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_MACFA              Reviewed;         154 AA.
Q8HXQ1; Q2PFU5;
21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
31-JAN-2018, entry version 91.
RecName: Full=Superoxide dismutase [Cu-Zn];
EC=1.15.1.1;
Name=SOD1; ORFNames=QmoA-14762;
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9541;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=12383507; DOI=10.1016/S0378-1119(02)00837-5;
Fukuhara R., Tezuka T., Kageyama T.;
"Structure, molecular evolution, and gene expression of primate
superoxide dismutases.";
Gene 296:99-109(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Medulla oblongata;
Kobayashi M., Tanuma R., Hirata M., Osada N., Kusuda J., Sugano S.,
Hashimoto K.;
"Analysis of gene expression in cynomolgus monkey tissues by macaque
cDNA oligo-chips.";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Destroys radicals which are normally produced within the
cells and which are toxic to biological systems.
-!- 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};
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}.
-!- PTM: Palmitoylation helps nuclear targeting and decreases
catalytic activity. {ECO:0000250}.
-!- PTM: Succinylation, adjacent to copper catalytic site, probably
inhibits activity. Desuccinylation by SIRT5 enhances activity.
{ECO:0000250|UniProtKB:P00441}.
-!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB087270; BAC20349.1; -; mRNA.
EMBL; AB220492; BAE73025.1; -; mRNA.
RefSeq; NP_001272335.1; NM_001285406.1.
UniGene; Mfa.4588; -.
ProteinModelPortal; Q8HXQ1; -.
SMR; Q8HXQ1; -.
PRIDE; Q8HXQ1; -.
GeneID; 102118687; -.
KEGG; mcf:102118687; -.
CTD; 6647; -.
HOVERGEN; HBG000062; -.
KO; K04565; -.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0032839; C:dendrite cytoplasm; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005777; C:peroxisome; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0043234; C:protein complex; ISS:UniProtKB.
GO; GO:0051087; F:chaperone binding; ISS:UniProtKB.
GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0030346; F:protein phosphatase 2B binding; ISS:UniProtKB.
GO; GO:0048365; F:Rac GTPase binding; IEA:Ensembl.
GO; GO:0004784; F:superoxide dismutase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; ISS:UniProtKB.
GO; GO:0008089; P:anterograde axonal transport; IEA:Ensembl.
GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
GO; GO:0060088; P:auditory receptor cell stereocilium organization; ISS:UniProtKB.
GO; GO:0007569; P:cell aging; ISS:UniProtKB.
GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
GO; GO:0007566; P:embryo implantation; ISS:UniProtKB.
GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
GO; GO:0060047; P:heart contraction; ISS:UniProtKB.
GO; GO:0050665; P:hydrogen peroxide biosynthetic process; ISS:UniProtKB.
GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB.
GO; GO:0046716; P:muscle cell cellular homeostasis; ISS:UniProtKB.
GO; GO:0002262; P:myeloid cell homeostasis; ISS:UniProtKB.
GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; ISS:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0060052; P:neurofilament cytoskeleton organization; ISS:UniProtKB.
GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
GO; GO:0032287; P:peripheral nervous system myelin maintenance; ISS:UniProtKB.
GO; GO:0043085; P:positive regulation of catalytic activity; ISS:UniProtKB.
GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl.
GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
GO; GO:0043087; P:regulation of GTPase activity; IEA:Ensembl.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:UniProtKB.
GO; GO:0040014; P:regulation of multicellular organism growth; ISS:UniProtKB.
GO; GO:0045859; P:regulation of protein kinase activity; ISS:UniProtKB.
GO; GO:0060087; P:relaxation of vascular smooth muscle; ISS:UniProtKB.
GO; GO:0019430; P:removal of superoxide radicals; ISS:UniProtKB.
GO; GO:0048678; P:response to axon injury; ISS:UniProtKB.
GO; GO:0042493; P:response to drug; ISS:UniProtKB.
GO; GO:0045471; P:response to ethanol; ISS:UniProtKB.
GO; GO:0009408; P:response to heat; ISS:UniProtKB.
GO; GO:0042542; P:response to hydrogen peroxide; ISS:UniProtKB.
GO; GO:0010033; P:response to organic substance; ISS:UniProtKB.
GO; GO:0000303; P:response to superoxide; ISS:UniProtKB.
GO; GO:0001895; P:retina homeostasis; ISS:UniProtKB.
GO; GO:0008090; P:retrograde axonal transport; IEA:Ensembl.
GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
GO; GO:0042554; P:superoxide anion generation; IEA:Ensembl.
GO; GO:0006801; P:superoxide metabolic process; ISS:UniProtKB.
GO; GO:0019226; P:transmission of nerve impulse; ISS: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.
2: Evidence at transcript level;
Acetylation; Antioxidant; Copper; Cytoplasm; Disulfide bond;
Lipoprotein; Metal-binding; Nucleus; Oxidoreductase; Palmitate;
Phosphoprotein; Zinc.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P00442}.
CHAIN 2 154 Superoxide dismutase [Cu-Zn].
/FTId=PRO_0000164059.
METAL 47 47 Copper; catalytic. {ECO:0000250}.
METAL 49 49 Copper; catalytic. {ECO:0000250}.
METAL 64 64 Copper; catalytic. {ECO:0000250}.
METAL 64 64 Zinc; structural. {ECO:0000250}.
METAL 72 72 Zinc; structural. {ECO:0000250}.
METAL 81 81 Zinc; structural. {ECO:0000250}.
METAL 84 84 Zinc; structural. {ECO:0000250}.
METAL 121 121 Copper; catalytic. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P00442}.
MOD_RES 4 4 N6-succinyllysine.
{ECO:0000250|UniProtKB:P08228}.
MOD_RES 10 10 N6-succinyllysine.
{ECO:0000250|UniProtKB:P08228}.
MOD_RES 92 92 N6-succinyllysine.
{ECO:0000250|UniProtKB:P08228}.
MOD_RES 99 99 Phosphoserine.
{ECO:0000250|UniProtKB:P00441}.
MOD_RES 103 103 Phosphoserine.
{ECO:0000250|UniProtKB:P00441}.
MOD_RES 106 106 Phosphoserine.
{ECO:0000250|UniProtKB:P07632}.
MOD_RES 108 108 Phosphoserine.
{ECO:0000250|UniProtKB:P08228}.
MOD_RES 123 123 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00441}.
MOD_RES 123 123 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P00441}.
MOD_RES 137 137 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P08228}.
MOD_RES 137 137 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P08228}.
LIPID 7 7 S-palmitoyl cysteine. {ECO:0000250}.
DISULFID 58 147 {ECO:0000250}.
CONFLICT 46 46 F -> Y (in Ref. 2; BAE73025).
{ECO:0000305}.
CONFLICT 154 154 Q -> H (in Ref. 2; BAE73025).
{ECO:0000305}.
SEQUENCE 154 AA; 15983 MW; 7B77BC2ED8CDDC2F CRC64;
MAMKAVCVLK GDSPVQGTIN FEQKESNGPV KVWGSITGLT EGLHGFHVHQ FGDNTQGCTS
AGPHFNPLSR QHGGPKDEER HVGDLGNVTA GKDGVAKVSF EDSVISLSGD HSIIGRTLVV
HEKADDLGKG GNEESKKTGN AGGRLACGVI GIAQ


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