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Database: UniProt/SWISS-PROT
Entry: SODM_CALJA
LinkDB: SODM_CALJA
Original site: SODM_CALJA 
ID   SODM_CALJA              Reviewed;         198 AA.
AC   Q8HXP0;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   21-NOV-2003, sequence version 2.
DT   25-APR-2018, entry version 80.
DE   RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE            EC=1.15.1.1;
GN   Name=SOD2;
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
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-98 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=BAC20360.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR   EMBL; AB087281; BAC20360.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001254675.1; NM_001267746.1.
DR   ProteinModelPortal; Q8HXP0; -.
DR   SMR; Q8HXP0; -.
DR   STRING; 9483.ENSCJAP00000021521; -.
DR   PRIDE; Q8HXP0; -.
DR   GeneID; 100410185; -.
DR   KEGG; cjc:100410185; -.
DR   CTD; 6648; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   HOVERGEN; HBG004451; -.
DR   InParanoid; Q8HXP0; -.
DR   KO; K04564; -.
DR   Proteomes; UP000008225; 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   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; 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; Complete proteome; Manganese; Metal-binding;
KW   Mitochondrion; Nitration; Oxidoreductase; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN         1    198       Superoxide dismutase [Mn], mitochondrial.
FT                                /FTId=PRO_0000159949.
FT   METAL        26     26       Manganese. {ECO:0000250}.
FT   METAL        74     74       Manganese. {ECO:0000250}.
FT   METAL       159    159       Manganese. {ECO:0000250}.
FT   METAL       163    163       Manganese. {ECO:0000250}.
FT   MOD_RES      34     34       Nitrated tyrosine.
FT                                {ECO:0000250|UniProtKB:P04179}.
FT   MOD_RES      44     44       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P04179}.
FT   MOD_RES      44     44       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P09671}.
FT   MOD_RES      51     51       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P09671}.
FT   MOD_RES      51     51       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P09671}.
FT   MOD_RES      90     90       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P09671}.
FT   MOD_RES      98     98       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P09671}.
FT   MOD_RES      98     98       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P09671}.
FT   MOD_RES     106    106       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P04179}.
FT   MOD_RES     106    106       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P09671}.
FT   MOD_RES     178    178       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P09671}.
SQ   SEQUENCE   198 AA;  22248 MW;  E7F8860B8C56F2CA CRC64;
     KHSLPDLPYD YGALEPHINA QIMQLHHSKH HAAYVNNLND TEEKYKEALA KGDVTAQIAL
     QPALKFNGGG HINHSIFWTN LSPNGGGEPK GELLEAIKRD FGSFDKFKER LTAASVGVQG
     SGWGWLGFNK ERGHLQIAAC PNQDPLQGTT GLIPLLGIDV WEHAYYLQYK NVRPDYLKAI
     WNVINWENVT ERYMACKK
//
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