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Superoxide dismutase [Cu-Zn] (EC 1.15.1.1)

 SODC_RABIT              Reviewed;         153 AA.
P09212;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 131.
RecName: Full=Superoxide dismutase [Cu-Zn];
EC=1.15.1.1;
Name=SOD1;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=New Zealand white; TISSUE=Lung;
Jackson R.M., Ho Y.;
Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases.
[2]
PROTEIN SEQUENCE OF 2-153.
PubMed=3214553;
Reinecke K., Wolf B., Michelson A.M., Pugrt K., Steffens G.J.,
Flohe L.;
"The amino-acid sequence of rabbit Cu-Zn superoxide dismutase.";
Biol. Chem. Hoppe-Seyler 369:715-725(1988).
-!- 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.
-!- SUBCELLULAR LOCATION: Cytoplasm. 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}.
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EMBL; Z22644; CAA80357.1; -; mRNA.
PIR; S33162; S33162.
RefSeq; NP_001076096.1; NM_001082627.1.
UniGene; Ocu.2588; -.
ProteinModelPortal; P09212; -.
SMR; P09212; -.
PRIDE; P09212; -.
GeneID; 100009313; -.
KEGG; ocu:100009313; -.
CTD; 6647; -.
HOGENOM; HOG000263447; -.
HOVERGEN; HBG000062; -.
InParanoid; P09212; -.
KO; K04565; -.
Proteomes; UP000001811; Unplaced.
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:0031012; C:extracellular matrix; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0030346; F:protein phosphatase 2B binding; ISS:UniProtKB.
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: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:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
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:0007605; P:sensory perception of sound; ISS:UniProtKB.
GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
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; PS00332; SOD_CU_ZN_2; 1.
1: Evidence at protein level;
Acetylation; Antioxidant; Complete proteome; Copper; Cytoplasm;
Direct protein sequencing; Disulfide bond; Lipoprotein; Metal-binding;
Nucleus; Oxidoreductase; Palmitate; Phosphoprotein;
Reference proteome; Zinc.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P00442,
ECO:0000269|PubMed:3214553}.
CHAIN 2 153 Superoxide dismutase [Cu-Zn].
/FTId=PRO_0000164066.
METAL 46 46 Copper; catalytic. {ECO:0000250}.
METAL 48 48 Copper; catalytic. {ECO:0000250}.
METAL 63 63 Copper; catalytic. {ECO:0000250}.
METAL 63 63 Zinc; structural. {ECO:0000250}.
METAL 71 71 Zinc; structural. {ECO:0000250}.
METAL 80 80 Zinc; structural. {ECO:0000250}.
METAL 83 83 Zinc; structural. {ECO:0000250}.
METAL 120 120 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 102 102 Phosphoserine.
{ECO:0000250|UniProtKB:P00441}.
MOD_RES 105 105 Phosphoserine.
{ECO:0000250|UniProtKB:P07632}.
MOD_RES 107 107 Phosphoserine.
{ECO:0000250|UniProtKB:P08228}.
MOD_RES 122 122 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00441}.
MOD_RES 122 122 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P00441}.
MOD_RES 136 136 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P08228}.
MOD_RES 136 136 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P08228}.
LIPID 7 7 S-palmitoyl cysteine. {ECO:0000250}.
DISULFID 57 146 {ECO:0000250}.
CONFLICT 17 17 A -> G (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 44 44 E -> G (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 54 54 R -> T (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 152 152 S -> A (in Ref. 2; AA sequence).
{ECO:0000305}.
SEQUENCE 153 AA; 15819 MW; B0A9C8DB56951EC9 CRC64;
MATKAVCVLK GDGPVEATIH FEQKGTGPVV VKGRITGLTE GLHEFHVHQF GDNRQGCTSA
GPHFNPLSKK HGGPKDEERH VGDLGNVTAG SNGVADVLIE DSVISLSGDM SVIGRTLVVH
EKEDDLGKGG NDESTKTGNA GSRLACGVIG ISP


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