ID SODC_LAMCR Reviewed; 139 AA.
AC P81036;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1;
DE Flags: Fragment;
GN Name=sod1;
OS Lampanyctus crocodilus (Jewel lanternfish) (Gasteropelecus crocodilus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Myctophata;
OC Myctophiformes; Myctophidae; Lampanyctus.
OX NCBI_TaxID=71160;
RN [1]
RP PROTEIN SEQUENCE OF 2-139.
RX PubMed=9253177; DOI=10.1016/s0305-0491(97)00136-3;
RA Capo C., Stroppolo M.E., Galtieri A., Lania A., Costanzo S.,
RA Petruzzelli R., Calabrese L., Polticelli F., Desideri A.;
RT "Characterization of Cu,Zn superoxide dismutase from the bathophile fish,
RT Lampanyctus crocodilus.";
RL Comp. Biochem. Physiol. 117B:403-407(1997).
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 GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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.
PE 1: Evidence at protein level;
KW Antioxidant; Copper; Cytoplasm; Direct protein sequencing; Lipoprotein;
KW Metal-binding; Nucleus; Oxidoreductase; Palmitate; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9253177"
FT CHAIN 2..>139
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000164072"
FT REGION 118..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 47
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT BINDING 49
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT BINDING 72
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 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT BINDING 114
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT LIPID 6
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT NON_TER 139
SQ SEQUENCE 139 AA; 14580 MW; 6DB2F8153C2D1410 CRC64;
MVKAVCVLKG TTGEVTGTVY FEQESDSAPV KLTGQIIGLA PGLHGFHVHA FGDNTNXXXX
XXXXXXXXXX THAGPTDKDR HVGDLGNVAK IDITDKMLTL NGPLSIIGRT MVIHEKADDL
GKGGNDESLK TGNAGGRMA
//
