SODE_CAEEL
ID SODE_CAEEL Reviewed; 221 AA.
AC P34461; O61260;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 04-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Extracellular superoxide dismutase [Cu-Zn];
DE Short=EC-SOD;
DE EC=1.15.1.1 {ECO:0000269|PubMed:9628580};
DE Flags: Precursor;
GN Name=sod-4; ORFNames=F55H2.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC ACTIVITY
RP (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), TISSUE
RP SPECIFICITY (ISOFORM 2), AND DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2;
RX PubMed=9628580; DOI=10.1093/dnares/5.1.25;
RA Fujii M., Ishii N., Joguchi A., Yasuda K., Ayusawa D.;
RT "A novel superoxide dismutase gene encoding membrane-bound and
RT extracellular isoforms by alternative splicing in Caenorhabditis elegans.";
RL DNA Res. 5:25-30(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-56, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-56, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: Protects cells against oxidative stress by converting
CC superoxide radicals to hydrogen peroxide (PubMed:9628580). Oxidative
CC stress is involved in various biological dysfunctions and senescence
CC (PubMed:9628580). {ECO:0000269|PubMed:9628580,
CC ECO:0000303|PubMed:9628580}.
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
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 Evidence={ECO:0000269|PubMed:9628580};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20697;
CC Evidence={ECO:0000269|PubMed:9628580};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
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 Evidence={ECO:0000269|PubMed:9628580};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20697;
CC Evidence={ECO:0000269|PubMed:9628580};
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 -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted, extracellular space
CC {ECO:0000269|PubMed:9628580}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Membrane
CC {ECO:0000269|PubMed:9628580}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2; Synonyms=Sod4-2;
CC IsoId=P34461-2; Sequence=Displayed;
CC Name=1; Synonyms=Sod4-1;
CC IsoId=P34461-1; Sequence=VSP_007920;
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Isoform 2 is preferentially expressed
CC in eggs. {ECO:0000269|PubMed:9628580}.
CC -!- DEVELOPMENTAL STAGE: Isoforms are expressed differently during
CC development, while isoform 2 is preferentially expressed in eggs,
CC isoform 1 is preferentially expressed in the adults.
CC {ECO:0000305|PubMed:9628580}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; AB003924; BAA28262.1; -; mRNA.
DR EMBL; Z27080; CAB61015.1; -; Genomic_DNA.
DR PIR; JE0097; JE0097.
DR PIR; JE0098; JE0098.
DR PIR; S40984; S40984.
DR RefSeq; NP_001255003.1; NM_001268074.1. [P34461-1]
DR AlphaFoldDB; P34461; -.
DR SMR; P34461; -.
DR STRING; 6239.F55H2.1b; -.
DR iPTMnet; P34461; -.
DR PaxDb; P34461; -.
DR PeptideAtlas; P34461; -.
DR EnsemblMetazoa; F55H2.1a.1; F55H2.1a.1; WBGene00004933. [P34461-1]
DR EnsemblMetazoa; F55H2.1a.2; F55H2.1a.2; WBGene00004933. [P34461-1]
DR GeneID; 176336; -.
DR UCSC; F55H2.1; c. elegans. [P34461-1]
DR CTD; 176336; -.
DR WormBase; F55H2.1a; CE25009; WBGene00004933; sod-4. [P34461-1]
DR eggNOG; KOG0441; Eukaryota.
DR GeneTree; ENSGT00940000155551; -.
DR InParanoid; P34461; -.
DR PhylomeDB; P34461; -.
DR Reactome; R-CEL-3299685; Detoxification of Reactive Oxygen Species.
DR PRO; PR:P34461; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004933; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; P34461; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IDA:WormBase.
DR GO; GO:0016020; C:membrane; IDA:WormBase.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0004784; F:superoxide dismutase activity; IDA:WormBase.
DR GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
DR GO; GO:0006801; P:superoxide metabolic process; IDA:WormBase.
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 Alternative splicing; Antioxidant; Copper; Disulfide bond; Glycoprotein;
KW Membrane; Metal-binding; Oxidoreductase; Reference proteome; Secreted;
KW Signal; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..221
FT /note="Extracellular superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000032861"
FT BINDING 70
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT DISULFID 81..170
FT /evidence="ECO:0000250"
FT VAR_SEQ 177..221
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:9628580"
FT /id="VSP_007920"
SQ 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
