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Entry: SODC_HORSE D7PPM2_HORSE
LinkDB: SODC_HORSE D7PPM2_HORSE
Original site: SODC_HORSE D7PPM2_HORSE 
ID   SODC_HORSE              Reviewed;         154 AA.
AC   P00443;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-OCT-2017, entry version 128.
DE   RecName: Full=Superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1;
GN   Name=SOD1;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8921896; DOI=10.1016/0378-1119(96)00339-3;
RA   de la Rua-Domenech R., Wiedmann M., Mohammed H.O., Cummings J.F.,
RA   Divers T.J., Batt C.A.;
RT   "Equine motor neuron disease is not linked to Cu/Zn superoxide
RT   dismutase mutations: sequence analysis of the equine Cu/Zn superoxide
RT   dismutase cDNA.";
RL   Gene 178:83-88(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=10331206; DOI=10.1292/jvms.61.291;
RA   Ishida N., Katayama Y., Sato F., Hasegawa T., Mukoyama H.;
RT   "The cDNA sequences of equine antioxidative enzyme genes Cu/Zn-SOD and
RT   Mn-SOD, and these expressions in equine tissues.";
RL   J. Vet. Med. Sci. 61:291-294(1999).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-154, AND ACETYLATION AT ALA-2.
RC   TISSUE=Liver;
RX   PubMed=7298616;
RA   Lerch K., Ammer D.;
RT   "Amino acid sequence of copper-zinc superoxide dismutase from horse
RT   liver.";
RL   J. Biol. Chem. 256:11545-11551(1981).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {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; U38956; AAC48682.1; -; mRNA.
DR   EMBL; AB001692; BAA76921.1; -; mRNA.
DR   PIR; JC5215; DSHOCZ.
DR   RefSeq; NP_001075295.1; NM_001081826.3.
DR   UniGene; Eca.28; -.
DR   ProteinModelPortal; P00443; -.
DR   SMR; P00443; -.
DR   STRING; 9796.ENSECAP00000007080; -.
DR   iPTMnet; P00443; -.
DR   PaxDb; P00443; -.
DR   PeptideAtlas; P00443; -.
DR   GeneID; 100033855; -.
DR   KEGG; ecb:100033855; -.
DR   CTD; 6647; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   HOGENOM; HOG000263447; -.
DR   HOVERGEN; HBG000062; -.
DR   InParanoid; P00443; -.
DR   KO; K04565; -.
DR   Proteomes; UP000002281; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
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.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Antioxidant; Complete proteome; Copper; Cytoplasm;
KW   Direct protein sequencing; Disulfide bond; Lipoprotein; Metal-binding;
KW   Nucleus; Oxidoreductase; Palmitate; Phosphoprotein;
KW   Reference proteome; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:7298616}.
FT   CHAIN         2    154       Superoxide dismutase [Cu-Zn].
FT                                /FTId=PRO_0000164056.
FT   METAL        47     47       Copper; catalytic. {ECO:0000250}.
FT   METAL        49     49       Copper; catalytic. {ECO:0000250}.
FT   METAL        64     64       Copper; catalytic. {ECO:0000250}.
FT   METAL        64     64       Zinc; structural. {ECO:0000250}.
FT   METAL        72     72       Zinc; structural. {ECO:0000250}.
FT   METAL        81     81       Zinc; structural. {ECO:0000250}.
FT   METAL        84     84       Zinc; structural. {ECO:0000250}.
FT   METAL       121    121       Copper; catalytic. {ECO:0000250}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000269|PubMed:7298616}.
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     103    103       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P00441}.
FT   MOD_RES     106    106       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P07632}.
FT   MOD_RES     108    108       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES     123    123       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P00441}.
FT   MOD_RES     123    123       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P00441}.
FT   MOD_RES     137    137       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES     137    137       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   LIPID         7      7       S-palmitoyl cysteine. {ECO:0000250}.
FT   DISULFID     58    147       {ECO:0000250}.
SQ   SEQUENCE   154 AA;  16071 MW;  890AA4D02A6704EA CRC64;
     MALKAVCVLK GDGPVHGVIH FEQQQEGGPV VLKGFIEGLT KGDHGFHVHE FGDNTQGCTT
     AGAHFNPLSK KHGGPKDEER HVGDLGNVTA DENGKADVDM KDSVISLSGK HSIIGRTMVV
     HEKQDDLGKG GNEESTKTGN AGSRLACGVI GIAP
//
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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (4)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (7)   
   InterPro (4)   
   Pfam (1)   
   PROSITE (2)   
Literature (3)   
   PubMed (3)   
All databases (26)   

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ID   D7PPM2_HORSE            Unreviewed;       154 AA.
AC   D7PPM2;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   25-OCT-2017, entry version 49.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796 {ECO:0000313|EMBL:ADG85264.1};
RN   [1] {ECO:0000313|EMBL:ADG85264.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Muscle {ECO:0000313|EMBL:ADG85264.1};
RA   Changlv L., Khazanehdari K.;
RT   "Characterization of equine copper-zinc-containing superoxide
RT   dismutase 1 (Cu/ZnSOD or SOD1).";
RL   Submitted (FEB-2010) 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       {ECO:0000256|RuleBase:RU000393}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000393}.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
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DR   EMBL; GU808338; ADG85264.1; -; Genomic_DNA.
DR   EMBL; GU808339; ADG85265.1; -; mRNA.
DR   RefSeq; NP_001075295.1; NM_001081826.3.
DR   UniGene; Eca.28; -.
DR   SMR; D7PPM2; -.
DR   GeneID; 100033855; -.
DR   KEGG; ecb:100033855; -.
DR   CTD; 6647; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   KO; K04565; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   2: Evidence at transcript level;
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       12    150       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   154 AA;  16071 MW;  890AA4D02A6704EA CRC64;
     MALKAVCVLK GDGPVHGVIH FEQQQEGGPV VLKGFIEGLT KGDHGFHVHE FGDNTQGCTT
     AGAHFNPLSK KHGGPKDEER HVGDLGNVTA DENGKADVDM KDSVISLSGK HSIIGRTMVV
     HEKQDDLGKG GNEESTKTGN AGSRLACGVI GIAP
//
  All links  
Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (4)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (7)   
   InterPro (4)   
   Pfam (1)   
   PROSITE (2)   
All databases (17)   

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