LinkDB: SODC_PIG D9D839_PIG
Original site: SODC_PIG D9D839_PIG
ID SODC_PIG Reviewed; 153 AA. AC P04178; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 168. 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 Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP PROTEIN SEQUENCE OF 2-153, AND ACETYLATION AT ALA-2. RX PubMed=3891411; DOI=10.1016/0014-5793(85)80722-5; RA Schinina M.E., Barra D., Simmaco M., Bossa F., Rotilio G.; RT "Primary structure of porcine Cu,Zn superoxide dismutase."; RL FEBS Lett. 186:267-270(1985). 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. 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 PIR; A00514; DSPGCZ. DR RefSeq; NP_001177351.1; NM_001190422.1. DR AlphaFoldDB; P04178; -. DR SMR; P04178; -. DR STRING; 9823.ENSSSCP00000026815; -. DR iPTMnet; P04178; -. DR PaxDb; 9823-ENSSSCP00000026815; -. DR PeptideAtlas; P04178; -. DR Ensembl; ENSSSCT00025029544.1; ENSSSCP00025012561.1; ENSSSCG00025021718.1. DR Ensembl; ENSSSCT00035075531.1; ENSSSCP00035030755.1; ENSSSCG00035056538.1. DR Ensembl; ENSSSCT00045037084.1; ENSSSCP00045025801.1; ENSSSCG00045021700.1. DR Ensembl; ENSSSCT00050072256.1; ENSSSCP00050031075.1; ENSSSCG00050053056.1. DR Ensembl; ENSSSCT00055038009.1; ENSSSCP00055030202.1; ENSSSCG00055019424.1. DR Ensembl; ENSSSCT00065090983.1; ENSSSCP00065039821.1; ENSSSCG00065066291.1. DR Ensembl; ENSSSCT00070028574.1; ENSSSCP00070023804.1; ENSSSCG00070014563.1. DR GeneID; 397036; -. DR KEGG; ssc:397036; -. DR eggNOG; KOG0441; Eukaryota. DR HOGENOM; CLU_056632_4_1_1; -. DR InParanoid; P04178; -. DR OrthoDB; 3470597at2759; -. DR TreeFam; TF105131; -. DR Reactome; R-SSC-114608; Platelet degranulation. DR Reactome; R-SSC-3299685; Detoxification of Reactive Oxygen Species. DR Proteomes; UP000008227; Unplaced. DR Proteomes; UP000314985; Chromosome 13. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. DR Genevisible; P04178; SS. 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:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005777; C:peroxisome; IBA:GO_Central. DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB. DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB. 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:0004784; F:superoxide dismutase activity; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; 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: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: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:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB. 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:0001895; P:retina homeostasis; ISS:UniProtKB. DR GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB. 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 1: Evidence at protein level; KW Acetylation; Antioxidant; Copper; Cytoplasm; Direct protein sequencing; KW Disulfide bond; Lipoprotein; Metal-binding; Nucleus; Oxidoreductase; KW Palmitate; Phosphoprotein; Reference proteome; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:3891411" FT CHAIN 2..153 FT /note="Superoxide dismutase [Cu-Zn]" FT /id="PRO_0000164064" FT REGION 56..80 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 46 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 48 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 63 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 63 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250" FT BINDING 71 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250" FT BINDING 80 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250" FT BINDING 83 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250" FT BINDING 120 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:0000269|PubMed:3891411" 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 91 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P08228" FT MOD_RES 102 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P00441" FT MOD_RES 107 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P08228" FT MOD_RES 122 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P00441" FT MOD_RES 122 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P00441" FT MOD_RES 136 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08228" FT MOD_RES 136 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 57..146 SQ SEQUENCE 153 AA; 15892 MW; 06B625E7D96DA318 CRC64; MATKAVCVLK GDGPVQGTIY FELKGEKTVL VTGTIKGLAE GDHGFHVHQF GDNTQGCTSA GPHFNPESKK HGGPKDQERH VGDLGNVTAG KDGVATVYIE DSVIALSGDH SIIGRTMVVH EKPDDLGRGG NEESTKTGNA GSRLACGVIG ITQ //
ID D9D839_PIG Unreviewed; 153 AA. AC D9D839; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAR-2024, entry version 91. DE RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|ARBA:ARBA00020928, ECO:0000256|RuleBase:RU000393}; DE EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000393}; GN Name=SOD1 {ECO:0000313|EMBL:ADI47520.1}; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823 {ECO:0000313|EMBL:ADI47520.1}; RN [1] {ECO:0000313|EMBL:AHW83665.1} RP NUCLEOTIDE SEQUENCE. RA Liu H., Li X., Mao Y., Miao S., Yan Z., Dong H.; RT "Electronic cloning and verification of cDNA of Sus scrofa."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADI47520.1} RP NUCLEOTIDE SEQUENCE. RA Du J.F., Zeng Y.Q., Wang H.; RT "The effect of CuZnSOD mRNA expression on muscle anti-oxidative activity RT and meat quality in pigs."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Destroys radicals which are normally produced within the CC cells and which are toxic to biological systems. CC {ECO:0000256|ARBA:ARBA00003917, ECO:0000256|RuleBase:RU000393}. 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 Evidence={ECO:0000256|RuleBase:RU000393}; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000256|RuleBase:RU000393}; CC Note=Binds 1 copper ion per subunit. {ECO:0000256|RuleBase:RU000393}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|RuleBase:RU000393}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU000393}; 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. {ECO:0000256|ARBA:ARBA00035019}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family. CC {ECO:0000256|ARBA:ARBA00010457, ECO:0000256|RuleBase:RU000393}. 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; GU944822; ADI47520.1; -; mRNA. DR EMBL; GQ913661; AHW83665.1; -; mRNA. DR RefSeq; NP_001177351.1; NM_001190422.1. DR AlphaFoldDB; D9D839; -. DR SMR; D9D839; -. DR GeneID; 397036; -. DR KEGG; ssc:397036; -. DR HOGENOM; CLU_056632_4_1_1; -. DR OrthoDB; 3470597at2759; -. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC. 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 Copper {ECO:0000256|RuleBase:RU000393}; KW Lipoprotein {ECO:0000256|ARBA:ARBA00023139}; KW Metal-binding {ECO:0000256|RuleBase:RU000393}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000393}; KW Palmitate {ECO:0000256|ARBA:ARBA00023139}; KW Zinc {ECO:0000256|RuleBase:RU000393}. FT DOMAIN 15..149 FT /note="Superoxide dismutase copper/zinc binding" FT /evidence="ECO:0000259|Pfam:PF00080" FT REGION 56..80 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 153 AA; 15892 MW; 06B625E7D96DA318 CRC64; MATKAVCVLK GDGPVQGTIY FELKGEKTVL VTGTIKGLAE GDHGFHVHQF GDNTQGCTSA GPHFNPESKK HGGPKDQERH VGDLGNVTAG KDGVATVYIE DSVIALSGDH SIIGRTMVVH EKPDDLGRGG NEESTKTGNA GSRLACGVIG ITQ //