Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Superoxide dismutase [Cu-Zn] (EC 1.15.1.1)

 SODC_CAEEL              Reviewed;         180 AA.
P34697; Q5W7E8; Q9N5Y1;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
29-APR-2008, sequence version 2.
28-FEB-2018, entry version 147.
RecName: Full=Superoxide dismutase [Cu-Zn];
EC=1.15.1.1;
Flags: Precursor;
Name=sod-1; ORFNames=C15F1.7;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
PubMed=8415630; DOI=10.1073/pnas.90.19.8905;
Larsen P.L.;
"Aging and resistance to oxidative damage in Caenorhabditis elegans.";
Proc. Natl. Acad. Sci. U.S.A. 90:8905-8909(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM B).
STRAIN=Bristol N2;
PubMed=8081212;
Giglio M.P., Hunter T., Bannister J.V., Bannister W.H., Hunter G.J.;
"The copper/zinc superoxide dismutase gene of Caenorhabditis
elegans.";
Biochem. Mol. Biol. Int. 33:41-44(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
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]
DISRUPTION PHENOTYPE.
PubMed=14657502; DOI=10.1126/science.1087167;
Shibata Y., Branicky R., Landaverde I.O., Hekimi S.;
"Redox regulation of germline and vulval development in Caenorhabditis
elegans.";
Science 302:1779-1782(2003).
[5]
ENZYME REGULATION, SUBUNIT, AND MUTAGENESIS OF ALA-167 AND ALA-169.
PubMed=16234242; DOI=10.1074/jbc.M509142200;
Jensen L.T., Culotta V.C.;
"Activation of CuZn superoxide dismutases from Caenorhabditis elegans
does not require the copper chaperone CCS.";
J. Biol. Chem. 280:41373-41379(2005).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18073424; DOI=10.1534/genetics.107.080788;
Yang W., Li J., Hekimi S.;
"A measurable increase in oxidative damage due to reduction in
superoxide detoxification fails to shorten the life span of long-lived
mitochondrial mutants of Caenorhabditis elegans.";
Genetics 177:2063-2074(2007).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=20380830; DOI=10.1016/j.ydbio.2010.03.026;
Yang Y., Han S.M., Miller M.A.;
"MSP hormonal control of the oocyte MAP kinase cascade and reactive
oxygen species signaling.";
Dev. Biol. 342:96-107(2010).
-!- FUNCTION: Destroys radicals which are normally produced within the
cells and which are toxic to biological systems (By similarity).
Required for normal brood size (PubMed:18073424). May be involved
in regulating mpk-1 phosphorylation downstream of phosphatase ptp-
2 during oocyte maturation (PubMed:20380830).
{ECO:0000250|UniProtKB:P00441, ECO:0000269|PubMed:18073424,
ECO:0000269|PubMed:20380830}.
-!- 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};
-!- ENZYME REGULATION: The insertion of copper which activates the
protein requires glutathione. This is independent of copper
chaperone for SOD1 (CCS), which activates orthologs.
{ECO:0000269|PubMed:16234242}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16234242}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=a;
IsoId=P34697-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=b;
IsoId=P34697-2; Sequence=VSP_033146;
-!- DISRUPTION PHENOTYPE: Worms exhibit increased oxidative stress and
reduced brood size (PubMed:18073424). RNAi-mediated knockdown
suppresses the slow germline development and the delayed egg-
production of clk-1 mutants (PubMed:14657502). RNAi-mediated
knockdown causes an increase in the number of oocytes with mpk-1
phosphorylation (PubMed:20380830). {ECO:0000269|PubMed:14657502,
ECO:0000269|PubMed:18073424, ECO:0000269|PubMed:20380830}.
-!- 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-NoDerivs License
-----------------------------------------------------------------------
EMBL; L20135; AAA28147.1; -; mRNA.
EMBL; X77020; CAA54318.1; -; Genomic_DNA.
EMBL; FO080553; CCD64617.1; -; Genomic_DNA.
EMBL; FO080553; CCD64618.1; -; Genomic_DNA.
PIR; S41319; A48256.
RefSeq; NP_001021956.1; NM_001026785.2. [P34697-1]
RefSeq; NP_001021957.1; NM_001026786.3. [P34697-2]
UniGene; Cel.19756; -.
PDB; 3KBE; X-ray; 1.10 A; A=24-180.
PDB; 3KBF; X-ray; 1.30 A; A=24-180.
PDBsum; 3KBE; -.
PDBsum; 3KBF; -.
ProteinModelPortal; P34697; -.
SMR; P34697; -.
BioGrid; 39479; 1.
IntAct; P34697; 1.
STRING; 6239.C15F1.7a; -.
EPD; P34697; -.
PaxDb; P34697; -.
PeptideAtlas; P34697; -.
PRIDE; P34697; -.
EnsemblMetazoa; C15F1.7a; C15F1.7a; WBGene00004930. [P34697-1]
GeneID; 174141; -.
