ID W5NQP5_SHEEP Unreviewed; 244 AA.
AC W5NQP5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN Name=SOD3 {ECO:0000313|Ensembl:ENSOARP00000000485.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000000485.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000000485.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000000485.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000000485.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
CC {ECO:0000256|RuleBase:RU000393}.
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:0000256|RuleBase:RU000393};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|RuleBase:RU000393};
CC Note=Binds 1 copper ion per subunit. {ECO:0000256|RuleBase:RU000393};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU000393};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU000393};
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000256|RuleBase:RU000393}.
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DR EMBL; AMGL01097470; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012035137.1; XM_012179747.2.
DR RefSeq; XP_012035138.1; XM_012179748.2.
DR RefSeq; XP_012035139.1; XM_012179749.2.
DR RefSeq; XP_012035141.1; XM_012179751.1.
DR RefSeq; XP_012035143.1; XM_012179753.1.
DR RefSeq; XP_014951906.1; XM_015096420.1.
DR RefSeq; XP_014951907.1; XM_015096421.1.
DR RefSeq; XP_014951908.1; XM_015096422.1.
DR RefSeq; XP_014951909.1; XM_015096423.1.
DR RefSeq; XP_014951911.1; XM_015096425.1.
DR AlphaFoldDB; W5NQP5; -.
DR SMR; W5NQP5; -.
DR STRING; 9940.ENSOARP00000000485; -.
DR PaxDb; 9940-ENSOARP00000000485; -.
DR Ensembl; ENSOART00000000513.1; ENSOARP00000000485.1; ENSOARG00000000485.1.
DR eggNOG; KOG0441; Eukaryota.
DR HOGENOM; CLU_056632_3_1_1; -.
DR OMA; DGSLWKY; -.
DR OrthoDB; 3470597at2759; -.
DR Proteomes; UP000002356; Chromosome 6.
DR Bgee; ENSOARG00000000485; Expressed in adrenal cortex and 50 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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: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 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Copper {ECO:0000256|RuleBase:RU000393};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|RuleBase:RU000393};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|RuleBase:RU000393}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..244
FT /note="Superoxide dismutase [Cu-Zn]"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004869684"
FT DOMAIN 82..214
FT /note="Superoxide dismutase copper/zinc binding"
FT /evidence="ECO:0000259|Pfam:PF00080"
SQ SEQUENCE 244 AA; 26452 MW; ABA184F2D4049664 CRC64;
MPALLCASLL LVACAWAASA DQVQQQMGSN TEEQIRDMHA KVTEIWQEMM QRQAAAIDPD
AALHAVCRVL PSATLEAEQP RVSGLVLFRQ LPHLSLLEAF FHLEGFPNEP NGTSRAIHVH
QFGDLSQGCD STGPHYNPMS VLHPQHPGDF GNFAVRDGQV WKYRSNLAAS LTGPHSIAGR
AVVVHAGEDD LGRGGNQASL ENGNAGRRLA CCVVGLCGPG PWAHQAQENA ERKKRRRESE
CKAV
//
