ID SODC_PANTR Reviewed; 154 AA. AC P60052; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 146. DE RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000250|UniProtKB:P00441}; DE EC=1.15.1.1 {ECO:0000250|UniProtKB:P00441}; GN Name=SOD1 {ECO:0000250|UniProtKB:P00441}; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pan. OX NCBI_TaxID=9598; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=12383507; DOI=10.1016/s0378-1119(02)00837-5; RA Fukuhara R., Tezuka T., Kageyama T.; RT "Structure, molecular evolution, and gene expression of primate superoxide RT dismutases."; RL Gene 296:99-109(2002). CC -!- FUNCTION: Destroys radicals which are normally produced within the CC cells and which are toxic to biological systems. CC -!- CATALYTIC ACTIVITY: 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 -!- 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 -!- SUBUNIT: Homodimer; non-disulfide-linked (By similarity). Heterodimer CC with SOD1. The heterodimer CCS:SOD1 interacts with SLC31A1; this CC heterotrimer is Cu(1+)-mediated and its maintenance is regulated CC through SOD1 activation (By similarity). {ECO:0000250|UniProtKB:P00441, CC ECO:0000250|UniProtKB:P08228}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. CC -!- PTM: Palmitoylation helps nuclear targeting and decreases catalytic CC activity. {ECO:0000250}. CC -!- PTM: Succinylation, adjacent to copper catalytic site, probably CC inhibits activity. Desuccinylation by SIRT5 enhances activity. CC {ECO:0000250|UniProtKB:P00441}. CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB087266; BAC20345.1; -; mRNA. DR RefSeq; NP_001009025.1; NM_001009025.1. DR AlphaFoldDB; P60052; -. DR BMRB; P60052; -. DR SMR; P60052; -. DR STRING; 9598.ENSPTRP00000023837; -. DR PaxDb; 9598-ENSPTRP00000023837; -. DR Ensembl; ENSPTRT00000025826.4; ENSPTRP00000023837.3; ENSPTRG00000013847.6. DR GeneID; 449637; -. DR KEGG; ptr:449637; -. DR VGNC; VGNC:14681; SOD1. DR eggNOG; KOG0441; Eukaryota. DR GeneTree; ENSGT00940000155551; -. DR HOGENOM; CLU_056632_4_1_1; -. DR InParanoid; P60052; -. DR OMA; AQRGFHI; -. DR OrthoDB; 3470597at2759; -. DR TreeFam; TF105131; -. DR Proteomes; UP000002277; Chromosome 21. DR Bgee; ENSPTRG00000013847; Expressed in primary visual cortex and 22 other cell types or tissues. DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0032839; C:dendrite cytoplasm; ISS:UniProtKB. DR GO; GO:0005615; C:extracellular space; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005777; C:peroxisome; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB. DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0030346; F:protein phosphatase 2B binding; ISS:UniProtKB. DR GO; GO:0051087; F:protein-folding chaperone binding; ISS:UniProtKB. DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl. DR GO; GO:0004784; F:superoxide dismutase activity; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0099610; P:action potential initiation; IEA:Ensembl. DR GO; GO:0008089; P:anterograde axonal transport; IEA:Ensembl. DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl. DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; ISS:UniProtKB. DR GO; GO:0008340; P:determination of adult lifespan; IEA:Ensembl. DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl. DR GO; GO:0007566; P:embryo implantation; ISS:UniProtKB. DR GO; GO:0010467; P:gene expression; IEA:Ensembl. DR GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB. DR GO; GO:0060047; P:heart contraction; ISS:UniProtKB. DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; ISS:UniProtKB. DR GO; GO:0006879; P:intracellular iron ion homeostasis; ISS:UniProtKB. DR GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB. DR GO; GO:0046716; P:muscle cell cellular homeostasis; ISS:UniProtKB. DR GO; GO:0002262; P:myeloid cell homeostasis; ISS:UniProtKB. DR GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; ISS:UniProtKB. DR GO; GO:0051093; P:negative regulation of developmental process; IEA:Ensembl. DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB. DR GO; GO:2000242; P:negative regulation of reproductive process; IEA:Ensembl. DR GO; GO:0060052; P:neurofilament cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0019228; P:neuronal action potential; IEA:Ensembl. DR GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB. DR GO; GO:0032287; P:peripheral nervous system myelin maintenance; ISS:UniProtKB. DR GO; GO:0043085; P:positive regulation of catalytic activity; ISS:UniProtKB. DR GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB. DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB. DR GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:0050766; P:positive regulation of phagocytosis; IEA:Ensembl. DR GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl. DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB. DR GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB. DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:UniProtKB. DR GO; GO:0040014; P:regulation of multicellular organism growth; ISS:UniProtKB. DR GO; GO:0045859; P:regulation of protein kinase activity; ISS:UniProtKB. DR GO; GO:0060087; P:relaxation of vascular associated smooth muscle; ISS:UniProtKB. DR GO; GO:0019430; P:removal of superoxide radicals; ISS:UniProtKB. DR GO; GO:0048678; P:response to axon injury; ISS:UniProtKB. DR GO; GO:0045471; P:response to ethanol; ISS:UniProtKB. DR GO; GO:0009408; P:response to heat; ISS:UniProtKB. DR GO; GO:0042542; P:response to hydrogen peroxide; ISS:UniProtKB. DR GO; GO:0010033; P:response to organic substance; ISS:UniProtKB. DR GO; GO:0000303; P:response to superoxide; ISS:UniProtKB. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0001895; P:retina homeostasis; ISS:UniProtKB. DR GO; GO:0008090; P:retrograde axonal transport; IEA:Ensembl. DR GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB. DR GO; GO:0042554; P:superoxide anion generation; IEA:Ensembl. DR GO; GO:0006801; P:superoxide metabolic process; ISS:UniProtKB. DR GO; GO:0019226; P:transmission of nerve impulse; ISS:UniProtKB. DR CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1. DR Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 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:SF103; SUPEROXIDE DISMUTASE [CU-ZN]; 1. DR PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1. DR Pfam; PF00080; Sod_Cu; 1. DR PRINTS; PR00068; CUZNDISMTASE. DR SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1. DR PROSITE; PS00087; SOD_CU_ZN_1; 1. DR PROSITE; PS00332; SOD_CU_ZN_2; 1. PE 2: Evidence at transcript level; KW Acetylation; Antioxidant; Copper; Cytoplasm; Disulfide bond; Lipoprotein; KW Metal-binding; Nucleus; Oxidoreductase; Palmitate; Phosphoprotein; KW Reference proteome; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P00442" FT CHAIN 2..154 FT /note="Superoxide dismutase [Cu-Zn]" FT /id="PRO_0000164063" FT BINDING 47 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 49 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 64 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 64 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250" FT BINDING 72 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250" FT BINDING 81 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250" FT BINDING 84 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250" FT BINDING 121 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P00442" FT MOD_RES 4 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P08228" FT MOD_RES 10 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P08228" FT MOD_RES 92 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P08228" FT MOD_RES 99 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P00441" FT MOD_RES 103 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P00441" FT MOD_RES 106 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07632" FT MOD_RES 108 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P08228" FT MOD_RES 123 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P00441" FT MOD_RES 123 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P00441" FT MOD_RES 137 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08228" FT MOD_RES 137 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08228" FT LIPID 7 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT DISULFID 58..147 FT /evidence="ECO:0000250" SQ SEQUENCE 154 AA; 15936 MW; 25CA38DA8D564483 CRC64; MATKAVCVLK GDGPVQGIIN FEQKESNGPV KVWGSIKGLT EGLHGFHVHE FGDNTAGCTS AGPHFNPLSR KHGGPKDEER HVGDLGNVTA DKDGVADVSI EDSVISLSGD HCIIGRTLVV HEKADDLGKG GNEESTKTGN AGSRLACGVI GIAQ //