GenomeNet

Database: RefSeq
Entry: NP_058746
LinkDB: NP_058746
Original site: NP_058746 
LOCUS       NP_058746                154 aa            linear   ROD 11-NOV-2018
DEFINITION  superoxide dismutase [Cu-Zn] [Rattus norvegicus].
ACCESSION   NP_058746
VERSION     NP_058746.1
DBSOURCE    REFSEQ: accession NM_017050.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Moller A, Bauer CS, Cohen RN, Webster CP and De Vos KJ.
  TITLE     Amyotrophic lateral sclerosis-associated mutant SOD1 inhibits
            anterograde axonal transport of mitochondria by reducing Miro1
            levels
  JOURNAL   Hum. Mol. Genet. 26 (23), 4668-4679 (2017)
   PUBMED   28973175
  REMARK    GeneRIF: Results provide evidence that ALS mutant SOD1 inhibits
            axonal transport of mitochondria by inducing PINK1/Parkin-dependent
            Miro1 degradation.
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Cowley PM, Nair DR, DeRuisseau LR, Keslacy S, Atalay M and
            DeRuisseau KC.
  TITLE     Oxidant production and SOD1 protein expression in single skeletal
            myofibers from Down syndrome mice
  JOURNAL   Redox Biol 13, 421-425 (2017)
   PUBMED   28697486
  REMARK    GeneRIF: SOD1 protein expression is upregulated and associated with
            greater oxidant production in skeletal muscle from Ts65Dn mice.
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Park C, Ji HM, Kim SJ, Kil SH, Lee JN, Kwak S, Choe SK and Park R.
  TITLE     Fenofibrate exerts protective effects against gentamicin-induced
            toxicity in cochlear hair cells by activating antioxidant enzymes
  JOURNAL   Int. J. Mol. Med. 39 (4), 960-968 (2017)
   PUBMED   28290603
  REMARK    GeneRIF: fenofibrate almost completely abolished GM-induced
            reactive oxygen species generation, which seemed to be mediated at
            least in part by the restoration of the expression of
            PPARalphadependent antioxidant enzymes, including catalase and
            superoxide dismutase (SOD)-1.
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Maremanda KP and Jena GB.
  TITLE     Methotrexate-induced germ cell toxicity and the important role of
            zinc and SOD1: Investigation of molecular mechanisms
  JOURNAL   Biochem. Biophys. Res. Commun. 483 (1), 596-601 (2017)
   PUBMED   28011267
  REMARK    GeneRIF: SOD1 and zinc have roles in methotrexate-induced germ cell
            toxicity
REFERENCE   5  (residues 1 to 154)
  AUTHORS   Pejic,S., Stojikjkovic,V., Todorovic,A., Gavrilovic,L.,
            Pavlovic,I., Popovic,N. and Pajovic,S.B.
  TITLE     Antioxidant Enzymes in Brain Cortex of Rats Exposed to Acute,
            Chronic and Combined Stress
  JOURNAL   Folia Biol. (Krakow) 64 (3), 189-195 (2016)
   PUBMED   29847079
  REMARK    GeneRIF: These results indicate that stress conditions most
            probably altered the cell redox equilibrium, thus influencing the
            antioxidant response in brain cortex.
REFERENCE   6  (residues 1 to 154)
  AUTHORS   Crapo JD, Oury T, Rabouille C, Slot JW and Chang LY.
  TITLE     Copper,zinc superoxide dismutase is primarily a cytosolic protein
            in human cells
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 89 (21), 10405-10409 (1992)
   PUBMED   1332049
REFERENCE   7  (residues 1 to 154)
  AUTHORS   Hsu JL, Visner GA, Burr IA and Nick HS.
  TITLE     Rat copper/zinc superoxide dismutase gene: isolation,
            characterization, and species comparison
  JOURNAL   Biochem. Biophys. Res. Commun. 186 (2), 936-943 (1992)
   PUBMED   1379810
REFERENCE   8  (residues 1 to 154)
  AUTHORS   Hass MA, Iqbal J, Clerch LB, Frank L and Massaro D.
  TITLE     Rat lung Cu,Zn superoxide dismutase. Isolation and sequence of a
            full-length cDNA and studies of enzyme induction
  JOURNAL   J. Clin. Invest. 83 (4), 1241-1246 (1989)
   PUBMED   2703531
REFERENCE   9  (residues 1 to 154)
  AUTHORS   Puga A and Oates EL.
  TITLE     Isolation and nucleotide sequence of rat Cu/Zn superoxide dismutase
            cDNA clones
  JOURNAL   Free Radic. Res. Commun. 3 (6), 337-346 (1987)
   PUBMED   3508449
REFERENCE   10 (residues 1 to 154)
  AUTHORS   Francke,U. and Taggart,R.T.
