LOCUS       NM_001757               1208 bp    mRNA    linear   PRI 06-DEC-2024
DEFINITION  Homo sapiens carbonyl reductase 1 (CBR1), transcript variant 1,
            mRNA.
ACCESSION   NM_001757
VERSION     NM_001757.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (bases 1 to 1208)
  AUTHORS   Chen,S., Chen,J., Chen,J. and Wang,Y.
  TITLE     [Altered expression of 15-hydroxyprostaglandin dehydrogenase in
            chronic rhinosinusitis with nasal polyps]
  JOURNAL   Lin Chuang Er Bi Yan Hou Tou Jing Wai Ke Za Zhi 37 (11), 891-896
            (2023)
   PUBMED   37905483
  REMARK    GeneRIF: [Altered expression of 15-hydroxyprostaglandin
            dehydrogenase in chronic rhinosinusitis with nasal polyps].
REFERENCE   2  (bases 1 to 1208)
  AUTHORS   Wang,T., Mao,P., Zhang,Y., Cui,B., Wang,M.D., Li,Y. and Gao,K.
  TITLE     LncRNA MYMLR promotes pituitary adenoma development by upregulating
            carbonyl reductase 1 via sponging miR-197-3p
  JOURNAL   Anticancer Drugs 33 (10), 1058-1068 (2022)
   PUBMED   36206098
  REMARK    GeneRIF: LncRNA MYMLR promotes pituitary adenoma development by
            upregulating carbonyl reductase 1 via sponging miR-197-3p.
REFERENCE   3  (bases 1 to 1208)
  AUTHORS   Mao,L., Wang,K., Zhang,P., Ren,S., Sun,J., Yang,M., Zhang,F. and
            Sun,B.
  TITLE     Carbonyl Reductase 1 Attenuates Ischemic Brain Injury by Reducing
            Oxidative Stress and Neuroinflammation
  JOURNAL   Transl Stroke Res 12 (5), 711-724 (2021)
   PUBMED   33964000
  REMARK    GeneRIF: Carbonyl Reductase 1 Attenuates Ischemic Brain Injury by
            Reducing Oxidative Stress and Neuroinflammation.
REFERENCE   4  (bases 1 to 1208)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (bases 1 to 1208)
  AUTHORS   Khazeem,M.M., Cowell,I.G., Harkin,L.F., Casement,J.W. and
            Austin,C.A.
  TITLE     Transcription of carbonyl reductase 1 is regulated by DNA
            topoisomerase II beta
  JOURNAL   FEBS Lett 594 (20), 3395-3405 (2020)
   PUBMED   32767399
  REMARK    GeneRIF: Transcription of carbonyl reductase 1 is regulated by DNA
            topoisomerase II beta.
REFERENCE   6  (bases 1 to 1208)
  AUTHORS   Wirth,H. and Wermuth,B.
  TITLE     Immunohistochemical localization of carbonyl reductase in human
            tissues
  JOURNAL   J Histochem Cytochem 40 (12), 1857-1863 (1992)
   PUBMED   1453004
REFERENCE   7  (bases 1 to 1208)
  AUTHORS   Inazu,N., Ruepp,B., Wirth,H. and Wermuth,B.
  TITLE     Carbonyl reductase from human testis: purification and comparison
            with carbonyl reductase from human brain and rat testis
  JOURNAL   Biochim Biophys Acta 1116 (1), 50-56 (1992)
   PUBMED   1540623
REFERENCE   8  (bases 1 to 1208)
  AUTHORS   Forrest,G.L., Akman,S., Doroshow,J., Rivera,H. and Kaplan,W.D.
  TITLE     Genomic sequence and expression of a cloned human carbonyl
            reductase gene with daunorubicin reductase activity
  JOURNAL   Mol Pharmacol 40 (4), 502-507 (1991)
   PUBMED   1921984
REFERENCE   9  (bases 1 to 1208)
  AUTHORS   Forrest,G.L., Akman,S., Krutzik,S., Paxton,R.J., Sparkes,R.S.,
            Doroshow,J., Felsted,R.L., Glover,C.J., Mohandas,T. and Bachur,N.R.
  TITLE     Induction of a human carbonyl reductase gene located on chromosome
            21
  JOURNAL   Biochim Biophys Acta 1048 (2-3), 149-155 (1990)
   PUBMED   2182121
REFERENCE   10 (bases 1 to 1208)
  AUTHORS   Wermuth,B., Platts,K.L., Seidel,A. and Oesch,F.
  TITLE     Carbonyl reductase provides the enzymatic basis of quinone
            detoxication in man
  JOURNAL   Biochem Pharmacol 35 (8), 1277-1282 (1986)
   PUBMED   3083821
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB124848.1.
            
            On Nov 22, 2018 this sequence version replaced NM_001757.3.
