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Database: UniProt/SWISS-PROT
Entry: SODC_CAPHI
LinkDB: SODC_CAPHI
Original site: SODC_CAPHI 
ID   SODC_CAPHI              Reviewed;         152 AA.
AC   Q5FB29;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-OCT-2017, entry version 75.
DE   RecName: Full=Superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1;
GN   Name=SOD1;
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Caprinae; Capra.
OX   NCBI_TaxID=9925;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Fukuhara R., Kageyama T.;
RT   "Mammalian superoxide dismutase.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}.
CC   -!- PTM: Palmitoylation helps nuclear targeting and decreases
CC       catalytic activity. {ECO:0000250}.
CC   -!- PTM: Succinylation, adjacent to copper catalytic site, probably
CC       inhibits activity. Desuccinylation by SIRT5 enhances activity.
CC       {ECO:0000250|UniProtKB:P00441}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
DR   EMBL; AB201469; BAD89543.1; -; mRNA.
DR   RefSeq; NP_001272479.1; NM_001285550.1.
DR   UniGene; Chi.235; -.
DR   ProteinModelPortal; Q5FB29; -.
DR   SMR; Q5FB29; -.
DR   PRIDE; Q5FB29; -.
DR   GeneID; 100861196; -.
DR   KEGG; chx:100861196; -.
DR   CTD; 6647; -.
DR   HOVERGEN; HBG000062; -.
DR   KO; K04565; -.
DR   OrthoDB; EOG091G0OG2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; ISS:UniProtKB.
DR   GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
DR   GO; GO:0019430; P:removal of superoxide radicals; ISS:UniProtKB.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Antioxidant; Copper; Cytoplasm; Disulfide bond;
KW   Lipoprotein; Metal-binding; Nucleus; Oxidoreductase; Palmitate;
KW   Phosphoprotein; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P00442}.
FT   CHAIN         2    152       Superoxide dismutase [Cu-Zn].
FT                                /FTId=PRO_0000164052.
FT   METAL        45     45       Copper; catalytic. {ECO:0000250}.
FT   METAL        47     47       Copper; catalytic. {ECO:0000250}.
FT   METAL        62     62       Copper; catalytic. {ECO:0000250}.
FT   METAL        62     62       Zinc; structural. {ECO:0000250}.
FT   METAL        70     70       Zinc; structural. {ECO:0000250}.
FT   METAL        79     79       Zinc; structural. {ECO:0000250}.
FT   METAL        82     82       Zinc; structural. {ECO:0000250}.
FT   METAL       119    119       Copper; catalytic. {ECO:0000250}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:P00442}.
FT   MOD_RES       4      4       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES      10     10       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES      90     90       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES     104    104       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P07632}.
FT   MOD_RES     106    106       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES     121    121       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P00441}.
FT   MOD_RES     121    121       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P00441}.
FT   MOD_RES     135    135       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES     135    135       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   LIPID         7      7       S-palmitoyl cysteine. {ECO:0000250}.
FT   DISULFID     56    145       {ECO:0000250}.
SQ   SEQUENCE   152 AA;  15653 MW;  B0257980664C1CD2 CRC64;
     MATKAVCVLK GDGPVQGTIH FEAKGDKVVV TGSITGLTEG DHGFHVHQFG DNTQGCTSAG
     PHFNPLSKKH GGPKDEERHV GDLGNVKADK NGVAIVDIVD PLISLSGEYS IIGRTMVVHE
     KPDDLGRGGN EESTKTGNAG SCLACGVIGI AP
//
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