KEGG; cel:CELE_C15F1.7; -.
UCSC; C15F1.7a; c. elegans. [P34697-1]
CTD; 174141; -.
WormBase; C15F1.7a; CE23550; WBGene00004930; sod-1. [P34697-1]
WormBase; C15F1.7b; CE20508; WBGene00004930; sod-1. [P34697-2]
eggNOG; KOG0441; Eukaryota.
eggNOG; COG2032; LUCA.
GeneTree; ENSGT00530000063226; -.
HOGENOM; HOG000263447; -.
InParanoid; P34697; -.
KO; K04565; -.
OMA; HKGDIGN; -.
OrthoDB; EOG091G0OG2; -.
PhylomeDB; P34697; -.
EvolutionaryTrace; P34697; -.
PRO; PR:P34697; -.
Proteomes; UP000001940; Chromosome II.
Bgee; WBGene00004930; -.
GO; GO:0005737; C:cytoplasm; IC:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:WormBase.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; IDA:WormBase.
GO; GO:0005507; F:copper ion binding; IDA:WormBase.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0004784; F:superoxide dismutase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
GO; GO:0001306; P:age-dependent response to oxidative stress; IDA:WormBase.
GO; GO:0055114; P:oxidation-reduction process; IDA:WormBase.
GO; GO:0060378; P:regulation of brood size; IMP:UniProtKB.
GO; GO:0040028; P:regulation of vulval development; IGI:WormBase.
GO; GO:0019430; P:removal of superoxide radicals; IMP:WormBase.
GO; GO:0006801; P:superoxide metabolic process; IDA:UniProtKB.
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;
3D-structure; Alternative splicing; Antioxidant; Complete proteome;
Copper; Cytoplasm; Disulfide bond; Metal-binding; Oxidoreductase;
Reference proteome; Signal; Zinc.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 180 Superoxide dismutase [Cu-Zn].
/FTId=PRO_0000164102.
METAL 68 68 Copper; catalytic. {ECO:0000250}.
METAL 70 70 Copper; catalytic. {ECO:0000250}.
METAL 85 85 Copper; catalytic. {ECO:0000250}.
METAL 85 85 Zinc; structural. {ECO:0000250}.
METAL 93 93 Zinc; structural. {ECO:0000250}.
METAL 102 102 Zinc; structural. {ECO:0000250}.
METAL 105 105 Zinc; structural. {ECO:0000250}.
METAL 142 142 Copper; catalytic. {ECO:0000250}.
DISULFID 79 171 {ECO:0000250}.
VAR_SEQ 1 22 Missing (in isoform b).
{ECO:0000303|PubMed:8415630}.
/FTId=VSP_033146.
MUTAGEN 167 167 A->P: Abolishes enzyme activation but has
no effect on disulfide bond formation or
dimer formation; when associated with A-
169. {ECO:0000269|PubMed:16234242}.
MUTAGEN 169 169 A->P: Abolishes enzyme activation but has
no effect on disulfide bond formation or
dimer formation; when associated with A-
167. {ECO:0000269|PubMed:16234242}.
STRAND 26 32 {ECO:0000244|PDB:3KBE}.
STRAND 37 43 {ECO:0000244|PDB:3KBE}.
STRAND 52 59 {ECO:0000244|PDB:3KBE}.
STRAND 65 71 {ECO:0000244|PDB:3KBE}.
TURN 76 79 {ECO:0000244|PDB:3KBE}.
HELIX 80 82 {ECO:0000244|PDB:3KBE}.
STRAND 93 95 {ECO:0000244|PDB:3KBE}.
HELIX 96 99 {ECO:0000244|PDB:3KBE}.
STRAND 105 109 {ECO:0000244|PDB:3KBE}.
STRAND 115 121 {ECO:0000244|PDB:3KBE}.
STRAND 127 130 {ECO:0000244|PDB:3KBE}.
STRAND 137 142 {ECO:0000244|PDB:3KBE}.
HELIX 153 155 {ECO:0000244|PDB:3KBF}.
HELIX 156 162 {ECO:0000244|PDB:3KBF}.
TURN 164 167 {ECO:0000244|PDB:3KBE}.
STRAND 168 176 {ECO:0000244|PDB:3KBE}.
