SODC_SHEEP
ID SODC_SHEEP Reviewed; 152 AA.
AC P09670;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1;
GN Name=SOD1;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP PROTEIN SEQUENCE OF 2-152.
RX PubMed=3770194; DOI=10.1016/0014-5793(86)80003-5;
RA Schinina M.E., Barra D., Gentilomo S., Bossa F., Capo C., Rotilio G.,
RA Calabrese L.;
RT "Primary structure of a cationic Cu,Zn superoxide dismutase. The sheep
RT enzyme.";
RL FEBS Lett. 207:7-10(1986).
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; A24475; A24475.
DR AlphaFoldDB; P09670; -.
DR SMR; P09670; -.
DR STRING; 9940.ENSOARP00000004609; -.
DR Ensembl; ENSOART00000004690; ENSOARP00000004609; ENSOARG00000004311.
DR Ensembl; ENSOART00000008577; ENSOARP00000008454; ENSOARG00000007880.
DR Ensembl; ENSOART00020002019; ENSOARP00020001683; ENSOARG00020001337.
DR eggNOG; KOG0441; Eukaryota.
DR HOGENOM; CLU_056632_4_1_1; -.
DR OMA; AQRGFHI; -.
DR OrthoDB; 1574423at2759; -.
DR Proteomes; UP000002356; Chromosome 1.
DR Proteomes; UP000002356; Chromosome 11.
DR Bgee; ENSOARG00000004311; Expressed in adult mammalian kidney and 56 other tissues.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0051087; F:chaperone binding; IEA:Ensembl.
DR GO; GO:0005507; F:copper ion binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0030346; F:protein phosphatase 2B binding; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0007568; P:aging; 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; IEA:Ensembl.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:Ensembl.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl.
DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:Ensembl.
DR GO; GO:0060047; P:heart contraction; IEA:Ensembl.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
DR GO; GO:0002262; P:myeloid cell homeostasis; IEA:Ensembl.
DR GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:2000242; P:negative regulation of reproductive process; IEA:Ensembl.
DR GO; GO:0060052; P:neurofilament cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
DR GO; GO:0032287; P:peripheral nervous system myelin maintenance; IEA:Ensembl.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IEA:Ensembl.
DR GO; GO:0001819; P:positive regulation of cytokine production; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:Ensembl.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IEA:Ensembl.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:0045859; P:regulation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0060087; P:relaxation of vascular associated smooth muscle; IEA:Ensembl.
DR GO; GO:0019430; P:removal of superoxide radicals; ISS:UniProtKB.
DR GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0009408; P:response to heat; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0001895; P:retina homeostasis; IEA:Ensembl.
DR GO; GO:0008090; P:retrograde axonal transport; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0042554; P:superoxide anion generation; IEA:Ensembl.
DR GO; GO:0019226; P:transmission of nerve impulse; IEA:Ensembl.
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:0000250|UniProtKB:P00442,
FT ECO:0000269|PubMed:3770194"
FT CHAIN 2..152
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000164068"
FT REGION 53..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 119
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 90
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08228"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07632"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08228"
FT MOD_RES 121
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00441"
FT MOD_RES 121
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00441"
FT MOD_RES 135
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08228"
FT MOD_RES 135
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 56..145
SQ SEQUENCE 152 AA; 15695 MW; B02570762B5E0932 CRC64;
MATKAVCVLK GDGPVQGTIR FEAKGDKVVV TGSITGLTEG DHGFHVHQFG DNTQGCTSAG
PHFNPLSKKH GGPKDEERHV GDLGNVKADK NGVAIVDIVD PLISLSGEYS IIGRTMVVHE
KPDDLGRGGN EESTKTGNAG GRLACGVIGI AP
