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Database: UniProt
Entry: M3Z8T3_MUSPF
LinkDB: M3Z8T3_MUSPF
Original site: M3Z8T3_MUSPF 
ID   M3Z8T3_MUSPF            Unreviewed;       246 AA.
AC   M3Z8T3;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   10-APR-2019, entry version 38.
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:ENSMPUP00000019997};
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000019997, ECO:0000313|Proteomes:UP000000715};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000019997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ID#1420 {ECO:0000313|Ensembl:ENSMPUP00000019997};
RA   Di Palma F., Alfoldi J., Johnson J., Jaffe D., Berlin A., Gnerre S.,
RA   Grabherr M., Hall G., Lara M., MacCallum I., Mauceli E.,
RA   Przyblyski D., Ribeiro F., Russell P., Sharpe T., Turner-Maier J.,
RA   Walker B.J., Young S., Birren B., Lindblad-Toh K.;
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMPUP00000019997}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2013) 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.
CC       {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.
CC       {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; AEYP01056645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004762737.1; XM_004762680.2.
DR   STRING; 9668.ENSMPUP00000019997; -.
DR   PRIDE; M3Z8T3; -.
DR   Ensembl; ENSMPUT00000020283; ENSMPUP00000019997; ENSMPUG00000020131.
DR   GeneID; 101688889; -.
DR   CTD; 6649; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   GeneTree; ENSGT00940000162224; -.
DR   InParanoid; M3Z8T3; -.
DR   OMA; SQGCDST; -.
DR   Proteomes; UP000000715; Unassembled WGS sequence.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 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; PTHR10003; 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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000715};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    246       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004045998.
FT   DOMAIN       81    216       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   246 AA;  26278 MW;  08CF930FB6C1BF30 CRC64;
     MLAPLLLCAY LLLAAPASRA WPAVDPEEPG SSTAAQIRDM HEKVTAIWQE LTQRQAAADG
     QDAVLHATCR VEPSATLDTA QPRVSGLVLF RQLAPGARLE AYFDLEGFPA EANSSSRAIH
     VHQFGDLSQG CESTGAHYNP LAVPHPQHPG DFGNFAVRDG RLFKYRGNLA ASLAGPHSIV
     GRAVVVHAGE DDLGRGGNPA SVENGNAGRR LACCVVGLSG PLPWARLAQE HAERKKRRRE
     SECKTA
//
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