SEQUENCE 180 AA; 18700 MW; 5F013D99A650AA97 CRC64;
MFMNLLTQVS NAIFPQVEAA QKMSNRAVAV LRGETVTGTI WITQKSENDQ AVIEGEIKGL
TPGLHGFHVH QYGDSTNGCI SAGPHFNPFG KTHGGPKSEI RHVGDLGNVE AGADGVAKIK
LTDTLVTLYG PNTVVGRSMV VHAGQDDLGE GVGDKAEESK KTGNAGARAA CGVIALAAPQ


Related products :

Catalog number Product name Quantity
ESOD-100 EnzyChrom™ Superoxide Dismutase Assay Kit, Quantitative determination of superoxide dismutase (SOD) enzyme activity by colorimetric (440nm) method 100Tests
U0596h CLIA Homo sapiens,hSod1,Human,SOD1,Superoxide dismutase [Cu-Zn],Superoxide dismutase 1 96T
E0596h ELISA kit Homo sapiens,hSod1,Human,SOD1,Superoxide dismutase [Cu-Zn],Superoxide dismutase 1 96T
E0596h ELISA Homo sapiens,hSod1,Human,SOD1,Superoxide dismutase [Cu-Zn],Superoxide dismutase 1 96T
ESOD-100 EnzyChrom™ Superoxide Dismutase Assay Kit, Quantitative determination of superoxide dismutase (SOD) enzyme activity by colorimetric (440nm) method. Procedure 1 hr. Kit size 100 tests. Detection limi 100tests
EIAAB39207 EC-SOD,Extracellular superoxide dismutase [Cu-Zn],Rat,Rattus norvegicus,Sod3,Sod-3,Superoxide dismutase B
orb81377 Human Superoxide Dismutase-1 protein Recombinant Human Cu_Zn Superoxide Dismutase produced in E.coli is a single monomeric non-glycosylated polypeptide chain containing 154 amino acids and having tota 5
LF-MA0065 anti-Superoxide Dismutase 2 (4F10) , Mouse monoclonal to Superoxide Dismutase 2, Isotype IgG1, Host Mouse 100 ul
LF-MA0019 anti-Superoxide Dismutase 4 (11G1), Mouse monoclonal to Superoxide Dismutase 4, Isotype IgG1, Host Mouse 100 ul
LF-MA0023 anti-Superoxide Dismutase 1 (72B1), Mouse monoclonal to Superoxide Dismutase 1, Isotype IgG1, Host Mouse 100 ul
LF-MA0121 anti-Superoxide Dismutase 3 (1H12), Mouse monoclonal to Superoxide Dismutase 3, Isotype IgG2b, Host Mouse 100 ul
LF-MA0066 anti-Superoxide Dismutase 2 (23G5) , Mouse monoclonal to Superoxide Dismutase 2, Isotype IgG1, Host Mouse 100 ul
SCH-MCA2595 MOUSE ANTI SUPEROXIDE DISMUTASE (Cu_Zn), Product Type Monoclonal Antibody, Specificity SUPEROXIDE DISMUTASE , Target Species Bovine, Host Mouse, Format Purified, Isotypes IgG1, Applications C, 0.1 mg
MCA2595 MOUSE ANTI SUPEROXIDE DISMUTASE (Cu_Zn), Product Type Monoclonal Antibody, Specificity SUPEROXIDE DISMUTASE , Target Species Bovine, Host Mouse, Format Purified, Isotypes IgG1, Applications C, 0.1 mg
LF-MA0030 anti-Superoxide Dismutase 2 (2A1), Mouse monoclonal to Superoxide Dismutase 2, Isotype IgG1, Host Mouse 100 ul
LF-MA0035 anti-Superoxide Dismutase 2 (1E8) , Mouse monoclonal to Superoxide Dismutase 2, Isotype IgG2b, Host Mouse 100 ul
LF-MA0016 anti-Superoxide Dismutase 4 (2A1), Mouse monoclonal to Superoxide Dismutase 4, Isotype IgG1, Host Mouse 100 ul
LF-MA0042 anti-Superoxide Dismutase 4 (3A1), Mouse monoclonal to Superoxide Dismutase 4, Isotype IgG2a, Host Mouse 100 ul
LF-MA0029 anti-Superoxide Dismutase 1 (8A1), Mouse monoclonal to Superoxide Dismutase 1, Isotype IgG1, Host Mouse 100 ul
LF-PA10015 anti-Superoxide Dismutase 2, Mouse polyclonal to Superoxide Dismutase 2, Isotype , Host Mouse 50 ug
LF-PA0021 anti-Superoxide Dismutase 2, Rabbit polyclonal to Superoxide Dismutase 2, Isotype IgG, Host Rabbit 100 ul
LF-PA0013 anti-Superoxide Dismutase 1, Rabbit polyclonal to Superoxide Dismutase 1, Isotype IgG, Host Rabbit 100 ul
orb80178 Human Superoxide Dismutase (homodimer) protein Recombinant Human Cu_Zn Superoxide Dismutase produced in E.coli is homodimer, non-glycosylated polypeptide chain containing 2x 154 amino acids and having 100
8475-0204 NATIVE BOVINE SUPEROXIDE DISMUTASE, Product Type Purified Protein, Specificity SUPEROXIDE DISMUTASE, Target Species Bovine, Host N_A, Format Purified, Isotypes , Applications E, Clone 100 KU
SCH-8475-0204 NATIVE BOVINE SUPEROXIDE DISMUTASE, Product Type Purified Protein, Specificity SUPEROXIDE DISMUTASE, Target Species Bovine, Host N_A, Format Purified, Isotypes , Applications E, Clone 100 KU


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur