ID SOD1_MESCR STANDARD; PRT; 152 AA. AC P93258; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE SUPEROXIDE DISMUTASE [CU-ZN] 1 (EC 1.15.1.1). GN SODCC.1 OR SOD1 OR SOD. OS Mesembryanthemum crystallinum (Common ice plant). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; eudicotyledons; Caryophyllidae; Caryophyllales; OC Aizoaceae; Mesembryanthemum. RN [1] RP SEQUENCE FROM N.A. RA Michalowski C.B., Quigley-Landreau F., Bohnert H.J.; RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DESTROYS RADICALS WHICH ARE NORMALLY PRODUCED WITHIN THE CC CELLS AND ARE TOXIC TO BIOLOGICAL SYSTEMS. CC -!- CATALYTIC ACTIVITY: 2 PEROXIDE RADICAL + 2 H(+) = O(2) + H(2)O(2). CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- MISCELLANEOUS: EUKARYOTIC CELLS CONTAIN A MITOCHONDRIAL CC MN-CONTAINING ENZYME & A CYTOPLASMIC CU-ZN-CONTAINING ENZYME. CC PLANT ALSO HAVE A CHLOROPLAST CU-ZN ENZYME. CC -!- SIMILARITY: BELONGS TO THE CU-ZN SUPEROXIDE DISMUTASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; U80069; AAB40394.1; -. DR HSSP; P07505; 1SRD. DR MENDEL; 9129; MEScr;SodCc;1. DR INTERPRO; IPR001424; -. DR PFAM; PF00080; sodcu; 1. DR PRINTS; PR00068; CUZNDISMTASE. DR PROSITE; PS00087; SOD_CU_ZN_1; 1. DR PROSITE; PS00332; SOD_CU_ZN_2; 1. KW Oxidoreductase; Copper; Zinc; Multigene family. FT METAL 45 45 COPPER (BY SIMILARITY). FT METAL 47 47 COPPER (BY SIMILARITY). FT METAL 62 62 COPPER AND ZINC (BY SIMILARITY). FT METAL 70 70 ZINC (BY SIMILARITY). FT METAL 79 79 ZINC (BY SIMILARITY). FT METAL 82 82 ZINC (BY SIMILARITY). FT METAL 119 119 COPPER (BY SIMILARITY). FT DISULFID 56 145 BY SIMILARITY. SQ SEQUENCE 152 AA; 15173 MW; 44771D3714ADB19C CRC64; MVKAVVVLSS SEGVSGTVQF TQEGSGPTTV TGNVSGLRPG LHGFHVHALG DTTNGCMSTG PHFNPAGKEH GAPEDETRHA GDLGNITVGD DGTATFTIID SQIPLTGPNS IVGRAVVVHA DPDDLGRGGH ELSKATGNAG GRVACGVIGL QG //