SODE_ONCVO
ID SODE_ONCVO Reviewed; 201 AA.
AC Q07449;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Extracellular superoxide dismutase [Cu-Zn];
DE Short=EC-SOD;
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=sod-4; Synonyms=sod2;
OS Onchocerca volvulus.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=6282;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8300230; DOI=10.1128/iai.62.2.713-716.1994;
RA James E.R., McLean D.C., Perler F.;
RT "Molecular cloning of an Onchocerca volvulus extracellular Cu-Zn superoxide
RT dismutase.";
RL Infect. Immun. 62:713-716(1994).
RN [2]
RP CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=9274879; DOI=10.1016/s0166-6851(97)00092-3;
RA Henkle-Duehrsen K., Tuan R.S., Wildenburg G., Eschbach M.-L., Tawe W.,
RA Zipfel P., Walter R.D.;
RT "Localization and functional analysis of the cytosolic and extracellular
RT CuZn superoxide dismutases in the human parasitic nematode Onchocerca
RT volvulus.";
RL Mol. Biochem. Parasitol. 88:187-202(1997).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems. May act in the
CC parasite defense against phagocyte-generated reactive oxygen species.
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 {ECO:0000269|PubMed:9274879}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L13778; AAA17049.1; -; mRNA.
DR PDB; 5IN2; X-ray; 1.55 A; A=44-201.
DR PDBsum; 5IN2; -.
DR AlphaFoldDB; Q07449; -.
DR SMR; Q07449; -.
DR STRING; 6282.Q07449; -.
DR HOGENOM; CLU_056632_4_2_1; -.
DR Proteomes; UP000024404; Unassembled WGS sequence.
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 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Copper; Disulfide bond; Metal-binding;
KW Oxidoreductase; Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..42
FT /evidence="ECO:0000255"
FT CHAIN 43..201
FT /note="Extracellular superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000032864"
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 DISULFID 100..192
FT /evidence="ECO:0000250"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:5IN2"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:5IN2"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:5IN2"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:5IN2"
FT STRAND 83..92
FT /evidence="ECO:0007829|PDB:5IN2"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:5IN2"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:5IN2"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:5IN2"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:5IN2"
FT STRAND 138..146
FT /evidence="ECO:0007829|PDB:5IN2"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:5IN2"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:5IN2"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:5IN2"
FT HELIX 177..183
FT /evidence="ECO:0007829|PDB:5IN2"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:5IN2"
SQ SEQUENCE 201 AA; 20904 MW; 97A9612247F85F80 CRC64;
MINSFIVIFL SFLIFINYAN LVCVEATHVY GRRSHSNGMH GNGARRAVAV LRGDAGVSGI
IYFQQGSGGS ITTISGSVSG LTPGLHGFHV HQYGDQTNGC TSAGDHYNPF GKTHGGPNDR
IKHIGDLGNI VAGANGVAEV YINSYDIKLR GPLSVIGHSL VVHANTDDLG QGTGNMREES
LKTGNAGSRL ACGVIGIAAV S
