LOCUS       NM_031000               1124 bp    mRNA    linear   ROD 07-FEB-2025
DEFINITION  Rattus norvegicus aldo-keto reductase family 1 member A1 (Akr1a1),
            mRNA.
ACCESSION   NM_031000
VERSION     NM_031000.3
KEYWORDS    RefSeq; RefSeq Select.
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  (bases 1 to 1124)
  AUTHORS   Zhou,H.L., Zhang,R., Anand,P., Stomberski,C.T., Qian,Z.,
            Hausladen,A., Wang,L., Rhee,E.P., Parikh,S.M., Karumanchi,S.A. and
            Stamler,J.S.
  TITLE     Author Correction: Metabolic reprogramming by the S-nitroso-CoA
            reductase system protects against kidney injury
  JOURNAL   Nature 570 (7759), E23 (2019)
   PUBMED   31089212
  REMARK    Correction to:[Nature. 2019 Jan;565(7737):96-100. doi:
            10.1038/s41586-018-0749-z.. PMID: 30487609]
REFERENCE   2  (bases 1 to 1124)
  AUTHORS   Liu,C., Li,Y., Wei,M., Zhao,L., Yu,Y. and Li,G.
  TITLE     Identification of a novel glycolysis-related gene signature that
            can predict the survival of patients with lung adenocarcinoma
  JOURNAL   Cell Cycle 18 (5), 568-579 (2019)
   PUBMED   30727821
REFERENCE   3  (bases 1 to 1124)
  AUTHORS   Homma,T., Shirato,T., Akihara,R., Kobayashi,S., Lee,J.,
            Yamada,K.I., Miyata,S., Takahashi,M. and Fujii,J.
  TITLE     Mice deficient in aldo-keto reductase 1a (Akr1a) are resistant to
            thioacetamide-induced liver injury
  JOURNAL   Toxicol Lett 294, 37-43 (2018)
   PUBMED   29763686
REFERENCE   4  (bases 1 to 1124)
  AUTHORS   Hlavac,V., Brynychova,V., Vaclavikova,R., Ehrlichova,M., Vrana,D.,
            Pecha,V., Trnkova,M., Kodet,R., Mrhalova,M., Kubackova,K.,
            Gatek,J., Vazan,P. and Soucek,P.
  TITLE     The role of cytochromes p450 and aldo-keto reductases in prognosis
            of breast carcinoma patients
  JOURNAL   Medicine (Baltimore) 93 (28), e255 (2014)
   PUBMED   25526449
REFERENCE   5  (bases 1 to 1124)
  AUTHORS   Kurahashi,T., Kwon,M., Homma,T., Saito,Y., Lee,J., Takahashi,M.,
            Yamada,K., Miyata,S. and Fujii,J.
  TITLE     Reductive detoxification of acrolein as a potential role for
            aldehyde reductase (AKR1A) in mammals
  JOURNAL   Biochem Biophys Res Commun 452 (1), 136-141 (2014)
   PUBMED   25152401
REFERENCE   6  (bases 1 to 1124)
  AUTHORS   Crosas,B., Hyndman,D.J., Gallego,O., Martras,S., Pares,X.,
            Flynn,T.G. and Farres,J.
  TITLE     Human aldose reductase and human small intestine aldose reductase
            are efficient retinal reductases: consequences for retinoid
            metabolism
  JOURNAL   Biochem J 373 (Pt 3), 973-979 (2003)
   PUBMED   12732097
REFERENCE   7  (bases 1 to 1124)
  AUTHORS   O'connor,T., Ireland,L.S., Harrison,D.J. and Hayes,J.D.
  TITLE     Major differences exist in the function and tissue-specific
            expression of human aflatoxin B1 aldehyde reductase and the
            principal human aldo-keto reductase AKR1 family members
  JOURNAL   Biochem J 343 Pt 2 (Pt 2), 487-504 (1999)
   PUBMED   10510318
REFERENCE   8  (bases 1 to 1124)
  AUTHORS   Suzuki,K., Koh,Y.H., Mizuno,H., Hamaoka,R. and Taniguchi,N.
  TITLE     Overexpression of aldehyde reductase protects PC12 cells from the
            cytotoxicity of methylglyoxal or 3-deoxyglucosone
  JOURNAL   J Biochem 123 (2), 353-357 (1998)
   PUBMED   9538214
REFERENCE   9  (bases 1 to 1124)
  AUTHORS   Barski,O.A., Gabbay,K.H., Grimshaw,C.E. and Bohren,K.M.
  TITLE     Mechanism of human aldehyde reductase: characterization of the
            active site pocket
  JOURNAL   Biochemistry 34 (35), 11264-11275 (1995)
   PUBMED   7669785
REFERENCE   10 (bases 1 to 1124)
  AUTHORS   Takahashi,M., Fujii,J., Teshima,T., Suzuki,K., Shiba,T. and
            Taniguchi,N.
  TITLE     Identity of a major 3-deoxyglucosone-reducing enzyme with aldehyde
            reductase in rat liver established by amino acid sequencing and
            cDNA expression
  JOURNAL   Gene 127 (2), 249-253 (1993)
   PUBMED   8500767
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D10854.1.
            
            On Jun 10, 2007 this sequence version replaced NM_031000.2.
