SODC_PRIGL
ID SODC_PRIGL Reviewed; 152 AA.
AC P11418;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1;
GN Name=sod1;
OS Prionace glauca (Blue shark) (Squalus glaucus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Carcharhinidae;
OC Prionace.
OX NCBI_TaxID=7815;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=2500367; DOI=10.1016/0014-5793(89)80682-9;
RA Calabrese L., Polticelli F., O'Neill P., Galtieri A., Barra D.,
RA Schinina M.E., Bossa F.;
RT "Substitution of arginine for lysine 134 alters electrostatic parameters of
RT the active site in shark Cu,Zn superoxide dismutase.";
RL FEBS Lett. 250:49-52(1989).
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;
CC Note=Binds 1 copper ion per subunit.;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR PIR; S04623; S04623.
DR AlphaFoldDB; P11418; -.
DR SMR; P11418; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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 Antioxidant; Copper; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW Lipoprotein; Metal-binding; Nucleus; Oxidoreductase; Palmitate; Zinc.
FT CHAIN 1..152
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000164074"
FT BINDING 44
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT BINDING 46
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT BINDING 61
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT BINDING 118
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT LIPID 5
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT DISULFID 55..144
FT /evidence="ECO:0000250"
SQ SEQUENCE 152 AA; 15841 MW; 6617642A4F23C5AE CRC64;
MKAVCVLKGT GEVTGTVLFE QAADGPVTLK GSITGLTPGK HGFHVHAFGD NTNGCISAGP
HYNPFSKNHG GPDDEERHVG DLGNVEANGN GVAEFEIKDR QLHLSGERSI IGRTLVVHEK
EDDLGKGGDE ESLRTGNAGS RLACGVIGIA KD
