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 27-MAR-2024, entry version 163. 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; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; 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., Carri M.T., RA 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: purification, RT identification of a heterodimer and differential heat 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 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., Desideri A., RA Rotilio G., Coda A., Wilson K.S., Bolognesi M.; RT "Three-dimensional structure of Xenopus laevis Cu,Zn superoxide dismutase b RT 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: 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; 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-Zn] A CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 1XSO; X-ray; 1.49 A; A/B=2-151. DR PDBsum; 1XSO; -. DR AlphaFoldDB; P15107; -. DR SMR; P15107; -. DR BioGRID; 98876; 1. DR AGR; Xenbase:XB-GENE-6254670; -. DR Xenbase; XB-GENE-6254670; sod1.L. DR OMA; AQRGFHI; -. DR OrthoDB; 3470597at2759; -. DR EvolutionaryTrace; P15107; -. DR Proteomes; UP000186698; Genome assembly. DR Bgee; 108707883; Expressed in oocyte and 19 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. 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; Superoxide dismutase, copper/zinc binding domain; 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:SF103; SUPEROXIDE DISMUTASE [CU-ZN]; 1. DR PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1. DR Pfam; PF00080; Sod_Cu; 1. DR PRINTS; PR00068; CUZNDISMTASE. DR SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 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; Direct protein sequencing; KW Disulfide bond; Lipoprotein; Metal-binding; Nucleus; Oxidoreductase; KW Palmitate; Reference proteome; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:2268321, FT ECO:0000269|PubMed:2751312" FT CHAIN 2..151 FT /note="Superoxide dismutase [Cu-Zn] B" FT /id="PRO_0000164077" FT BINDING 45 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT BINDING 47 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT BINDING 62 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT BINDING 62 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT BINDING 70 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT BINDING 79 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT BINDING 82 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT BINDING 118 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT LIPID 6 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT DISULFID 56..144 FT CONFLICT 61 FT /note="S -> P (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 3..9 FT /evidence="ECO:0007829|PDB:1XSO" FT STRAND 11..13 FT /evidence="ECO:0007829|PDB:1XSO" FT STRAND 15..23 FT /evidence="ECO:0007829|PDB:1XSO" FT STRAND 28..36 FT /evidence="ECO:0007829|PDB:1XSO" FT STRAND 39..48 FT /evidence="ECO:0007829|PDB:1XSO" FT HELIX 55..59 FT /evidence="ECO:0007829|PDB:1XSO" FT STRAND 76..78 FT /evidence="ECO:0007829|PDB:1XSO" FT STRAND 82..89 FT /evidence="ECO:0007829|PDB:1XSO" FT STRAND 92..101 FT /evidence="ECO:0007829|PDB:1XSO" FT STRAND 103..106 FT /evidence="ECO:0007829|PDB:1XSO" FT STRAND 113..120 FT /evidence="ECO:0007829|PDB:1XSO" FT STRAND 127..129 FT /evidence="ECO:0007829|PDB:1XSO" FT HELIX 132..135 FT /evidence="ECO:0007829|PDB:1XSO" FT STRAND 141..146 FT /evidence="ECO:0007829|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 //