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Database: UniProt
Entry: H2MYT0_ORYLA
LinkDB: H2MYT0_ORYLA
Original site: H2MYT0_ORYLA 
ID   H2MYT0_ORYLA            Unreviewed;       211 AA.
AC   H2MYT0;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   10-APR-2019, entry version 39.
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:ENSORLP00000024188};
OS   Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae;
OC   Oryziinae; Oryzias.
OX   NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000024188, ECO:0000313|Proteomes:UP000001038};
RN   [1] {ECO:0000313|Ensembl:ENSORLP00000024188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000024188};
RX   PubMed=17554307; DOI=10.1038/nature05846;
RA   Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B.,
RA   Yamada T., Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D.,
RA   Shimada A., Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A.,
RA   Asakawa S., Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K.,
RA   Sugano S., Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F.,
RA   Nomoto H., Nogata K., Morishita T., Endo T., Shin-I T., Takeda H.,
RA   Morishita S., Kohara Y.;
RT   "The medaka draft genome and insights into vertebrate genome
RT   evolution.";
RL   Nature 447:714-719(2007).
RN   [2] {ECO:0000313|Ensembl:ENSORLP00000024188}
RP   IDENTIFICATION.
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000024188}, and HNI
RC   {ECO:0000313|Ensembl:ENSORLP00000024188};
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSORLP00000024188}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HNI {ECO:0000313|Ensembl:ENSORLP00000024188};
RA   Ichikawa K., Yoshimura J., Morishita S.;
RT   "CpG methylation of centromeres and impact of large insertions on
RT   vertebrate speciation.";
RL   Submitted (APR-2017) 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:
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   STRING; 8090.ENSORLP00000024188; -.
DR   Ensembl; ENSORLT00000024189; ENSORLP00000024188; ENSORLG00000019434.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   GeneTree; ENSGT00940000162224; -.
DR   InParanoid; H2MYT0; -.
DR   OMA; SQGCDST; -.
DR   TreeFam; TF105133; -.
DR   Proteomes; UP000001038; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR   GO; GO:0016532; F:superoxide dismutase copper chaperone activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
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:UP000001038};
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:UP000001038};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     26       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        27    211       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5017433079.
FT   DOMAIN       62    194       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   211 AA;  22930 MW;  35D40A7A0CA06402 CRC64;
     MSLHRSVRVL EMAFLVWLAC SQQCFSTHTD HLLPPEFSQY NGTLYAACKV SPSTSLPDDL
     PKVYGQALFK QDHGQGKLQV LLQLAGFPED ESPQSRAIHI HQYGDLSQGC ISTGGHYNPY
     GVDHPNHPGD FGNFVAHEGR ISEQIESEAT LFGGLSVLGR AVVVHETIDD LGQGGDVGSL
     LHGNAGRRLA CCVIGMSSSD LWEEQQKLQS S
//
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