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Database: UniProt/SWISS-PROT
Entry: SODC_CAMDR
LinkDB: SODC_CAMDR
Original site: SODC_CAMDR 
ID   SODC_CAMDR              Reviewed;         153 AA.
AC   H6BDU4;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 1.
DT   30-AUG-2017, entry version 24.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000255|RuleBase:RU000393, ECO:0000303|PubMed:22312292};
DE            EC=1.15.1.1 {ECO:0000250|UniProtKB:P00442, ECO:0000255|RuleBase:RU000393};
GN   Name=SOD1 {ECO:0000303|PubMed:22312292};
OS   Camelus dromedarius (Dromedary) (Arabian camel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Tylopoda;
OC   Camelidae; Camelus.
OX   NCBI_TaxID=9838 {ECO:0000312|EMBL:AEF32527.1};
RN   [1] {ECO:0000312|EMBL:AEF32527.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND PHYLOGENETIC
RP   ANALYSIS.
RX   PubMed=22312292; DOI=10.3390/ijms13010879;
RA   Ataya F.S., Fouad D., Al-Olayan E., Malik A.;
RT   "Molecular cloning, characterization and predicted structure of a
RT   putative copper-zinc SOD from the camel, Camelus dromedarius.";
RL   Int. J. Mol. Sci. 13:879-900(2012).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000250|UniProtKB:P00442, ECO:0000255|RuleBase:RU000393}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000250|UniProtKB:P00442, ECO:0000255|RuleBase:RU000393}.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000250|UniProtKB:P00441,
CC         ECO:0000255|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit.
CC       {ECO:0000250|UniProtKB:P00441, ECO:0000255|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P00441,
CC         ECO:0000255|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00441,
CC       ECO:0000255|RuleBase:RU000393};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P00442}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00441}.
CC       Nucleus {ECO:0000250|UniProtKB:P00441}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in liver. Also expressed in
CC       testis and to a lesser extent in kidney, lung and spleen.
CC       {ECO:0000269|PubMed:22312292}.
CC   -!- PTM: Palmitoylation helps nuclear targeting and decreases
CC       catalytic activity. {ECO:0000250|UniProtKB:P00441}.
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:0000255|RuleBase:RU000393, ECO:0000305}.
DR   EMBL; JF758876; AEF32527.1; -; mRNA.
DR   RefSeq; XP_010975659.1; XM_010977357.1.
DR   SMR; H6BDU4; -.
DR   GeneID; 105086775; -.
DR   KEGG; cdk:105086775; -.
DR   CTD; 6647; -.
DR   OrthoDB; EOG091G0OG2; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0004784; F:superoxide dismutase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; 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; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 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    153       Superoxide dismutase [Cu-Zn].
FT                                /FTId=PRO_0000438320.
FT   METAL        46     46       Copper; catalytic.
FT                                {ECO:0000250|UniProtKB:P00442}.
FT   METAL        48     48       Copper; catalytic.
FT                                {ECO:0000250|UniProtKB:P00442}.
FT   METAL        63     63       Copper; catalytic.
FT                                {ECO:0000250|UniProtKB:P00442}.
FT   METAL        63     63       Zinc; structural.
FT                                {ECO:0000250|UniProtKB:P00442}.
FT   METAL        71     71       Zinc; structural.
FT                                {ECO:0000250|UniProtKB:P00442}.
FT   METAL        80     80       Zinc; structural.
FT                                {ECO:0000250|UniProtKB:P00442}.
FT   METAL        83     83       Zinc; structural.
FT                                {ECO:0000250|UniProtKB:P00442}.
FT   METAL       120    120       Copper; catalytic.
FT                                {ECO:0000250|UniProtKB:P00442}.
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      91     91       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES      98     98       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P00441}.
FT   MOD_RES     105    105       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P07632}.
FT   MOD_RES     107    107       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES     122    122       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P00441}.
FT   MOD_RES     122    122       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P00441}.
FT   MOD_RES     136    136       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES     136    136       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   LIPID         7      7       S-palmitoyl cysteine.
FT                                {ECO:0000250|UniProtKB:P00441}.
FT   DISULFID     57    146       {ECO:0000250|UniProtKB:P00442}.
SQ   SEQUENCE   153 AA;  15743 MW;  3756F1B50E53B76E CRC64;
     MALKAVCVLK GDGQVQGTIH FEQKENGPVM VSGSISGLAE GDHGFHVHQF GDNTQGCTSA
     GPHFNPLSKK HGGPKDQERH VGDLGNVTAG KDGVAIVSIE DPVISLSGDH SIIGRTMVVH
     EKPDDLGKGG NEESTKTGNA GSRLACGVIG IAQ
//
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