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 03-AUG-2022, entry version 132.
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; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; 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., 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).
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-Zn] A
CC 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 later
CC 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};
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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 AlphaFoldDB; P13926; -.
DR SMR; P13926; -.
DR GeneID; 100381040; -.
DR CTD; 100381040; -.
DR Xenbase; XB-GENE-6252314; sod1.S.
DR OMA; KWVAFHV; -.
DR OrthoDB; 1574423at2759; -.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 100381040; Expressed in oocyte and 19 other tissues.
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; Disulfide bond;
KW Lipoprotein; Metal-binding; Nucleus; Oxidoreductase; Palmitate;
KW 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] A"
FT /id="PRO_0000164076"
FT BINDING 45
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT LIPID 6
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT DISULFID 56..144
FT /evidence="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
