SODE_RABIT
ID SODE_RABIT Reviewed; 244 AA.
AC P41975;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Extracellular superoxide dismutase [Cu-Zn];
DE Short=EC-SOD;
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=SOD3;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=New Zealand white;
RA Laukkanen M.O., Aittomaki S.J., Hiltunen T.P., Yla-Herttuala S.;
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=New Zealand white; TISSUE=Heart;
RA Laukkanen M.O., Hiltunen M.O., Aittomaki S., Janne J., Yla-Herttuala S.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE.
RA Laukkanen M.O., Aittomaeki S., Mannermaa S., Hiltunen M.O.,
RA Yla-Herttuala S.;
RT "Cloning and characterization of rabbit extracellular superoxide
RT dismutase.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE OF 43-155.
RC STRAIN=New Zealand white; TISSUE=Aorta;
RA Hiltunen T.P., Nikkari T., Yla-Herttuala S.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protect the extracellular space from toxic effect of reactive
CC oxygen intermediates by converting superoxide radicals into hydrogen
CC peroxide and oxygen. {ECO:0000250}.
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: Homotetramer. Directly interacts with ATP7A; this interaction
CC is copper-dependent and is required for SOD3 activity.
CC {ECO:0000250|UniProtKB:P08294}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. Golgi apparatus,
CC trans-Golgi network {ECO:0000250|UniProtKB:O09164}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; Z67878; CAA91785.1; -; mRNA.
DR EMBL; Y13339; CAA73783.1; -; Genomic_DNA.
DR EMBL; AJ007044; CAA07431.1; -; Genomic_DNA.
DR EMBL; X78139; CAA55018.1; -; mRNA.
DR RefSeq; NP_001076101.1; NM_001082632.1.
DR AlphaFoldDB; P41975; -.
DR SMR; P41975; -.
DR STRING; 9986.ENSOCUP00000006450; -.
DR PRIDE; P41975; -.
DR GeneID; 100009320; -.
DR KEGG; ocu:100009320; -.
DR CTD; 6649; -.
DR eggNOG; KOG0441; Eukaryota.
DR HOGENOM; CLU_056632_3_1_1; -.
DR InParanoid; P41975; -.
DR OMA; MHAKITE; -.
DR OrthoDB; 1574423at2759; -.
DR TreeFam; TF105133; -.
DR BRENDA; 1.15.1.1; 1749.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; 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; -; 1.
DR InterPro; IPR024141; EC-SOD.
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 PANTHER; PTHR10003:SF77; PTHR10003:SF77; 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; Golgi apparatus;
KW Metal-binding; Oxidoreductase; Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..244
FT /note="Extracellular superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000032858"
FT REGION 221..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 118
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 67..212
FT /evidence="ECO:0000250"
FT DISULFID 129..211
FT /evidence="ECO:0000250"
FT CONFLICT 53
FT /note="R -> W (in Ref. 4; CAA55018)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 244 AA; 25688 MW; 7C9B1C59F942F2C5 CRC64;
MLALVCSCLL LAALPADTWS GPAAVELGSD TVEQIRDTHA KVTEIWQALT QQRAAQGEPA
GALHAVCRVQ PSATLDAAQP RVSGLVVFRQ LGPGAQLEAF FDLEGFPVEA NLSSRAIHVH
QFGDLSQGCD STGAHYNPLA VQHPQHPGDF GNFAVRDGRL WKYRSGLAAS LAGPHSIVGR
AVVVHAGEDD LGRGGNAASV ENGNAGPRLA CCVVGASGPA PWARQAQEHA ERKKRRRESE
CKAA
