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Database: UniProt/SWISS-PROT UniProt/TrEMBL
Entry: SOD1B_XENLA A0A1L8HCL3_XENLA
LinkDB: SOD1B_XENLA A0A1L8HCL3_XENLA
Original site: SOD1B_XENLA A0A1L8HCL3_XENLA 
tr:A0A1L8HCL3_XENLA : No such data.

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   10-MAY-2017, entry version 139.
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; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
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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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (7)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (2)   
   NCBI-Gene (2)   
   UniGene (1)   
   XENBASE (1)   
Protein sequence (2)   
   RefSeq(pep) (2)   
DNA sequence (2)   
   EMBL (2)   
3D Structure (1)   
   PDB (1)   
Protein domain (5)   
   InterPro (2)   
   Pfam (1)   
   PROSITE (2)   
Literature (5)   
   PubMed (5)   
All databases (27)   

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