ID SODM_MACFA Reviewed; 222 AA.
AC Q8HXP3; Q2PFT1;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 3.
DT 13-FEB-2019, entry version 82.
DE RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=SOD2; ORFNames=QnpA-14761;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Parietal cortex;
RA Kobayashi M., Tanuma R., Hirata M., Osada N., Kusuda J., Sugano S.,
RA Hashimoto K.;
RT "Analysis of gene expression in cynomolgus monkey tissues by macaque
RT cDNA oligo-chips.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-222.
RX PubMed=12383507; DOI=10.1016/S0378-1119(02)00837-5;
RA Fukuhara R., Tezuka T., Kageyama T.;
RT "Structure, molecular evolution, and gene expression of primate
RT superoxide dismutases.";
RL Gene 296:99-109(2002).
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological
CC systems. {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.
CC {ECO:0000250|UniProtKB:P04179};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- PTM: Nitrated under oxidative stress. Nitration coupled with
CC oxidation inhibits the catalytic activity.
CC {ECO:0000250|UniProtKB:P07895}.
CC -!- PTM: Acetylation at Lys-122 decreases enzymatic activity.
CC Deacetylated by SIRT3 upon exposure to ionizing radiations or
CC after long fasting (By similarity).
CC {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
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC20357.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR EMBL; AB220506; BAE73039.1; -; mRNA.
DR EMBL; AB087278; BAC20357.1; ALT_INIT; mRNA.
DR RefSeq; NP_001274560.1; NM_001287631.1.
DR RefSeq; XP_005551576.1; XM_005551519.2.
DR RefSeq; XP_015303876.1; XM_015448390.1.
DR UniGene; Mfa.5336; -.
DR ProteinModelPortal; Q8HXP3; -.
DR SMR; Q8HXP3; -.
DR PRIDE; Q8HXP3; -.
DR Ensembl; ENSMFAT00000014537; ENSMFAP00000040270; ENSMFAG00000046278.
DR GeneID; 102123902; -.
DR KEGG; mcf:102123902; -.
DR CTD; 6648; -.
DR GeneTree; ENSGT00390000011877; -.
DR HOVERGEN; HBG004451; -.
DR KO; K04564; -.
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 GO; GO:0006801; P:superoxide metabolic process; ISS:UniProtKB.
DR Gene3D; 1.10.287.990; -; 1.
DR Gene3D; 2.40.500.20; -; 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; Transit peptide; Ubl conjugation.
FT TRANSIT 1 24 Mitochondrion. {ECO:0000250}.
FT CHAIN 25 222 Superoxide dismutase [Mn], mitochondrial.
FT /FTId=PRO_0000159953.
FT METAL 50 50 Manganese. {ECO:0000250}.
FT METAL 98 98 Manganese. {ECO:0000250}.
FT METAL 183 183 Manganese. {ECO:0000250}.
FT METAL 187 187 Manganese. {ECO:0000250}.
FT MOD_RES 58 58 Nitrated tyrosine.
FT {ECO:0000250|UniProtKB:P04179}.
FT MOD_RES 68 68 N6-acetyllysine; alternate.
FT {ECO:0000250|UniProtKB:P04179}.
FT MOD_RES 68 68 N6-succinyllysine; alternate.
FT {ECO:0000250|UniProtKB:P09671}.
FT MOD_RES 75 75 N6-acetyllysine; alternate.
FT {ECO:0000250|UniProtKB:P09671}.
FT MOD_RES 75 75 N6-succinyllysine; alternate.
FT {ECO:0000250|UniProtKB:P09671}.
FT MOD_RES 114 114 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P09671}.
FT MOD_RES 122 122 N6-acetyllysine; alternate.
FT {ECO:0000250|UniProtKB:P09671}.
FT MOD_RES 122 122 N6-succinyllysine; alternate.
FT {ECO:0000250|UniProtKB:P09671}.
FT MOD_RES 130 130 N6-acetyllysine; alternate.
FT {ECO:0000250|UniProtKB:P04179}.
FT MOD_RES 130 130 N6-succinyllysine; alternate.
FT {ECO:0000250|UniProtKB:P09671}.
FT MOD_RES 202 202 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P09671}.
SQ SEQUENCE 222 AA; 24697 MW; C9F1A0FC5902B434 CRC64;
MLSRAVCGTG RQLAPALGYL GSRQKHSLPD LPYDYGALEP HINAQIMQLH HSKHHAAYVN
NLNVTEEKYQ EALAKGDVTA QIALQPALKF NGGGHINHSI FWTNLSPNGG GEPKGELLEA
IKRDFGSFEK FKEKLTAASV GVQGSGWGWL GFNKERGQLQ IAACPNQDPL QGTTGLIPLL
GIDVWEHAYY LQYKNVRPDY LKAIWNVINW ENVTERYMAC KK
//
