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Database: UniProt/SWISS-PROT
Entry: SOD1B_XENLA
LinkDB: SOD1B_XENLA
Original site: SOD1B_XENLA 
ID   SOD1B_XENLA             Reviewed;         151 AA.
AC   P15107; Q5D025;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-OCT-2017, entry version 140.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] B;
DE            Short=XSODB;
DE            EC=1.15.1.1;
GN   Name=sod1-b;
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].
RC   TISSUE=Tadpole;
RX   PubMed=2326205; DOI=10.1093/nar/18.6.1641;
RA   Carri M.T., Battistoni A., Mariottini P., Rotilio G.;
RT   "Xenopus laevis Cu,Zn superoxide dismutase B cDNA sequence.";
RL   Nucleic Acids Res. 18:1641-1641(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) 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).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS).
RX   PubMed=15299740; DOI=10.1107/S0907444995007608;
RA   Djinovic Carugo K., Battistoni A., Carri M.T., Polticelli F.,
RA   Desideri A., Rotilio G., Coda A., Wilson K.S., Bolognesi M.;
RT   "Three-dimensional structure of Xenopus laevis Cu,Zn superoxide
RT   dismutase b determined by X-ray crystallography at 1.5-A resolution.";
RL   Acta Crystallogr. D 52:176-188(1996).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC       Note=Binds 1 copper ion per subunit.;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit.;
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   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
DR   EMBL; X51518; CAA35890.1; -; mRNA.
DR   EMBL; BC070696; AAH70696.1; -; mRNA.
DR   PIR; S09568; S09568.
DR   RefSeq; NP_001080933.1; NM_001087464.1.
DR   RefSeq; XP_018101434.1; XM_018245945.1.
DR   UniGene; Xl.42; -.
DR   PDB; 1XSO; X-ray; 1.49 A; A/B=2-151.
DR   PDBsum; 1XSO; -.
DR   ProteinModelPortal; P15107; -.
DR   SMR; P15107; -.
DR   GeneID; 108707883; -.
DR   GeneID; 394274; -.
DR   KEGG; xla:108707883; -.
DR   KEGG; xla:394274; -.
DR   CTD; 394274; -.
DR   Xenbase; XB-GENE-6254670; sod1.
DR   HOVERGEN; HBG000062; -.
DR   KO; K04565; -.
DR   EvolutionaryTrace; P15107; -.
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   3D-structure; Antioxidant; Copper; Cytoplasm;
KW   Direct protein sequencing; Disulfide bond; Lipoprotein; Metal-binding;
KW   Nucleus; Oxidoreductase; 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] B.
FT                                /FTId=PRO_0000164077.
FT   METAL        45     45       Copper; catalytic.
FT   METAL        47     47       Copper; catalytic.
FT   METAL        62     62       Copper; catalytic.
FT   METAL        62     62       Zinc; structural.
FT   METAL        70     70       Zinc; structural.
FT   METAL        79     79       Zinc; structural.
FT   METAL        82     82       Zinc; structural.
FT   METAL       118    118       Copper; catalytic.
FT   LIPID         6      6       S-palmitoyl cysteine. {ECO:0000250}.
FT   DISULFID     56    144
FT   CONFLICT     61     61       S -> P (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   STRAND        3      9       {ECO:0000244|PDB:1XSO}.
FT   STRAND       11     13       {ECO:0000244|PDB:1XSO}.
FT   STRAND       15     23       {ECO:0000244|PDB:1XSO}.
FT   STRAND       28     36       {ECO:0000244|PDB:1XSO}.
FT   STRAND       39     48       {ECO:0000244|PDB:1XSO}.
FT   HELIX        55     59       {ECO:0000244|PDB:1XSO}.
FT   STRAND       76     78       {ECO:0000244|PDB:1XSO}.
FT   STRAND       82     89       {ECO:0000244|PDB:1XSO}.
FT   STRAND       92    101       {ECO:0000244|PDB:1XSO}.
FT   STRAND      103    106       {ECO:0000244|PDB:1XSO}.
FT   STRAND      113    120       {ECO:0000244|PDB:1XSO}.
FT   STRAND      127    129       {ECO:0000244|PDB:1XSO}.
FT   HELIX       132    135       {ECO:0000244|PDB:1XSO}.
FT   STRAND      141    146       {ECO:0000244|PDB:1XSO}.
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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