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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.
08-MAY-2019, entry version 153.
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}.
-----------------------------------------------------------------------
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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]
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-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.
ExpressionAtlas; P34461; baseline and differential.
GO; GO:0005576; C:extracellular region; 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: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


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[sodC DDB_G0282993] Extracellular superoxide dismutase [Cu-Zn] 3 (EC-SOD 3) (EC 1.15.1.1)
[sod-1 C15F1.7] Superoxide dismutase [Cu-Zn] (EC 1.15.1.1)
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[sod-1 NCU02133] Superoxide dismutase [Cu-Zn] (EC 1.15.1.1)
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[SOD2] Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1)
[Sod2 Sod-2] Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1)
[sodB sod sodA Rv3846 MTCY01A6.22c] Superoxide dismutase [Fe] (EC 1.15.1.1)
[Sod2] Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1)
[sod1-a] Superoxide dismutase [Cu-Zn] A (XSODA) (EC 1.15.1.1)
[FSD2 APG8 At5g51100 MWD22.4] Superoxide dismutase [Fe] 2, chloroplastic (EC 1.15.1.1) (Protein ALBINO OR PALE GREEN 8) (Protein FE SUPEROXIDE DISMUTASE 2)
[mbnA MettrDRAFT_4473] Methanobactin mb-OB3b (Copper-binding compound) (CBC) (Hydrogen peroxide reductase) (EC 1.11.1.-) (Superoxide dismutase) (EC 1.15.1.1)
[hchA A9819_11910 ACN81_03425 AML35_08765 AW059_23935 BANRA_00208 BANRA_00433 BANRA_02614 BHF46_18455 BMT91_24760 BvCmsC61A_00149 BvCmsH15A_00510 BvCmsKSNP120_04693 BvCmsKSP026_03873 BvCmsKSP076_04891 C4J69_22715 C7B08_25495 CR538_10415 D2F89_25795 D3Y67_22910 D9G42_11130 D9I97_22010 D9J11_25195 DP258_02540 E5M00_18610 EC3234A_36c00010 EC382_21100 ECTO6_01955 EFV06_13085 EPS71_23885 FORC82_1921 NCTC8500_02249 NCTC9037_02122 NCTC9117_02637 NCTC9969_02156 SAMEA3472108_01151 SAMEA3484427_04795 SAMEA3484429_02051 SAMEA3752557_05476 SAMEA3752559_04333] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[sodA sod] Superoxide dismutase [Mn/Fe] (EC 1.15.1.1)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[sodF1 sodB sodF SCO2633 SC8E4A.03] Superoxide dismutase [Fe-Zn] 1 (EC 1.15.1.1) (FeSOD I) (SOD2)
[hchA A8M42_01610 AM465_15370 AWF59_019055 AZZ83_004235 B9N33_26475 BFD68_20845 C1I57_21890 C7B02_06890 CCZ14_26645 CCZ17_22700 CRT43_11430 CT143_08220 D3C88_02905 D9D33_15385 D9E49_19020 D9I20_10460 D9J46_03345 DNR41_00375 DS966_16070 DU333_03260 DW236_02290 ECTO124_02024 EGT48_04930 EPS76_06485 EPS91_17475 EPS94_00505 ERS085406_02591 EWK56_00075 ExPECSC007_02422 ExPECSC065_02714 HmCmsJML122_02218 NCTC10766_03778 NCTC7928_05955 NCTC8450_02317 NCTC9007_02951 NCTC9075_02834 NCTC9775_01269 SY51_11150 U12A_02105 U14A_02105] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[CCS At1g12520 F5O11.26 T12C24.6] Copper chaperone for superoxide dismutase, chloroplastic/cytosolic (AtCCS) (Superoxide dismutase copper chaperone)
[sod1 sod VNG_1190G] Superoxide dismutase [Mn] 1 (EC 1.15.1.1)
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BMT53_00170 BUE81_10670 BvCms12BK_01457 BvCms28BK_04168 BvCmsHHP001_02632 BvCmsKKP061_00566 BvCmsKSP008_02510 BvCmsKSP015_01352 BvCmsKSP036_04668 BvCmsKSP045_04450 BvCmsKSP058_03204 BvCmsKSP067_02879 BvCmsKSP083_03900 BvCmsNSNP027_04914 BvCmsNSP006_03750 BvCmsNSP007_03329 BvCmsNSP039_03266 BvCmsNSP047_03567 BvCmsNSP078_03451 BvCmsSINP011_04162 BvCmsSIP006_05510 BvCmsSIP082_02402 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 CDL37_00765 CIJ94_05515 COD46_23180 CQP61_17160 CRD98_26150 CY655_12940 D5618_21870 D9D20_21030 D9D43_06110 D9H68_20750 D9H70_25730 D9I87_15275 DL800_09215 DNQ41_14245 DQE83_22775 DTL43_21780 DTM25_06080 DU321_04440 E2855_02503 E2863_02392 EC95NR1_00961 ED648_25045 EFB45_10990 EPS97_16570 EPT01_11070 EQ825_23250 ERS085379_01273 ERS085386_05041 EVY21_22520 ExPECSC038_01920 EXX32_14605 EXX71_02385 EXX78_21815 EYD11_09165 HmCmsJML079_02678 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13462_05714 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PU06_24500 SAMEA3472043_00447 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[hchA ACN77_19040 BvCmsKSP081_02693 BvCmsSINP012_02510 C2M16_14375 C7235_09910 C9E25_26080 EAI46_23445 EFV08_20755 EJC48_03045 EJC75_08600 ERS085365_03701 ERS139211_04220 EVY14_26820 EXX77_21120 SAMEA3752553_03148] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]

Bibliography :
[29926349] Production of functional human CuZn-SOD and EC-SOD in bitransgenic cloned goat milk.
[29772010] Hypergravity enhances the therapeutic effect of dexamethasone in allergic asthma and rhinitis animal model.
[29029079] Sialylation of extracellular superoxide dismutase (EC-SOD) enhances furin-mediated cleavage and secretion.
[29020797] Extracellular Superoxide Dismutase Attenuates Renal Oxidative Stress Through the Activation of Adenosine Monophosphate-Activated Protein Kinase in Diabetic Nephropathy.
[28878123] The R213G polymorphism in SOD3 protects against allergic airway inflammation.
[28757400] Epigenetic regulation of EC-SOD expression in aging lung fibroblasts: Role of histone acetylation.
[27966735] Genetic polymorphisms in extracellular superoxide dismutase Leu53Leu, Arg213Gly, and Ala40Thr and susceptibility to type 2 diabetes mellitus.
[27904046] CoCl Decreases EC-SOD Expression through Histone Deacetylation in COS7 Cells.
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