID; 109538429; -.
DR KEGG; dpa:109538429; -.
DR HOGENOM; CLU_056632_4_1_1; -.
DR OMA; AQRGFHI; -.
DR OrthoDB; 3470597at2759; -.
DR Proteomes; UP000019118; Unassembled WGS sequence.
DR Proteomes; UP000030742; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
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; Superoxide dismutase, copper/zinc binding domain; 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:SF103; SUPEROXIDE DISMUTASE [CU-ZN]; 1.
DR PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR PRINTS; PR00068; CUZNDISMTASE.
DR SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE 2: Evidence at transcript level;
KW Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW Copper {ECO:0000256|RuleBase:RU000393};
KW Metal-binding {ECO:0000256|RuleBase:RU000393};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000393};
KW Reference proteome {ECO:0000313|Proteomes:UP000030742};
KW Zinc {ECO:0000256|RuleBase:RU000393}.
FT DOMAIN 13..147
FT /note="Superoxide dismutase copper/zinc binding"
FT /evidence="ECO:0000259|Pfam:PF00080"
SQ SEQUENCE 153 AA; 15681 MW; EE947131E0726370 CRC64;
MVKAVAVLKS EVVNGTVFFS QEGNNPVQVN GSLSGLKEGL HGFHIHEFGD NTNGCISAGP
HFNPNDKEHG GPTDADRHAG DLGNIEANAE GVAKINITDK QISLSGANSI IGRTVVVHAD
PDDLGKGGHE LSKTTGNAGG RLACAVIGLA QPN
//
