SODM_PIG
ID SODM_PIG Reviewed; 144 AA.
AC P28768;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE EC=1.15.1.1;
DE Flags: Fragment;
GN Name=SOD2;
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 NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=1556751; DOI=10.1007/bf00182394;
RA Smith M.W., Doolittle R.F.;
RT "A comparison of evolutionary rates of the two major kinds of superoxide
RT dismutase.";
RL J. Mol. Evol. 34:175-184(1992).
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
CC {ECO:0000250|UniProtKB:P07895}.
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=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P04179};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:P04179};
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- PTM: Nitrated under oxidative stress. Nitration coupled with oxidation
CC inhibits the catalytic activity. {ECO:0000250|UniProtKB:P07895}.
CC -!- PTM: Acetylation at Lys-122 decreases enzymatic activity. Deacetylated
CC by SIRT3 upon exposure to ionizing radiations or after long fasting (By
CC similarity). {ECO:0000250|UniProtKB:P04179}.
CC -!- PTM: Polyubiquitinated; leading to proteasomal degradation.
CC Deubiquitinated by USP36 which increases protein stability.
CC {ECO:0000250|UniProtKB:P04179}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; X64057; CAA45413.1; -; mRNA.
DR PIR; S23661; S23661.
DR AlphaFoldDB; P28768; -.
DR SMR; P28768; -.
DR STRING; 9823.ENSSSCP00000027960; -.
DR PaxDb; P28768; -.
DR PeptideAtlas; P28768; -.
DR PRIDE; P28768; -.
DR eggNOG; KOG0876; Eukaryota.
DR InParanoid; P28768; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0004784; F:superoxide dismutase activity; ISS:UniProtKB.
DR Gene3D; 1.10.287.990; -; 1.
DR Gene3D; 3.55.40.20; -; 1.
DR InterPro; IPR001189; Mn/Fe_SOD.
DR InterPro; IPR019832; Mn/Fe_SOD_C.
DR InterPro; IPR019831; Mn/Fe_SOD_N.
DR InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR InterPro; IPR036314; SOD_C_sf.
DR Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 1.
DR PRINTS; PR01703; MNSODISMTASE.
DR SUPFAM; SSF46609; SSF46609; 1.
DR SUPFAM; SSF54719; SSF54719; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Manganese; Metal-binding; Mitochondrion; Nitration;
KW Oxidoreductase; Reference proteome; Ubl conjugation.
FT CHAIN <1..>144
FT /note="Superoxide dismutase [Mn], mitochondrial"
FT /id="PRO_0000159957"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT MOD_RES 18
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P04179"
FT MOD_RES 28
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04179"
FT MOD_RES 28
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09671"
FT MOD_RES 35
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09671"
FT MOD_RES 35
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09671"
FT MOD_RES 74
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09671"
FT MOD_RES 82
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09671"
FT MOD_RES 82
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09671"
FT MOD_RES 90
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04179"
FT MOD_RES 90
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09671"
FT NON_TER 1
FT NON_TER 144
SQ SEQUENCE 144 AA; 15639 MW; E12DDA154F3302B1 CRC64;
HINAQIMQLH HSEHHAAYVN NLNVVEEKYQ EALKKGDVTA QVALQPALKF NGGGHINHSI
FWTNLSPNGG GEPKGELLEA IKRDFGSFEK FKEKLTAVSV GVQGSGWGWL GFNKEQGRLQ
IAACSNQDPL QGTTGLVPLL GIDV
