SODM_CAVPO
ID SODM_CAVPO Reviewed; 211 AA.
AC P49114;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE EC=1.15.1.1;
DE Flags: Precursor; Fragment;
GN Name=SOD2;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hartley; TISSUE=Lung;
RX PubMed=8597602; DOI=10.1016/0167-4781(95)00214-6;
RA Yuan H.T., Bingle C.D., Kelly F.J.;
RT "Differential patterns of antioxidant enzyme mRNA expression in guinea pig
RT lung and liver during development.";
RL Biochim. Biophys. Acta 1305:163-171(1996).
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; U39843; AAC52719.1; -; mRNA.
DR PIR; S65795; S65795.
DR AlphaFoldDB; P49114; -.
DR SMR; P49114; -.
DR STRING; 10141.ENSCPOP00000017103; -.
DR PRIDE; P49114; -.
DR eggNOG; KOG0876; Eukaryota.
DR InParanoid; P49114; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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 GO; GO:0001315; P:age-dependent response to reactive oxygen species; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; 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..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 25..>211
FT /note="Superoxide dismutase [Mn], mitochondrial"
FT /id="PRO_0000032867"
FT BINDING 50
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT MOD_RES 58
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P04179"
FT MOD_RES 68
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04179"
FT MOD_RES 68
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09671"
FT MOD_RES 75
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09671"
FT MOD_RES 75
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09671"
FT MOD_RES 114
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09671"
FT MOD_RES 122
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09671"
FT MOD_RES 122
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09671"
FT MOD_RES 130
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04179"
FT MOD_RES 130
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09671"
FT MOD_RES 202
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09671"
FT NON_TER 211
SQ SEQUENCE 211 AA; 23236 MW; 2032559161993E2D CRC64;
MLCRAVCSAS RRLAPALGIL GVRQKHSLPD LPYDYGALQP HINAEIMQLH HSKHHAAYLN
NLNIAEEKYQ EALAKGDVTA QVALQPALKF NGGGHINHSI FWTNLSPNGG GEPKGELLEA
IKRDFGSFDK FKEKLTAVSV GVQGSGWGWL GFNKERGCLQ IAACSNQDPL QGTTGLIPLL
GIDVWEHAYY LQLKNVRPDY LKAIWKVIKN S
