GENTAUR Molecular Products.

 SODE_CAEEL              Reviewed;         221 AA.
 P34461; O61260;
 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
 04-AUG-2003, sequence version 2.
 05-DEC-2018, entry version 152.
 RecName: Full=Extracellular superoxide dismutase [Cu-Zn];
          Short=EC-SOD;
          EC=1.15.1.1;
 Flags: Precursor;
 Name=sod-4; ORFNames=F55H2.1;
 Caenorhabditis elegans.
 Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
 Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
 Caenorhabditis.
 NCBI_TaxID=6239;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
 STRAIN=Bristol N2;
 PubMed=9628580; DOI=10.1093/dnares/5.1.25;
 Fujii M., Ishii N., Joguchi A., Yasuda K., Ayusawa D.;
 "A novel superoxide dismutase gene encoding membrane-bound and
 extracellular isoforms by alternative splicing in Caenorhabditis
 elegans.";
 DNA Res. 5:25-30(1998).
 [2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=Bristol N2;
 PubMed=7906398; DOI=10.1038/368032a0;
 Wilson R., Ainscough R., Anderson K., Baynes C., Berks M.,
 Bonfield J., Burton J., Connell M., Copsey T., Cooper J., Coulson A.,
 Craxton M., Dear S., Du Z., Durbin R., Favello A., Fraser A.,
 Fulton L., Gardner A., Green P., Hawkins T., Hillier L., Jier M.,
 Johnston L., Jones M., Kershaw J., Kirsten J., Laisster N.,
 Latreille P., Lightning J., Lloyd C., Mortimore B., O'Callaghan M.,
 Parsons J., Percy C., Rifken L., Roopra A., Saunders D., Shownkeen R.,
 Sims M., Smaldon N., Smith A., Smith M., Sonnhammer E., Staden R.,
 Sulston J., Thierry-Mieg J., Thomas K., Vaudin M., Vaughan K.,
 Waterston R., Watson A., Weinstock L., Wilkinson-Sproat J.,
 Wohldman P.;
 "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
 elegans.";
 Nature 368:32-38(1994).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=Bristol N2;
 PubMed=9851916; DOI=10.1126/science.282.5396.2012;
 The C. elegans sequencing consortium;
 "Genome sequence of the nematode C. elegans: a platform for
 investigating biology.";
 Science 282:2012-2018(1998).
 [4]
 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-56, AND IDENTIFICATION BY
 MASS SPECTROMETRY.
 STRAIN=Bristol N2;
 PubMed=12754521; DOI=10.1038/nbt829;
 Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
 Kasai K., Takahashi N., Isobe T.;
 "Lectin affinity capture, isotope-coded tagging and mass spectrometry
 to identify N-linked glycoproteins.";
 Nat. Biotechnol. 21:667-672(2003).
 [5]
 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-56, AND IDENTIFICATION BY
 MASS SPECTROMETRY.
 STRAIN=Bristol N2;
 PubMed=17761667; DOI=10.1074/mcp.M600392-MCP200;
 Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
 Taoka M., Takahashi N., Isobe T.;
 "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
 elegans and suggests an atypical translocation mechanism for integral
 membrane proteins.";
 Mol. Cell. Proteomics 6:2100-2109(2007).
 -!- FUNCTION: Destroys radicals which are normally produced within the
     cells and which are toxic to biological systems. {ECO:0000250}.
 -!- CATALYTIC ACTIVITY:
     Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
       ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
       ChEBI:CHEBI:18421; EC=1.15.1.1;
 -!- COFACTOR:
     Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
     Note=Binds 1 copper ion per subunit. {ECO:0000250};
 -!- COFACTOR:
     Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
     Note=Binds 1 zinc ion per subunit. {ECO:0000250};
 -!- SUBCELLULAR LOCATION: Isoform 1: Secreted, extracellular space.
 -!- SUBCELLULAR LOCATION: Isoform 2: Membrane {ECO:0000305};
     Peripheral membrane protein {ECO:0000305}.
 -!- ALTERNATIVE PRODUCTS:
     Event=Alternative splicing; Named isoforms=2;
     Name=2; Synonyms=Sod4-2;
       IsoId=P34461-2; Sequence=Displayed;
     Name=1; Synonyms=Sod4-1;
       IsoId=P34461-1; Sequence=VSP_007920;
 -!- TISSUE SPECIFICITY: Isoform 2 is preferentially expressed in eggs.
 -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
     {ECO:0000305}.
 -----------------------------------------------------------------------
 Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
 Distributed under the Creative Commons Attribution (CC BY 4.0) License
 -----------------------------------------------------------------------
 EMBL; AB003924; BAA28262.1; -; mRNA.
