SODC_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 03-AUG-2022, entry version 160.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1;
GN Name=SOD1;
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.
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}.
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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; P04178; -.
DR PeptideAtlas; P04178; -.
DR PRIDE; P04178; -.
DR Ensembl; ENSSSCT00025029544; ENSSSCP00025012561; ENSSSCG00025021718.
DR Ensembl; ENSSSCT00035075531; ENSSSCP00035030755; ENSSSCG00035056538.
DR Ensembl; ENSSSCT00045037084; ENSSSCP00045025801; ENSSSCG00045021700.
DR Ensembl; ENSSSCT00050072256; ENSSSCP00050031075; ENSSSCG00050053056.
DR Ensembl; ENSSSCT00055038009; ENSSSCP00055030202; ENSSSCG00055019424.
DR Ensembl; ENSSSCT00065090983; ENSSSCP00065039821; ENSSSCG00065066291.
DR Ensembl; ENSSSCT00070028574; ENSSSCP00070023804; ENSSSCG00070014563.
DR GeneID; 397036; -.
DR KEGG; ssc:397036; -.
DR CTD; 6647; -.
DR eggNOG; KOG0441; Eukaryota.
DR HOGENOM; CLU_056632_4_1_1; -.
DR InParanoid; P04178; -.
DR OrthoDB; 1574423at2759; -.
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 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:0051087; F:chaperone binding; 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: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: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: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; -; 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 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
