ID   SODM_RABIT              Reviewed;         202 AA.
AC   P41982;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE            EC=1.15.1.1;
DE   Flags: Precursor; Fragment;
GN   Name=SOD2;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand white;
RA   Jackson R.M.;
RL   Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
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; L28808; AAA31401.1; -; mRNA.
DR   AlphaFoldDB; P41982; -.
DR   SMR; P41982; -.
DR   InParanoid; P41982; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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; IPR019833; Mn/Fe_SOD_BS.
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   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Manganese; Metal-binding; Mitochondrion; Nitration;
KW   Oxidoreductase; Reference proteome; Transit peptide; Ubl conjugation.
FT   TRANSIT         <1..5
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           6..>202
FT                   /note="Superoxide dismutase [Mn], mitochondrial"
FT                   /id="PRO_0000032873"
FT   BINDING         31
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         39
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P04179"
FT   MOD_RES         49
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P04179"
FT   MOD_RES         49
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P09671"
FT   MOD_RES         95
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09671"
FT   MOD_RES         103
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P09671"
FT   MOD_RES         103
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P09671"
FT   MOD_RES         111
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P04179"
FT   MOD_RES         111
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P09671"
FT   MOD_RES         183
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09671"
FT   NON_TER         1
FT   NON_TER         202
SQ   SEQUENCE   202 AA;  22656 MW;  6F1BB8DA15C33AA7 CRC64;
     HGRGMKHSLP DLPYDYGALE PHINAQIMEL HHSKHHAAYV NNLNATEEKY REALARGDVT
     AHVALQPALK FKGGGHINHT IFWTNLSPNG GGEPKGELLE AIKRDFGSFD KFKERLTAVS
     VGVQGSGWGW LGFNKEQGHL QIAACANQDP LQGTTGLIPL LGIDVWEHAY YLQYKNVRPD
     YLKAIWNVIT WENVTERYMA CK