LOCUS       NM_029901               1222 bp    mRNA    linear   ROD 08-FEB-2025
DEFINITION  Mus musculus aldo-keto reductase family 1, member C21 (Akr1c21),
            mRNA.
ACCESSION   NM_029901
VERSION     NM_029901.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (bases 1 to 1222)
  AUTHORS   Dhagat,U., Endo,S., Mamiya,H., Hara,A. and El-Kabbani,O.
  TITLE     Studies on a Tyr residue critical for the binding of coenzyme and
            substrate in mouse 3(17)alpha-hydroxysteroid dehydrogenase
            (AKR1C21): structure of the Y224D mutant enzyme
  JOURNAL   Acta Crystallogr D Biol Crystallogr 66 (Pt 2), 198-204 (2010)
   PUBMED   20124700
  REMARK    GeneRIF: mutation resulted in a change in the conformation of the
            flexible loop B, including the V-shaped groove, which is a unique
            feature of the active-site architecture of wild-type AKR1C21 and is
            formed by the side chains of Tyr224 and Trp227.
REFERENCE   2  (bases 1 to 1222)
  AUTHORS   Dhagat,U., Endo,S., Mamiya,H., Hara,A. and El-Kabbani,O.
  TITLE     Structure of the G225P/G226P mutant of mouse
            3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) ternary complex:
            implications for the binding of inhibitor and substrate
  JOURNAL   Acta Crystallogr D Biol Crystallogr 65 (Pt 3), 257-265 (2009)
   PUBMED   19237748
  REMARK    GeneRIF: Gly225 & Gly226 help determine the substrate
            stereospecificity. The G225P/G226P mutation reduced the affinity
            for both 3alpha- & 17alpha-hydroxysteroid substrates by up to
            160-fold, indicating that these residues are critical for substrate
            binding.
REFERENCE   3  (bases 1 to 1222)
  AUTHORS   Faucher,F., Cantin,L., Pereira de Jesus-Tran,K., Lemieux,M.,
            Luu-The,V., Labrie,F. and Breton,R.
  TITLE     Mouse 17alpha-hydroxysteroid dehydrogenase (AKR1C21) binds steroids
            differently from other aldo-keto reductases: identification and
            characterization of amino acid residues critical for substrate
            binding
  JOURNAL   J Mol Biol 369 (2), 525-540 (2007)
   PUBMED   17442338
  REMARK    GeneRIF: study reports a ternary complex crystal structure
            (m17alpha-HSD:NADP(+):epi-T) determined at 1.85 A resolution
            reveals a unique steroid-binding mode for an AKR enzyme
REFERENCE   4  (bases 1 to 1222)
  AUTHORS   Faucher,F., Pereira de Jesus-Tran,K., Cantin,L., Luu-The,V.,
            Labrie,F. and Breton,R.
  TITLE     Crystal structures of mouse 17alpha-hydroxysteroid dehydrogenase
            (apoenzyme and enzyme-NADP(H) binary complex): identification of
            molecular determinants responsible for the unique 17alpha-reductive
            activity of this enzyme
  JOURNAL   J Mol Biol 364 (4), 747-763 (2006)
   PUBMED   17034817
  REMARK    GeneRIF: crystal structure of the m17alpha-HSD enzyme in its
            apo-form (1.9 A resolution) as well as those of two different forms
            of this enzyme in binary complex with NADP(H) (2.9 A and 1.35 A
            resolution)(
REFERENCE   5  (bases 1 to 1222)
  AUTHORS   Bellemare,V., Faucher,F., Breton,R. and Luu-The,V.
  TITLE     Characterization of 17alpha-hydroxysteroid dehydrogenase activity
            (17alpha-HSD) and its involvement in the biosynthesis of
            epitestosterone
  JOURNAL   BMC Biochem 6, 12 (2005)
   PUBMED   16018803
  REMARK    Publication Status: Online-Only
REFERENCE   6  (bases 1 to 1222)
  AUTHORS   El-Kabbani,O., Ishikura,S., Wagner,A., Schulze-Briese,C. and
            Hara,A.
