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Database: UniProt/SWISS-PROT UniProt/TrEMBL
Entry: SODC_MACMU H9FMP4_MACMU
LinkDB: SODC_MACMU H9FMP4_MACMU
Original site: SODC_MACMU H9FMP4_MACMU 
ID   SODC_MACMU              Reviewed;         154 AA.
AC   Q8HXQ0;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-OCT-2017, entry version 114.
DE   RecName: Full=Superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1;
GN   Name=SOD1;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
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 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; AB087271; BAC20350.1; -; mRNA.
DR   RefSeq; NP_001027976.1; NM_001032804.1.
DR   UniGene; Mmu.882; -.
DR   ProteinModelPortal; Q8HXQ0; -.
DR   SMR; Q8HXQ0; -.
DR   STRING; 9544.ENSMMUP00000002283; -.
DR   PRIDE; Q8HXQ0; -.
DR   Ensembl; ENSMMUT00000002415; ENSMMUP00000002283; ENSMMUG00000001711.
DR   GeneID; 574096; -.
DR   KEGG; mcc:574096; -.
DR   CTD; 6647; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   GeneTree; ENSGT00530000063226; -.
DR   HOGENOM; HOG000263447; -.
DR   HOVERGEN; HBG000062; -.
DR   InParanoid; Q8HXQ0; -.
DR   KO; K04565; -.
DR   OMA; IHTFGDN; -.
DR   OrthoDB; EOG091G0OG2; -.
DR   TreeFam; TF105131; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000001711; -.
DR   ExpressionAtlas; Q8HXQ0; baseline.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0032839; C:dendrite cytoplasm; ISS:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR   GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005777; C:peroxisome; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0043234; C:protein complex; ISS:UniProtKB.
DR   GO; GO:0051087; F:chaperone binding; ISS:UniProtKB.
DR   GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0030346; F:protein phosphatase 2B binding; ISS:UniProtKB.
DR   GO; GO:0048365; F:Rac GTPase binding; IEA:Ensembl.
DR   GO; GO:0004784; F:superoxide dismutase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0000187; P:activation of MAPK activity; ISS:UniProtKB.
DR   GO; GO:0008089; P:anterograde axonal transport; IEA:Ensembl.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
DR   GO; GO:0060088; P:auditory receptor cell stereocilium organization; ISS:UniProtKB.
DR   GO; GO:0007569; P:cell aging; ISS:UniProtKB.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR   GO; GO:0007566; P:embryo implantation; ISS:UniProtKB.
DR   GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
DR   GO; GO:0060047; P:heart contraction; ISS:UniProtKB.
DR   GO; GO:0050665; P:hydrogen peroxide biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; ISS:UniProtKB.
DR   GO; GO:0002262; P:myeloid cell homeostasis; ISS:UniProtKB.
DR   GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR   GO; GO:0060052; P:neurofilament cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
DR   GO; GO:0032287; P:peripheral nervous system myelin maintenance; ISS:UniProtKB.
DR   GO; GO:0043085; P:positive regulation of catalytic activity; ISS:UniProtKB.
DR   GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR   GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl.
DR   GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
DR   GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
DR   GO; GO:0043087; P:regulation of GTPase activity; IEA:Ensembl.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:UniProtKB.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; ISS:UniProtKB.
DR   GO; GO:0045859; P:regulation of protein kinase activity; ISS:UniProtKB.
DR   GO; GO:0060087; P:relaxation of vascular smooth muscle; ISS:UniProtKB.
DR   GO; GO:0019430; P:removal of superoxide radicals; ISS:UniProtKB.
DR   GO; GO:0048678; P:response to axon injury; ISS:UniProtKB.
DR   GO; GO:0042493; P:response to drug; ISS:UniProtKB.
DR   GO; GO:0045471; P:response to ethanol; ISS:UniProtKB.
DR   GO; GO:0009408; P:response to heat; ISS:UniProtKB.
DR   GO; GO:0042542; P:response to hydrogen peroxide; ISS:UniProtKB.
DR   GO; GO:0010033; P:response to organic substance; ISS:UniProtKB.
DR   GO; GO:0000303; P:response to superoxide; ISS:UniProtKB.
DR   GO; GO:0001895; P:retina homeostasis; ISS:UniProtKB.
DR   GO; GO:0008090; P:retrograde axonal transport; IEA:Ensembl.
DR   GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   GO; GO:0042554; P:superoxide anion generation; IEA:Ensembl.
DR   GO; GO:0006801; P:superoxide metabolic process; ISS:UniProtKB.
DR   GO; GO:0019226; P:transmission of nerve impulse; 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   2: Evidence at transcript level;
KW   Acetylation; Antioxidant; Complete proteome; Copper; Cytoplasm;
KW   Disulfide bond; Lipoprotein; Metal-binding; Nucleus; Oxidoreductase;
KW   Palmitate; Phosphoprotein; Reference proteome; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P00442}.
FT   CHAIN         2    154       Superoxide dismutase [Cu-Zn].
FT                                /FTId=PRO_0000164061.
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: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      92     92       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES      99     99       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P00441}.
