SODE_SCHMA
ID SODE_SCHMA Reviewed; 184 AA.
AC P16026;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Extracellular superoxide dismutase [Cu-Zn];
DE Short=EC-SOD;
DE EC=1.15.1.1;
DE Flags: Precursor;
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=3169203; DOI=10.1016/0014-4894(88)90010-0;
RA Simurda M.C., van Kuelen H., Rekosh D.M., Loverde P.T.;
RT "Schistosoma mansoni: identification and analysis of an mRNA and a gene
RT encoding superoxide dismutase (Cu/Zn).";
RL Exp. Parasitol. 67:73-84(1988).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
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; M27529; AAA29937.1; -; mRNA.
DR EMBL; M28545; AAA29934.1; -; Genomic_DNA.
DR EMBL; M28543; AAA29934.1; JOINED; Genomic_DNA.
DR EMBL; M28544; AAA29934.1; JOINED; Genomic_DNA.
DR PIR; A37019; A37019.
DR RefSeq; XP_018647047.1; XM_018794575.1.
DR AlphaFoldDB; P16026; -.
DR SMR; P16026; -.
DR STRING; 6183.Smp_095980.1; -.
DR EnsemblMetazoa; Smp_095980.1; Smp_095980.1; Smp_095980.
DR GeneID; 8341691; -.
DR KEGG; smm:Smp_095980; -.
DR WBParaSite; Smp_095980.1; Smp_095980.1; Smp_095980.
DR CTD; 8341691; -.
DR eggNOG; KOG0441; Eukaryota.
DR HOGENOM; CLU_056632_4_2_1; -.
DR OMA; CGIILET; -.
DR OrthoDB; 1574423at2759; -.
DR PhylomeDB; P16026; -.
DR Proteomes; UP000008854; 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 2: Evidence at transcript level;
KW Antioxidant; Copper; Disulfide bond; Glycoprotein; Metal-binding;
KW Oxidoreductase; Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..18
FT CHAIN 19..184
FT /note="Extracellular superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000032865"
FT BINDING 76
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 87..176
FT /evidence="ECO:0000250"
SQ SEQUENCE 184 AA; 20346 MW; C14FD37026FA88B3 CRC64;
MTVYSYLVIL FILLDNYCSA YGYGYSYYHR RHFDPAIASF TKEPYIGAVW FTQHGDYMYV
NGSVAGLPPG KLLGTHVHRY GGLGNMCLEA GPHFNPFNQR HGPRHGYPRH AGDLGNIRVG
RGGVAKFDFY VTIKGLGPFD GFIGRALVIH ANRDDLGRNR DEGSRTTGNS GPRLACATIG
FRAP
