ID A0A3Q7RFG4_VULVU Unreviewed; 153 AA.
AC A0A3Q7RFG4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|ARBA:ARBA00020928, ECO:0000256|RuleBase:RU000393};
DE EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000393};
GN Name=SOD1 {ECO:0000313|RefSeq:XP_025840916.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025840916.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025840916.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025840916.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025840916.1};
RG RefSeq;
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|ARBA:ARBA00003917, 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 -!- SUBUNIT: Homodimer; non-disulfide-linked (By similarity). Heterodimer
CC with SOD1. The heterodimer CCS:SOD1 interacts with SLC31A1; this
CC heterotrimer is Cu(1+)-mediated and its maintenance is regulated
CC through SOD1 activation. {ECO:0000256|ARBA:ARBA00035019}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000256|ARBA:ARBA00010457, ECO:0000256|RuleBase:RU000393}.
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DR RefSeq; XP_025840916.1; XM_025985131.1.
DR AlphaFoldDB; A0A3Q7RFG4; -.
DR STRING; 9627.ENSVVUP00000003777; -.
DR KEGG; vvp:112909262; -.
DR OrthoDB; 3470597at2759; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0005634; C:nucleus; 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: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.
DR PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|RuleBase:RU000393};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023139};
KW Metal-binding {ECO:0000256|RuleBase:RU000393};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW Zinc {ECO:0000256|RuleBase:RU000393}.
FT DOMAIN 15..149
FT /note="Superoxide dismutase copper/zinc binding"
FT /evidence="ECO:0000259|Pfam:PF00080"
SQ SEQUENCE 153 AA; 15844 MW; DF076BE323295AAE CRC64;
MEMKAVCVLK GQGPVEGTIH FVQKGSGPVV VSGTITGLTE GEHGFHVHQF GDNTQGCTSA
GPHFNPLSKK HGGPKDQERH VGDLGNVTAG KDGVAIVSIE DSLIALSGDY SIIGRTMVVH
EKRDDLGKGD NEESTQTGNA GSRLACGVIG IAK
//