            
            Summary: The protein encoded by this gene belongs to the
            short-chain dehydrogenases/reductases (SDR) family, which function
            as NADPH-dependent oxidoreductases having wide specificity for
            carbonyl compounds, such as quinones, prostaglandins, and various
            xenobiotics. Alternatively spliced transcript variants have been
            found for this gene. [provided by RefSeq, Nov 2013].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            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 :: AB124848.1, J04056.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000290349.11/ ENSP00000290349.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
            COMPLETENESS: full length.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-1208              AB124848.1         101-1308
FEATURES             Location/Qualifiers
     source          1..1208
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.12"
     gene            1..1208
                     /gene="CBR1"
                     /gene_synonym="CBR; hCBR1; PG-9-KR; SDR21C1"
                     /note="carbonyl reductase 1"
                     /db_xref="GeneID:873"
                     /db_xref="HGNC:HGNC:1548"
                     /db_xref="MIM:114830"
     exon            1..381
                     /gene="CBR1"
                     /gene_synonym="CBR; hCBR1; PG-9-KR; SDR21C1"
                     /inference="alignment:Splign:2.1.0"
     CDS             93..926
                     /gene="CBR1"
                     /gene_synonym="CBR; hCBR1; PG-9-KR; SDR21C1"
                     /EC_number="1.1.1.189"
                     /EC_number="1.1.1.197"
                     /EC_number="1.1.1.184"
                     /EC_number="1.1.1.196"
                     /EC_number="1.1.1.71"
                     /note="isoform 1 is encoded by transcript variant 1;
                     carbonyl reductase (NADPH) 1; prostaglandin-E(2)
                     9-reductase; prostaglandin 9-ketoreductase; carbonyl
                     reductase [NADPH] 1; 20-beta-hydroxysteroid dehydrogenase;
                     NADPH-dependent carbonyl reductase 1;
                     15-hydroxyprostaglandin dehydrogenase; short chain
                     dehydrogenase/reductase family 21C member 1; epididymis
                     secretory sperm binding protein; alcohol dehydrogenase
                     [NAD(P)+] CBR1"
                     /codon_start=1
                     /product="carbonyl reductase [NADPH] 1 isoform 1"
                     /protein_id="NP_001748.1"
                     /db_xref="CCDS:CCDS13641.1"
                     /db_xref="GeneID:873"
                     /db_xref="HGNC:HGNC:1548"
                     /db_xref="MIM:114830"
                     /translation="MSSGIHVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQ
                     AAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVLVNNAGIAFKVADPTP
                     FHIQAEVTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSIMSVRALKSCSPELQQKFRS
                     ETITEEELVGLMNKFVEDTKKGVHQKEGWPSSAYGVTKIGVTVLSRIHARKLSEQRKG
                     DKILLNACCPGWVRTDMAGPKATKSPEEGAETPVYLALLPPDAEGPHGQFVSEKRVEQ
                     W"
     exon            382..489
                     /gene="CBR1"
                     /gene_synonym="CBR; hCBR1; PG-9-KR; SDR21C1"
                     /inference="alignment:Splign:2.1.0"
     exon            490..1208
                     /gene="CBR1"
                     /gene_synonym="CBR; hCBR1; PG-9-KR; SDR21C1"
                     /inference="alignment:Splign:2.1.0"
     regulatory      1187..1192
                     /regulatory_class="polyA_signal_sequence"
                     /gene="CBR1"
                     /gene_synonym="CBR; hCBR1; PG-9-KR; SDR21C1"
                     /note="hexamer: AATAAA"
     polyA_site      1208
                     /gene="CBR1"
                     /gene_synonym="CBR; hCBR1; PG-9-KR; SDR21C1"
                     /note="major polyA site"
ORIGIN      
        1 agactcgagc agtctctgga acacgctgcg gggctcccgg gcctgagcca ggtctgttct
       61 ccacgcaggt gttccgcgcg ccccgttcag ccatgtcgtc cggcatccat gtagcgctgg
      121 tgactggagg caacaagggc atcggcttgg ccatcgtgcg cgacctgtgc cggctgttct
      181 cgggggacgt ggtgctcacg gcgcgggacg tgacgcgggg ccaggcggcc gtacagcagc
      241 tgcaggcgga gggcctgagc ccgcgcttcc accagctgga catcgacgat ctgcagagca
      301 tccgcgccct gcgcgacttc ctgcgcaagg agtacggggg cctggacgtg ctggtcaaca
      361 acgcgggcat cgccttcaag gttgctgatc ccacaccctt tcatattcaa gctgaagtga
      421 cgatgaaaac aaatttcttt ggtacccgag atgtgtgcac agaattactc cctctaataa
      481 aaccccaagg gagagtggtg aacgtatcta gcatcatgag cgtcagagcc cttaaaagct
      541 gcagcccaga gctgcagcag aagttccgca gtgagaccat cactgaggag gagctggtgg
      601 ggctcatgaa caagtttgtg gaggatacaa agaagggagt gcaccagaag gagggctggc
      661 ccagcagcgc atacggggtg acgaagattg gcgtcaccgt tctgtccagg atccacgcca
      721 ggaaactgag tgagcagagg aaaggggaca agatcctcct gaatgcctgc tgcccagggt
      781 gggtgagaac tgacatggcg ggacccaagg ccaccaagag cccagaagaa ggtgcagaga
      841 cccctgtgta cttggccctt ttgcccccag atgctgaggg tccccatgga caatttgttt
      901 cagagaagag agttgaacag tggtgagctg ggctcacagc tccatccatg ggccccattt
      961 tgtaccttgt cctgagttgg tccaaagggc atttacaatg tcataaatat ccttatataa
     1021 gaaaaaaaat gatctcttat caattagcac tcactaatgt actactaatt gagcaaccta
     1081 cgcactcagt tgactacgta aatctgtcag gtcttttgtg atttcctctg atgcaggaga
     1141 ggaaaaattg taattgatga aaataatgaa tgaaaatcaa cagatgaata aatggttctt
     1201 tataagtg
//