 EMBL; Z27080; CAB61015.1; -; Genomic_DNA.
 PIR; JE0097; JE0097.
 PIR; JE0098; JE0098.
 PIR; S40984; S40984.
 RefSeq; NP_001255003.1; NM_001268074.1. [P34461-1]
 UniGene; Cel.19659; -.
 ProteinModelPortal; P34461; -.
 SMR; P34461; -.
 STRING; 6239.F55H2.1b; -.
 iPTMnet; P34461; -.
 PaxDb; P34461; -.
 PeptideAtlas; P34461; -.
 PRIDE; P34461; -.
 EnsemblMetazoa; F55H2.1a; F55H2.1a; WBGene00004933. [P34461-1]
 GeneID; 176336; -.
 UCSC; F55H2.1; c. elegans. [P34461-1]
 CTD; 176336; -.
 WormBase; F55H2.1a; CE25009; WBGene00004933; sod-4. [P34461-1]
 eggNOG; KOG0441; Eukaryota.
 eggNOG; COG2032; LUCA.
 GeneTree; ENSGT00940000155551; -.
 HOGENOM; HOG000263447; -.
 InParanoid; P34461; -.
 PhylomeDB; P34461; -.
 Reactome; R-CEL-114608; Platelet degranulation.
 Reactome; R-CEL-3299685; Detoxification of Reactive Oxygen Species.
 PRO; PR:P34461; -.
 Proteomes; UP000001940; Chromosome III.
 Bgee; WBGene00004933; Expressed in 4 organ(s), highest expression level in adult organism.
 GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
 GO; GO:0005615; C:extracellular space; IDA:WormBase.
 GO; GO:0016020; C:membrane; IDA:WormBase.
 GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
 GO; GO:0004784; F:superoxide dismutase activity; IDA:WormBase.
 GO; GO:0016532; F:superoxide dismutase copper chaperone activity; IBA:GO_Central.
 GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
 GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
 GO; GO:0006801; P:superoxide metabolic process; IDA:WormBase.
 CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
 Gene3D; 2.60.40.200; -; 1.
 InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
 InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
 InterPro; IPR018152; SOD_Cu/Zn_BS.
 InterPro; IPR001424; SOD_Cu_Zn_dom.
 PANTHER; PTHR10003; PTHR10003; 1.
 Pfam; PF00080; Sod_Cu; 1.
 PRINTS; PR00068; CUZNDISMTASE.
 SUPFAM; SSF49329; SSF49329; 1.
 PROSITE; PS00087; SOD_CU_ZN_1; 1.
 PROSITE; PS00332; SOD_CU_ZN_2; 1.
 1: Evidence at protein level;
 Alternative splicing; Antioxidant; Complete proteome; Copper;
 Disulfide bond; Glycoprotein; Membrane; Metal-binding; Oxidoreductase;
 Reference proteome; Secreted; Signal; Zinc.
 SIGNAL        1     19       {ECO:0000255}.
 CHAIN        20    221       Extracellular superoxide dismutase [Cu-
                              Zn].
                              /FTId=PRO_0000032861.
 METAL        70     70       Copper; catalytic. {ECO:0000250}.
 METAL        72     72       Copper; catalytic. {ECO:0000250}.
 METAL        87     87       Copper; catalytic. {ECO:0000250}.
 METAL        87     87       Zinc; structural. {ECO:0000250}.
 METAL        95     95       Zinc; structural. {ECO:0000250}.
 METAL       104    104       Zinc; structural. {ECO:0000250}.
 METAL       107    107       Zinc; structural. {ECO:0000250}.
 METAL       144    144       Copper; catalytic. {ECO:0000250}.
 CARBOHYD     56     56       N-linked (GlcNAc...) asparagine.
                              {ECO:0000269|PubMed:12754521,
                              ECO:0000269|PubMed:17761667}.
 DISULFID     81    170       {ECO:0000250}.
 VAR_SEQ     177    221       Missing (in isoform 1).
                              {ECO:0000303|PubMed:9628580}.
                              /FTId=VSP_007920.
 SEQUENCE   221 AA;  23326 MW;  0769AC65F17CC883 CRC64;
 MKTRVVLILA LSVCIEAASE VIRARAYIFK AEAGKIPTEL IGTIDFDQSG SFLKLNGSVS
 GLAAGKHGFH IHEKGDTGNG CLSAGGHYNP HKLSHGAPDD SNRHIGDLGN IESPASGDTL
 ISVSDSLASL SGQYSIIGRS VVIHEKTDDL GRGTSDQSKT TGNAGSRLAC GTIGTVEERI
 LETTTASLPP VTQSQPIGSS SYYYSTFYLP IILYFLLSRI L

Related products :