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Database: UniProt
Entry: A0A1L8HCL3_XENLA
LinkDB: A0A1L8HCL3_XENLA
Original site: A0A1L8HCL3_XENLA 
ID   A0A1L8HCL3_XENLA        Unreviewed;       151 AA.
AC   A0A1L8HCL3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   16-JAN-2019, entry version 11.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=sod1 {ECO:0000313|Xenbase:XB-GENE-6254670};
GN   ORFNames=XELAEV_18011510mg {ECO:0000313|EMBL:OCT93839.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:OCT93839.1, ECO:0000313|Proteomes:UP000186698};
RN   [1] {ECO:0000313|Proteomes:UP000186698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J {ECO:0000313|Proteomes:UP000186698};
RX   PubMed=27762356; DOI=10.1038/nature19840;
RA   Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA   Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J.,
RA   Quigley I., Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B.,
RA   Simakov O., Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T.,
RA   Watanabe M., Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S.,
RA   van Kruijsbergen I., Shu S., Carlson J., Kinoshita T., Ohta Y.,
RA   Mawaribuchi S., Jenkins J., Grimwood J., Schmutz J., Mitros T.,
RA   Mozaffari S.V., Suzuki Y., Haramoto Y., Yamamoto T.S., Takagi C.,
RA   Heald R., Miller K., Haudenschild C., Kitzman J., Nakayama T.,
RA   Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V., Karimi K.,
RA   Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W., Shendure J.,
RA   DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA   Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y.,
RA   Veenstra G.J., Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT   "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL   Nature 538:336-343(2016).
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; CM004468; OCT93839.1; -; Genomic_DNA.
DR   RefSeq; NP_001080933.1; NM_001087464.1.
DR   RefSeq; XP_018101434.1; XM_018245945.1.
DR   UniGene; Xl.42; -.
DR   SMR; A0A1L8HCL3; -.
DR   GeneID; 108707883; -.
DR   GeneID; 394274; -.
DR   KEGG; xla:108707883; -.
DR   KEGG; xla:394274; -.
DR   CTD; 394274; -.
DR   Xenbase; XB-GENE-6254670; sod1.
DR   KO; K04565; -.
DR   OrthoDB; 1574423at2759; -.
DR   Proteomes; UP000186698; Chromosome 2l.
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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000186698};
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:UP000186698};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       11    147       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   151 AA;  15418 MW;  8DA6A8FDA1C7FB36 CRC64;
     MVKAVCVLAG SGDVKGVVHF EQQDEGAVSV EGKIEGLTDG LHGFHIHVFG DNTNGCMSAG
     SHFNPENKNH GAPGDTDRHV GDLGNVTAEG GVAQFKITDS LISLKGPNSI IGRTAVVHEK
     ADDLGKGGND ESLKTGNAGG RLACGVIGYS P
//
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