            
            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 :: D10854.1, BC059133.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132275, SAMD00132305
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1124
                     /organism="Rattus norvegicus"
                     /mol_type="mRNA"
                     /strain="DONRYU"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q35"
     gene            1..1124
                     /gene="Akr1a1"
                     /gene_synonym="Akr1a4"
                     /note="aldo-keto reductase family 1 member A1"
                     /db_xref="GeneID:78959"
                     /db_xref="RGD:68346"
     exon            1..47
                     /gene="Akr1a1"
                     /gene_synonym="Akr1a4"
                     /inference="alignment:Splign:2.1.0"
     exon            48..137
                     /gene="Akr1a1"
                     /gene_synonym="Akr1a4"
                     /inference="alignment:Splign:2.1.0"
     CDS             54..1031
                     /gene="Akr1a1"
                     /gene_synonym="Akr1a4"
                     /EC_number="1.1.1.2"
                     /EC_number="1.1.1.54"
                     /EC_number="1.1.1.19"
                     /EC_number="1.1.1.20"
                     /EC_number="1.1.1.372"
                     /note="alcohol dehydrogenase; aldehyde reductase;
                     3-DG-reducing enzyme; glucuronate reductase;
                     glucuronolactone reductase; scorR; S-nitroso-CoA
                     reductase"
                     /codon_start=1
                     /product="aldo-keto reductase family 1 member A1"
                     /protein_id="NP_112262.1"
                     /db_xref="GeneID:78959"
                     /db_xref="RGD:68346"
                     /translation="MTASSVLLHTGQKMPLIGLGTWKSEPGQVKAAIKYALSVGYRHI
                     DCASVYGNETEIGEALKESVGAGKAVPREELFVTSKLWNTKHHPEDVEPAVRKTLADL
                     QLEYLDLYLMHWPYAFERGDNPFPKNADGTVKYDSTHYKETWKALEALVAKGLVKALG
                     LSNFSSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDR
                     AWRHPDEPVLLEEPVVLALAEKHGRSPAQILLRWQVQRKVICIPKSITPSRILQNIQV
                     FDFTFSPEEMKQLDALNKNWRYIVPMITVDGKRVPRDAGHPLYPFNDPY"
     exon            138..257
                     /gene="Akr1a1"
                     /gene_synonym="Akr1a4"
                     /inference="alignment:Splign:2.1.0"
     exon            258..409
                     /gene="Akr1a1"
                     /gene_synonym="Akr1a4"
                     /inference="alignment:Splign:2.1.0"
     exon            410..605
                     /gene="Akr1a1"
                     /gene_synonym="Akr1a4"
                     /inference="alignment:Splign:2.1.0"
     exon            606..805
                     /gene="Akr1a1"
                     /gene_synonym="Akr1a4"
                     /inference="alignment:Splign:2.1.0"
     exon            806..878
                     /gene="Akr1a1"
                     /gene_synonym="Akr1a4"
                     /inference="alignment:Splign:2.1.0"
     exon            879..965
                     /gene="Akr1a1"
                     /gene_synonym="Akr1a4"
                     /inference="alignment:Splign:2.1.0"
     exon            966..1124
                     /gene="Akr1a1"
                     /gene_synonym="Akr1a4"
                     /inference="alignment:Splign:2.1.0"
     polyA_site      1124
                     /gene="Akr1a1"
                     /gene_synonym="Akr1a4"
ORIGIN      
        1 gaattctggc cactttgtct tctccacagc ctgtgctcat tgccaagggg acaatgacgg
       61 cctccagtgt cctcctgcac actggacaga agatgcctct gattggtctg gggacatgga
      121 agagtgagcc tggtcaggtg aaagcagcta ttaaatatgc ccttagcgta ggctaccgcc
      181 acattgactg tgcttctgta tatggcaatg aaactgagat tggagaggcc ctgaaggaga
      241 gtgtgggagc aggcaaggca gtacctcgag aggagctgtt tgtgacctcc aagctgtgga
      301 atactaagca ccaccctgag gatgtagaac ctgctgtccg gaagacgctg gctgatctgc
      361 agctggagta tttggacctc tatttgatgc attggcctta tgccttcgag cggggagaca
      421 atccctttcc caagaatgcc gatggaactg tcaaatatga ctccactcac tataaggaga
      481 cctggaaggc tctggaggca ctggtggcaa aggggctggt gaaagccttg ggcttgtcca
      541 acttcagcag tcggcagata gatgatgtcc tcagtgtggc ctcggtgcgc ccagctgtct
      601 tgcaggtgga atgccatcca tacctggctc aaaatgagct cattgcccac tgtcaagcac
      661 gaggcttgga ggtgacagct tacagcccct tgggttcatc ggatcgtgct tggcgccacc
      721 ctgatgagcc agtcctgctt gaggaaccag ttgtcttggc actagctgaa aaacatggcc
      781 gatctccagc tcagatcttg ctcagatggc aggttcagcg gaaagtaatc tgcatcccca
      841 aaagcatcac tccttcccgc atccttcaga acattcaggt atttgatttc acctttagtc
      901 cagaggagat gaagcaatta gatgctctga acaaaaattg gcggtatatt gtgcccatga
      961 ttacggtgga tgggaagaga gtccccagag atgctggaca ccctctgtat ccctttaatg
     1021 acccatactg aggcccgtag tttctcagct tccctttcag ttctcctgct aagcattgcc
     1081 tgctactccc aagaaagaag gactcaataa agccattgaa gtgt
//
