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Database: UniProt/SWISS-PROT
Entry: SODC_PANTR
LinkDB: SODC_PANTR
Original site: SODC_PANTR 
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   13-FEB-2019, entry version 123.
DE   RecName: Full=Superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1;
GN   Name=SOD1;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   superoxide 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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}.
CC   -!- PTM: Palmitoylation helps nuclear targeting and decreases
CC       catalytic 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}.
DR   EMBL; AB087266; BAC20345.1; -; mRNA.
DR   RefSeq; NP_001009025.1; NM_001009025.1.
DR   UniGene; Ptr.428; -.
DR   ProteinModelPortal; P60052; -.
DR   SMR; P60052; -.
DR   STRING; 9598.ENSPTRP00000023837; -.
DR   PaxDb; P60052; -.
DR   PRIDE; P60052; -.
DR   Ensembl; ENSPTRT00000025826; ENSPTRP00000023837; ENSPTRG00000013847.
DR   GeneID; 449637; -.
DR   KEGG; ptr:449637; -.
DR   CTD; 6647; -.
DR   VGNC; VGNC:14681; SOD1.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   GeneTree; ENSGT00940000155551; -.
DR   HOGENOM; HOG000263447; -.
DR   HOVERGEN; HBG000062; -.
DR   InParanoid; P60052; -.
DR   KO; K04565; -.
DR   OMA; MAMKAVC; -.
DR   OrthoDB; 1574423at2759; -.
DR   TreeFam; TF105131; -.
DR   Proteomes; UP000002277; Unplaced.
DR   Bgee; ENSPTRG00000013847; Expressed in 6 organ(s), highest expression level in liver.
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; ISS:UniProtKB.
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; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR   GO; GO:0051087; F:chaperone binding; 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:0048365; F:Rac GTPase binding; IEA:Ensembl.
DR   GO; GO:0004784; F:superoxide dismutase activity; ISS:UniProtKB.
DR   GO; GO:0016532; F:superoxide dismutase copper chaperone activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0000187; P:activation of MAPK activity; ISS:UniProtKB.
DR   GO; GO:0008089; P:anterograde axonal transport; IEA:Ensembl.
DR   GO; GO:0060088; P:auditory receptor cell stereocilium organization; ISS:UniProtKB.
DR   GO; GO:0007569; P:cell aging; ISS:UniProtKB.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0007566; P:embryo implantation; ISS:UniProtKB.
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: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: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:0060052; P:neurofilament cytoskeleton organization; ISS:UniProtKB.
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: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:0043087; P:regulation of GTPase activity; IEA:Ensembl.
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 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:0042493; P:response to drug; 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: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; -; 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; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 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; Complete proteome; Copper; Cytoplasm;
KW   Disulfide bond; Lipoprotein; Metal-binding; Nucleus; Oxidoreductase;
KW   Palmitate; Phosphoprotein; Reference proteome; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P00442}.
FT   CHAIN         2    154       Superoxide dismutase [Cu-Zn].
FT                                /FTId=PRO_0000164063.
FT   METAL        47     47       Copper; catalytic. {ECO:0000250}.
FT   METAL        49     49       Copper; catalytic. {ECO:0000250}.
FT   METAL        64     64       Copper; catalytic. {ECO:0000250}.
FT   METAL        64     64       Zinc; structural. {ECO:0000250}.
FT   METAL        72     72       Zinc; structural. {ECO:0000250}.
FT   METAL        81     81       Zinc; structural. {ECO:0000250}.
FT   METAL        84     84       Zinc; structural. {ECO:0000250}.
FT   METAL       121    121       Copper; catalytic. {ECO:0000250}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:P00442}.
FT   MOD_RES       4      4       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES      10     10       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES      92     92       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES      99     99       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P00441}.
FT   MOD_RES     103    103       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P00441}.
FT   MOD_RES     106    106       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P07632}.
FT   MOD_RES     108    108       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES     123    123       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P00441}.
FT   MOD_RES     123    123       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P00441}.
FT   MOD_RES     137    137       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES     137    137       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   LIPID         7      7       S-palmitoyl cysteine. {ECO:0000250}.
FT   DISULFID     58    147       {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
//
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