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Database: UniProt/SWISS-PROT
Entry: SOD1A_XENLA
LinkDB: SOD1A_XENLA
Original site: SOD1A_XENLA 
ID   SOD1A_XENLA             Reviewed;         151 AA.
AC   P13926; Q0P3T2; Q2VPM0;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JAN-2019, entry version 123.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] A;
DE            Short=XSODA;
DE            EC=1.15.1.1;
GN   Name=sod1-a;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   TISSUE=Oocyte;
RX   PubMed=2598938; DOI=10.1111/j.1432-1033.1989.tb15226.x;
RA   Montesano L., Carri M.T., Mariottini P., Amaldi F., Rotilio G.;
RT   "Developmental expression of Cu,Zn superoxide dismutase in Xenopus.
RT   Constant level of the enzyme in oogenesis and embryogenesis.";
RL   Eur. J. Biochem. 186:421-426(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 2-151.
RX   PubMed=2751312; DOI=10.1016/0003-9861(89)90246-4;
RA   Schinina M.E., Barra D., Bossa F., Calabrese L., Montesano L.,
RA   Carri M.T., Mariottini P., Amaldi F., Rotilio G.;
RT   "Primary structure from amino acid and cDNA sequences of two Cu,Zn
RT   superoxide dismutase variants from Xenopus laevis.";
RL   Arch. Biochem. Biophys. 272:507-515(1989).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-31, AND SUBUNIT.
RX   PubMed=2268321; DOI=10.1016/S0006-291X(05)80911-8;
RA   Capo C.R., Polticelli F., Calabrese L., Schinina M.E., Carri M.T.,
RA   Rotilio G.;
RT   "The Cu,Zn superoxide dismutase isoenzymes of Xenopus laevis:
RT   purification, identification of a heterodimer and differential heat
RT   sensitivity.";
RL   Biochem. Biophys. Res. Commun. 173:1186-1193(1990).
RN   [5]
RP   3D-STRUCTURE MODELING.
RX   PubMed=1896428; DOI=10.1002/prot.340100208;
RA   Falconi M., Rotilio G., Desideri A.;
RT   "Modelling the three-dimensional structure and electrostatic potential
RT   field of the two Cu,Zn superoxide dismutase variants from Xenopus
RT   laevis.";
RL   Proteins 10:149-155(1991).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
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   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer, and heterodimer of Superoxide dismutase [Cu-
CC       Zn] A and B. {ECO:0000269|PubMed:2268321}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       Expression accumulates through oogenesis, remaining more or less
CC       constant at the beginning of embryogenesis, to slightly increase
CC       later on (at protein level). {ECO:0000269|PubMed:2598938}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI22467.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; X16585; CAA34602.1; -; mRNA.
DR   EMBL; BC108610; AAI08611.1; -; mRNA.
DR   EMBL; BC122466; AAI22467.1; ALT_INIT; mRNA.
DR   PIR; S05021; S05021.
DR   RefSeq; XP_018104357.1; XM_018248868.1.
DR   UniGene; Xl.1162; -.
DR   UniGene; Xl.85768; -.
DR   ProteinModelPortal; P13926; -.
DR   SMR; P13926; -.
DR   GeneID; 100381040; -.
DR   KEGG; xla:100381040; -.
DR   CTD; 100381040; -.
DR   Xenbase; XB-GENE-6252314; sod1.
DR   HOVERGEN; HBG000062; -.
DR   KO; K04565; -.
DR   OrthoDB; 1574423at2759; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
KW   Antioxidant; Copper; Cytoplasm; Direct protein sequencing;
KW   Disulfide bond; Lipoprotein; Metal-binding; Nucleus; Oxidoreductase;
KW   Palmitate; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:2268321,
FT                                ECO:0000269|PubMed:2751312}.
FT   CHAIN         2    151       Superoxide dismutase [Cu-Zn] A.
FT                                /FTId=PRO_0000164076.
FT   METAL        45     45       Copper; catalytic. {ECO:0000250}.
FT   METAL        47     47       Copper; catalytic. {ECO:0000250}.
FT   METAL        62     62       Copper; catalytic. {ECO:0000250}.
FT   METAL        62     62       Zinc; structural. {ECO:0000250}.
FT   METAL        70     70       Zinc; structural. {ECO:0000250}.
FT   METAL        79     79       Zinc; structural. {ECO:0000250}.
FT   METAL        82     82       Zinc; structural. {ECO:0000250}.
FT   METAL       118    118       Copper; catalytic. {ECO:0000250}.
FT   LIPID         6      6       S-palmitoyl cysteine. {ECO:0000250}.
FT   DISULFID     56    144       {ECO:0000250}.
SQ   SEQUENCE   151 AA;  15721 MW;  6ABE0B23C120E77E CRC64;
     MVKAVCVLAG SGDVKGVVRF EQQDDGDVTV EGKIEGLTDG NHGFHIHVFG DNTNGCLSAG
     PHFNPQNKNH GSPKDADRHV GDLGNVTAEG GVAQFKFTDP QISLKGERSI IGRTAVVHEK
     QDDLGKGGDD ESLKTGNAGG RLACGVIGFC P
//
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