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SODE_RAT
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   03-AUG-2022, entry version 162.
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   GlyGen; Q08420; 1 site.
DR   PaxDb; Q08420; -.
DR   Ensembl; ENSRNOT00000005155; ENSRNOP00000005155; ENSRNOG00000003869.
DR   GeneID; 25352; -.
DR   KEGG; rno:25352; -.
DR   CTD; 6649; -.
DR   RGD; 3733; Sod3.
DR   eggNOG; KOG0441; Eukaryota.
DR   GeneTree; ENSGT00940000162224; -.
DR   HOGENOM; CLU_056632_3_1_1; -.
DR   InParanoid; Q08420; -.
DR   OMA; MHAKITE; -.
DR   OrthoDB; 1574423at2759; -.
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 tissues.
DR   Genevisible; Q08420; RN.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:RGD.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
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; -; 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   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
 
 
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