ID SODE_RAT Reviewed; 244 AA.
AC Q08420; Q64667;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 27-MAR-2024, entry version 171.
DE RecName: Full=Extracellular superoxide dismutase [Cu-Zn];
DE Short=EC-SOD;
DE EC=1.15.1.1 {ECO:0000269|PubMed:8227019};
DE AltName: Full=Superoxide dismutase B;
DE Flags: Precursor;
GN Name=Sod3; Synonyms=Sod-3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Epididymis;
RX PubMed=8328962; DOI=10.1042/bj2930021;
RA Perry A.C.F., Jones R., Hall L.;
RT "Isolation and characterization of a rat cDNA clone encoding a secreted
RT superoxide dismutase reveals the epididymis to be a major site of its
RT expression.";
RL Biochem. J. 293:21-25(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX PubMed=8227019; DOI=10.1016/s0021-9258(19)74510-4;
RA Willems J., Zwijsen A., Slegers H., Nicolai S., Bettadapura J.,
RA Raymackers J., Scarcez T.;
RT "Purification and sequence of rat extracellular superoxide dismutase B
RT secreted by C6 glioma.";
RL J. Biol. Chem. 268:24614-24621(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS, AND CATALYTIC ACTIVITY.
RC STRAIN=Sprague-Dawley; TISSUE=Uterus;
RX PubMed=8643556; DOI=10.1073/pnas.93.11.5219;
RA Carlsson L.M., Marklund S.M., Edlund T.;
RT "The rat extracellular superoxide dismutase dimer is converted to a
RT tetramer by the exchange of a single amino acid.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:5219-5222(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 Evidence={ECO:0000269|PubMed:8227019};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20697;
CC Evidence={ECO:0000305|PubMed:8227019};
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 (PubMed:8643556). Interacts with ATP7A; this
CC interaction is copper-dependent and is required for SOD3 activity.
CC {ECO:0000250|UniProtKB:P08294, ECO:0000269|PubMed:8643556}.
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; X68041; CAA48177.1; -; mRNA.
DR EMBL; Z24721; CAA80849.1; -; mRNA.
DR EMBL; X94371; CAA64149.1; -; mRNA.
DR EMBL; BC061861; AAH61861.1; -; mRNA.
DR PIR; A49097; A49097.
DR RefSeq; NP_037012.1; NM_012880.1.
DR AlphaFoldDB; Q08420; -.
DR SMR; Q08420; -.
DR STRING; 10116.ENSRNOP00000005155; -.
DR GlyCosmos; Q08420; 1 site, No reported glycans.
DR GlyGen; Q08420; 1 site.
DR PhosphoSitePlus; Q08420; -.
DR PaxDb; 10116-ENSRNOP00000005155; -.
DR Ensembl; ENSRNOT00000005155.4; ENSRNOP00000005155.2; ENSRNOG00000003869.4.
DR Ensembl; ENSRNOT00055019165; ENSRNOP00055015440; ENSRNOG00055011318.
DR Ensembl; ENSRNOT00060027730; ENSRNOP00060022286; ENSRNOG00060016186.
DR Ensembl; ENSRNOT00065004598; ENSRNOP00065003297; ENSRNOG00065003240.
DR GeneID; 25352; -.
DR KEGG; rno:25352; -.
DR AGR; RGD:3733; -.
DR RGD; 3733; Sod3.
DR eggNOG; KOG0441; Eukaryota.
DR GeneTree; ENSGT00940000162224; -.
DR HOGENOM; CLU_056632_3_1_1; -.
DR InParanoid; Q08420; -.
DR OMA; DGSLWKY; -.
DR OrthoDB; 3470597at2759; -.
DR PhylomeDB; Q08420; -.
DR TreeFam; TF105133; -.
DR Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
DR PRO; PR:Q08420; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000003869; Expressed in adult mammalian kidney and 19 other cell types or tissues.
DR Genevisible; Q08420; RN.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; ISO:RGD.
DR GO; GO:0004784; F:superoxide dismutase activity; IDA:RGD.
DR GO; GO:0097746; P:blood vessel diameter maintenance; IMP:RGD.
DR GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
DR GO; GO:0046688; P:response to copper ion; IMP:RGD.
DR GO; GO:0001666; P:response to hypoxia; ISO:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IEP:RGD.
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:SF77; EXTRACELLULAR 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.
DR PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE 1: Evidence at protein level;
KW Antioxidant; Copper; Disulfide bond; Glycoprotein; Golgi apparatus;
KW Metal-binding; Oxidoreductase; Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..244
FT /note="Extracellular superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000032859"
FT REGION 224..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 121
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 138
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 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 70..215
FT /evidence="ECO:0000250"
FT DISULFID 132..214
FT /evidence="ECO:0000250"
FT MUTAGEN 48
FT /note="D->V: Homotetramerization."
FT /evidence="ECO:0000269|PubMed:8643556"
FT CONFLICT 235..237
FT /note="RRR -> WRW (in Ref. 1; CAA48177)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 244 AA; 26620 MW; B66726301CE5B614 CRC64;
MVAFLFCNLL LVACGSVTWT MSDTGESGVD LADRLDLVEK IGDTHSKDLE IWMELGKQRE
ADAREMHAVC RVQPSAMLPP DQPQITGLVL FRQLGPSSRL EASFNLEGFP AEQNTSNHAI
HVHEFGDLSQ GCESTGPHYN PLGVPHPQHP GDFGNFVVRD GRLWKHRMGL ATSLAGPHSI
LGRAVVVHAG EDDLGKGGNQ ASVQNGNAGR RLACCVVGTS NSEAWESQTK ERKKRRRESE
CKTT
//
