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Database: UniProt/TrEMBL
Entry: Q6SCL6_MUSDO
LinkDB: Q6SCL6_MUSDO
Original site: Q6SCL6_MUSDO 
ID   Q6SCL6_MUSDO            Unreviewed;       153 AA.
AC   Q6SCL6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   25-OCT-2017, entry version 71.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
OS   Musca domestica (House fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Muscoidea; Muscidae; Musca.
OX   NCBI_TaxID=7370 {ECO:0000313|EMBL:AAR23787.1};
RN   [1] {ECO:0000313|EMBL:AAR23787.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Du R., Geng H., An C., Hao Y.;
RT   "Molecular cloning and expression analysis of SOD from Musca
RT   domestica.";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFP59329.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ALHF {ECO:0000313|EMBL:AFP59329.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:AFP59329.1};
RA   Liu N., Zhang L., Li M., Reid W.;
RT   "Transcriptome of adult Musca domestica launches a platform for
RT   comparative house fly gene expression and characterization of
RT   differential gene expression among resistant and susceptible house
RT   flies.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {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; AY460107; AAR23787.1; -; mRNA.
DR   EMBL; KA644700; AFP59329.1; -; mRNA.
DR   RefSeq; NP_001295981.1; NM_001309052.1.
DR   ProteinModelPortal; Q6SCL6; -.
DR   SMR; Q6SCL6; -.
DR   GeneID; 101890504; -.
DR   KEGG; mde:101890504; -.
DR   CTD; 692639; -.
DR   KO; K04565; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; -; 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   2: Evidence at transcript level;
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       11    148       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   153 AA;  15583 MW;  D06D9ACEA3A096C1 CRC64;
     MPAKAVCVIN GDAKGTVFFE QTDESSPVVV TGEVTGLSKG LHGFHVHEFG DNTNGCTSAG
     PHFNPKGKEH GAPSDENRHV GDLGNIEASG DGPTKVNITD SQISLFGANS ILGRTVVVHA
     DPDDLGKGGH ELSKSTGNAG ARIGCGVIGI AKI
//
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