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Database: UniProt
Entry: P28768
LinkDB: P28768
Original site: P28768 
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   05-DEC-2018, entry version 104.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RX   PubMed=1556751;
RA   Smith M.W., Doolittle R.F.;
RT   "A comparison of evolutionary rates of the two major kinds of
RT   superoxide 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
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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
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}.
DR   EMBL; X64057; CAA45413.1; -; mRNA.
DR   PIR; S23661; S23661.
DR   UniGene; Ssc.17042; -.
DR   ProteinModelPortal; P28768; -.
DR   SMR; P28768; -.
DR   STRING; 9823.ENSSSCP00000027960; -.
DR   PaxDb; P28768; -.
DR   PeptideAtlas; P28768; -.
DR   PRIDE; P28768; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   HOVERGEN; HBG004451; -.
DR   InParanoid; P28768; -.
DR   Proteomes; UP000008227; 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:0046872; F:metal ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; ISS:UniProtKB.
DR   GO; GO:0007568; P:aging; IBA:GO_Central.
DR   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 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; Complete proteome; Manganese; Metal-binding;
KW   Mitochondrion; Nitration; Oxidoreductase; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN        <1   >144       Superoxide dismutase [Mn], mitochondrial.
FT                                /FTId=PRO_0000159957.
FT   METAL        10     10       Manganese. {ECO:0000250}.
FT   METAL        58     58       Manganese. {ECO:0000250}.
FT   METAL       143    143       Manganese. {ECO:0000250}.
FT   MOD_RES      18     18       Nitrated tyrosine.
FT                                {ECO:0000250|UniProtKB:P04179}.
FT   MOD_RES      28     28       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P04179}.
FT   MOD_RES      28     28       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P09671}.
FT   MOD_RES      35     35       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P09671}.
FT   MOD_RES      35     35       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P09671}.
FT   MOD_RES      74     74       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P09671}.
FT   MOD_RES      82     82       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P09671}.
FT   MOD_RES      82     82       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P09671}.
FT   MOD_RES      90     90       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P04179}.
FT   MOD_RES      90     90       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P09671}.
FT   NON_TER       1      1
FT   NON_TER     144    144
SQ   SEQUENCE   144 AA;  15639 MW;  E12DDA154F3302B1 CRC64;
     HINAQIMQLH HSEHHAAYVN NLNVVEEKYQ EALKKGDVTA QVALQPALKF NGGGHINHSI
     FWTNLSPNGG GEPKGELLEA IKRDFGSFEK FKEKLTAVSV GVQGSGWGWL GFNKEQGRLQ
     IAACSNQDPL QGTTGLVPLL GIDV
//
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