SODE_BRUPA
ID SODE_BRUPA Reviewed; 199 AA.
AC P41963;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Extracellular superoxide dismutase [Cu-Zn];
DE Short=EC-SOD;
DE EC=1.15.1.1;
DE Flags: Precursor;
OS Brugia pahangi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6280;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8112870; DOI=10.1128/iai.62.3.961-967.1994;
RA Tang L., Ou X., Henkle K.J., Selkirk M.E.;
RT "Extracellular and cytoplasmic CuZn superoxide dismutases from Brugia
RT lymphatic filarial nematode parasites.";
RL Infect. Immun. 62:961-967(1994).
CC -!- FUNCTION: Protect the extracellular space from toxic effect of reactive
CC oxygen intermediates by converting superoxide radicals into hydrogen
CC peroxide and oxygen. May act in the parasite defense by neutralizing
CC superoxide generated by activated leukocytes, thus acting as both an
CC antioxidant and an anti-inflammatory factor.
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 -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; X76283; CAA53901.1; -; mRNA.
DR AlphaFoldDB; P41963; -.
DR SMR; P41963; -.
DR STRING; 6280.P41963; -.
DR Proteomes; UP000038020; Genome Assembly.
DR GO; GO:0005615; C:extracellular space; 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 2: Evidence at transcript level;
KW Antioxidant; Copper; Disulfide bond; Glycoprotein; Metal-binding;
KW Oxidoreductase; Secreted; Signal; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..199
FT /note="Extracellular superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000032860"
FT BINDING 89
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 100..192
FT /evidence="ECO:0000250"
SQ SEQUENCE 199 AA; 21255 MW; 31CE6FD31E0F7537 CRC64;
MMIASFAIFL SHIIFITYAT SNQRYFKPNM HNNMTITIRR TITKTATAIA VLHSDNGNIN
GTIHFQQDKN STTISGEIKG LTPGLHGFHV HQYGDTTNGC ISAGPHFNPY NKTHGDPTDE
MRHVGDLGNI VAGADGTAHI DISDKHVQLL GPNSIIGRSL VVHADQDDLG KGVGDKKDES
LKTGNAGGRV ACGIVAISA
