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Extracellular superoxide dismutase [Cu-Zn] (EC-SOD) (EC 1.15.1.1)

 SODE_CAEEL              Reviewed;         221 AA.
P34461; O61260;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
04-AUG-2003, sequence version 2.
23-MAY-2018, entry version 148.
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;
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
-!- 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}.
-----------------------------------------------------------------------
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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; -.
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.
HOGENOM; HOG000263447; -.
InParanoid; P34461; -.
PhylomeDB; P34461; -.
Reactome; R-CEL-3299685; Detoxification of Reactive Oxygen Species.
PRO; PR:P34461; -.
Proteomes; UP000001940; Chromosome III.
Bgee; WBGene00004933; -.
ExpressionAtlas; P34461; baseline and differential.
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:0008270; F:zinc ion binding; 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


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