  TITLE     Assignment of the gene for cytoplasmic superoxide dismutase (Sod-1)
            to a region of chromosome 16 and of Hprt to a region of the X
            chromosome in the mouse
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 76 (10), 5230-5233 (1979)
   PUBMED   291939
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from Y00404.1.
            
            Summary: catalyzes the conversion of superoxide to hydrogen
            peroxide and molecular oxygen; involved in response to oxidative
            stress [RGD, Feb 2006].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Y00404.1, CA339871.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00052296, SAMD00052297
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..154
                     /product="superoxide dismutase [Cu-Zn]"
                     /EC_number="1.15.1.1"
                     /note="superoxide dismutase 1, soluble"
                     /calculated_mol_wt=15781
     Site            2
                     /site_type="other"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N-acetylalanine. {ECO:0000250|UniProtKB:P00442};
                     propagated from UniProtKB/Swiss-Prot (P07632.2)"
     Region          3..147
                     /region_name="Cu-Zn_Superoxide_Dismutase"
                     /note="Copper/zinc superoxide dismutase (SOD). superoxide
                     dismutases catalyse the conversion of superoxide radicals
                     to molecular oxygen. Three evolutionarily distinct
                     families of SODs are known, of which the
                     copper/zinc-binding family is one. Defects in the...;
                     cd00305"
                     /db_xref="CDD:238186"
     Site            4
                     /site_type="modified"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-succinyllysine. {ECO:0000250|UniProtKB:P08228};
                     propagated from UniProtKB/Swiss-Prot (P07632.2)"
     Site            order(6,8,18,20,51..53,114..115)
                     /site_type="other"
                     /note="E-class dimer interface [polypeptide binding]"
                     /db_xref="CDD:238186"
     Site            10
                     /site_type="modified"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-succinyllysine. {ECO:0000250|UniProtKB:P08228};
                     propagated from UniProtKB/Swiss-Prot (P07632.2)"
     Site            order(31,89)
                     /site_type="other"
                     /note="P-class dimer interface [polypeptide binding]"
                     /db_xref="CDD:238186"
     Site            order(47,49,64,81,84,121)
                     /site_type="active"
                     /db_xref="CDD:238186"
     Site            order(47,49,64,121)
                     /site_type="other"
                     /note="Cu2+ binding site [ion binding]"
                     /db_xref="CDD:238186"
     Site            order(64,72,81,84)
                     /site_type="other"
                     /note="Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238186"
     Site            92
                     /site_type="modified"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-succinyllysine. {ECO:0000250|UniProtKB:P08228};
                     propagated from UniProtKB/Swiss-Prot (P07632.2)"
     Site            99
                     /site_type="other"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000244|PubMed:22673903};
                     propagated from UniProtKB/Swiss-Prot (P07632.2)"
     Site            106
                     /site_type="other"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000244|PubMed:22673903};
                     propagated from UniProtKB/Swiss-Prot (P07632.2)"
     Site            108
                     /site_type="other"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000244|PubMed:22673903};
                     propagated from UniProtKB/Swiss-Prot (P07632.2)"
     Site            123
                     /site_type="other"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-acetyllysine, alternate.
                     {ECO:0000250|UniProtKB:P00441}; propagated from
                     UniProtKB/Swiss-Prot (P07632.2)"
     Site            123
                     /site_type="modified"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-succinyllysine, alternate.
                     {ECO:0000250|UniProtKB:P00441}; propagated from
                     UniProtKB/Swiss-Prot (P07632.2)"
     Site            137
                     /site_type="other"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-acetyllysine, alternate.
                     {ECO:0000250|UniProtKB:P08228}; propagated from
                     UniProtKB/Swiss-Prot (P07632.2)"
     Site            137
                     /site_type="modified"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-succinyllysine, alternate.
                     {ECO:0000250|UniProtKB:P08228}; propagated from
                     UniProtKB/Swiss-Prot (P07632.2)"
     CDS             1..154
                     /gene="Sod1"
                     /gene_synonym="CuZnSOD"
                     /coded_by="NM_017050.1:94..558"
                     /db_xref="GeneID:24786"
                     /db_xref="RGD:3731"
ORIGIN      
        1 mamkavcvlk gdgpvqgvih feqkasgepv vvsgqitglt egehgfhvhq ygdntqgctt
       61 agphfnphsk khggpadeer hvgdlgnvaa gkdgvanvsi edrvislsge hsiigrtmvv
      121 hekqddlgkg gneestktgn agsrlacgvi giaq
//
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