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;  15983 MW;  7B77BC2ED8CDDC2F CRC64;
     MAMKAVCVLK GDSPVQGTIN FEQKESNGPV KVWGSITGLT EGLHGFHVHQ FGDNTQGCTS
     AGPHFNPLSR QHGGPKDEER HVGDLGNVTA GKDGVAKVSF EDSVISLSGD HSIIGRTLVV
     HEKADDLGKG GNEESKKTGN AGGRLACGVI GIAQ
//
  All links  
Ontology (68)   
   GO (68)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (7)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
   ENSEMBL-UP (3)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (7)   
   InterPro (4)   
   Pfam (1)   
   PROSITE (2)   
Literature (1)   
   PubMed (1)   
All databases (86)   

Download RDF
ID   H9FMP4_MACMU            Unreviewed;       154 AA.
AC   H9FMP4;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   25-OCT-2017, entry version 50.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=SOD1 {ECO:0000313|EMBL:AFE75903.1};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|EMBL:AFE75903.1};
RN   [1] {ECO:0000313|EMBL:AFE75903.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Caudate {ECO:0000313|EMBL:AFE75903.1}, Testis
RC   {ECO:0000313|EMBL:AFI35180.1}, and Thymus
RC   {ECO:0000313|EMBL:AFH29269.1};
RX   PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA   Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X.,
RA   Pandey S., Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P.,
RA   Tharp G.K., Marcais G., Roberts M., Ferguson B., Fox H.S.,
RA   Treangen T., Salzberg S.L., Yorke J.A., Norgren R.B.Jr.;
RT   "A new rhesus macaque assembly and annotation for next-generation
RT   sequencing analyses.";
RL   Biol. Direct 9:20-20(2014).
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; JU332147; AFE75903.1; -; mRNA.
DR   EMBL; JU472465; AFH29269.1; -; mRNA.
DR   EMBL; JV045109; AFI35180.1; -; mRNA.
DR   RefSeq; NP_001027976.1; NM_001032804.1.
DR   UniGene; Mmu.882; -.
DR   SMR; H9FMP4; -.
DR   GeneID; 574096; -.
DR   KEGG; mcc:574096; -.
DR   CTD; 6647; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   KO; K04565; -.
DR   OMA; IHTFGDN; -.
DR   OrthoDB; EOG091G0OG2; -.
DR   Bgee; ENSMMUG00000001711; -.
DR   ExpressionAtlas; H9FMP4; baseline.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0032839; C:dendrite cytoplasm; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005777; C:peroxisome; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0043234; C:protein complex; IEA:Ensembl.
DR   GO; GO:0051087; F:chaperone binding; IEA:Ensembl.
DR   GO; GO:0005507; F:copper ion binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0030346; F:protein phosphatase 2B binding; IEA:Ensembl.
DR   GO; GO:0048365; F:Rac GTPase binding; IEA:Ensembl.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR   GO; GO:0000187; P:activation of MAPK activity; IEA:Ensembl.
DR   GO; GO:0008089; P:anterograde axonal transport; IEA:Ensembl.
DR   GO; GO:0060088; P:auditory receptor cell stereocilium organization; IEA:Ensembl.
DR   GO; GO:0007569; P:cell aging; IEA:Ensembl.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:Ensembl.
DR   GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:Ensembl.
DR   GO; GO:0060047; P:heart contraction; IEA:Ensembl.
DR   GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IEA:Ensembl.
DR   GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
DR   GO; GO:0002262; P:myeloid cell homeostasis; IEA:Ensembl.
DR   GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; IEA:Ensembl.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0060052; P:neurofilament cytoskeleton organization; IEA:Ensembl.
DR   GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
DR   GO; GO:0032287; P:peripheral nervous system myelin maintenance; IEA:Ensembl.
DR   GO; GO:0001819; P:positive regulation of cytokine production; IEA:Ensembl.
DR   GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR   GO; GO:0043087; P:regulation of GTPase activity; IEA:Ensembl.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; IEA:Ensembl.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0060087; P:relaxation of vascular smooth muscle; IEA:Ensembl.
DR   GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
DR   GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR   GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR   GO; GO:0009408; P:response to heat; IEA:Ensembl.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR   GO; GO:0001895; P:retina homeostasis; IEA:Ensembl.
DR   GO; GO:0008090; P:retrograde axonal transport; IEA:Ensembl.
DR   GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR   GO; GO:0042554; P:superoxide anion generation; IEA:Ensembl.
DR   GO; GO:0019226; P:transmission of nerve impulse; IEA:Ensembl.
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;  15983 MW;  7B77BC2ED8CDDC2F CRC64;
     MAMKAVCVLK GDSPVQGTIN FEQKESNGPV KVWGSITGLT EGLHGFHVHQ FGDNTQGCTS
     AGPHFNPLSR QHGGPKDEER HVGDLGNVTA GKDGVAKVSF EDSVISLSGD HSIIGRTLVV
     HEKADDLGKG GNEESKKTGN AGGRLACGVI GIAQ
//
  All links  
Ontology (56)   
   GO (56)   
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 (3)   
   EMBL (3)   
Protein domain (7)   
   InterPro (4)   
   Pfam (1)   
   PROSITE (2)   
Literature (1)   
   PubMed (1)   
All databases (73)   

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