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Database: UniProt
Entry: H0ZGM0_TAEGU
LinkDB: H0ZGM0_TAEGU
Original site: H0ZGM0_TAEGU 
ID   H0ZGM0_TAEGU            Unreviewed;       172 AA.
AC   H0ZGM0;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   10-APR-2019, entry version 49.
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:ENSTGUP00000009732};
OS   Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea;
OC   Estrildidae; Estrildinae; Taeniopygia.
OX   NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000009732, ECO:0000313|Proteomes:UP000007754};
RN   [1] {ECO:0000313|Ensembl:ENSTGUP00000009732, ECO:0000313|Proteomes:UP000007754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20360741; DOI=10.1038/nature08819;
RA   Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA   Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA   Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA   Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C.,
RA   London S.E., Li Y., Lin Y.C., George J., Sweedler J., Southey B.,
RA   Gunaratne P., Watson M., Nam K., Backstrom N., Smeds L., Nabholz B.,
RA   Itoh Y., Whitney O., Pfenning A.R., Howard J., Volker M.,
RA   Skinner B.M., Griffin D.K., Ye L., McLaren W.M., Flicek P.,
RA   Quesada V., Velasco G., Lopez-Otin C., Puente X.S., Olender T.,
RA   Lancet D., Smit A.F., Hubley R., Konkel M.K., Walker J.A.,
RA   Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., Eichler E.E.,
RA   Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., Burt D.,
RA   Scharff C., Adam I., Richard H., Sultan M., Soldatov A., Lehrach H.,
RA   Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., Nelson J.,
RA   Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT   "The genome of a songbird.";
RL   Nature 464:757-762(2010).
RN   [2] {ECO:0000313|Ensembl:ENSTGUP00000009732}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2012) 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; ABQF01015360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSTGUT00000009838; ENSTGUP00000009732; ENSTGUG00000009451.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   GeneTree; ENSGT00940000162224; -.
DR   InParanoid; H0ZGM0; -.
DR   OMA; SQGCDST; -.
DR   TreeFam; TF105133; -.
DR   Reactome; R-TGU-3299685; Detoxification of Reactive Oxygen Species.
DR   Proteomes; UP000007754; Chromosome 4.
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:UP000007754};
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:UP000007754};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       16    151       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   172 AA;  19295 MW;  6687FA5DCC972883 CRC64;
     YATCEMKPSS KIDADKPQVT GQVLFRQSYS YGRLEALFYL DGFPLDNNQS SRAIHIHELG
     DLSNGCDSTG GHYNPFRVNH PRHPGDFGNF LPKEGKIRKY KTNLFATIFG PYSIMGRSVV
     IHEQEDDMGK GNNKASLENG NAGKRLACCV IGISNKNLWE EKLPEVTDKK KR
//
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