  TITLE     Crystallization and preliminary X-ray diffraction analysis of mouse
            3(17)alpha-hydroxysteroid dehydrogenase
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 61 (Pt 7), 688-690
            (2005)
   PUBMED   16511129
  REMARK    GeneRIF: X-ray diffraction analysis of mouse
            3(17)alpha-hydroxysteroid dehydrogenase
REFERENCE   7  (bases 1 to 1222)
  AUTHORS   Ishikura,S., Usami,N., Nakajima,S., Kameyama,A., Shiraishi,H.,
            Carbone,V., El-Kabbani,O. and Hara,A.
  TITLE     Characterization of two isoforms of mouse 3(17)alpha-hydroxysteroid
            dehydrogenases of the aldo-keto reductase family
  JOURNAL   Biol Pharm Bull 27 (12), 1939-1945 (2004)
   PUBMED   15577209
REFERENCE   8  (bases 1 to 1222)
  AUTHORS   Vergnes,L., Phan,J., Stolz,A. and Reue,K.
  TITLE     A cluster of eight hydroxysteroid dehydrogenase genes belonging to
            the aldo-keto reductase supergene family on mouse chromosome 13
  JOURNAL   J Lipid Res 44 (3), 503-511 (2003)
   PUBMED   12562828
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY721648.1, AY742217.1, AI882115.1 and AI035317.1.
            
            On Feb 23, 2007 this sequence version replaced NM_029901.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK020439.1, BC061057.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849385 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
            COMPLETENESS: complete on the 3' end.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-74                BY721648.1         1-74
            75-517              AY742217.1         1-443
            518-538             AI882115.1         516-536
            539-1046            AY742217.1         465-972
            1047-1222           AI035317.1         1-176               c
FEATURES             Location/Qualifiers
     source          1..1222
                     /organism="Mus musculus"
                     /mol_type="mRNA"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="13"
                     /map="13 2.56 cM"
     gene            1..1222
                     /gene="Akr1c21"
                     /gene_synonym="9430025F20Rik"
                     /note="aldo-keto reductase family 1, member C21"
                     /db_xref="GeneID:77337"
                     /db_xref="MGI:MGI:1924587"
     exon            1..158
                     /gene="Akr1c21"
                     /gene_synonym="9430025F20Rik"
                     /inference="alignment:Splign:2.1.0"
     CDS             75..1046
                     /gene="Akr1c21"
                     /gene_synonym="9430025F20Rik"
                     /EC_number="1.1.1.209"
                     /note="3(17)alpha-hydroxysteroid dehydrogenase; DD1; DD3;
                     17-alpha-HSD; dihydrodiol dehydrogenase type 1;
                     dihydrodiol dehydrogenase type 3; 3-alpha-hydroxysteroid
                     dehydrogenase; 17-alpha-hydroxysteroid dehydrogenase; 3(or
                     17)-alpha-hydroxysteroid dehydrogenase"
                     /codon_start=1
                     /product="aldo-keto reductase family 1 member C21"
                     /protein_id="NP_084177.2"
                     /db_xref="CCDS:CCDS26225.1"
                     /db_xref="GeneID:77337"
                     /db_xref="MGI:MGI:1924587"
                     /translation="MNSKCHCVILNDGNFIPVLGFGTALPLECPKSKAKELTKIAIDA
                     GFHHFDSASVYNTEDHVGEAIRSKIADGTVRREDIFYTSKVWCTSLHPELVRASLERS
                     LQKLQFDYVDLYLIHYPMALKPGEENFPVDEHGKLIFDRVDLCATWEAMEKCKDAGLT
                     KSIGVSNFNYRQLEMILNKPGLKYKPVCNQVECHPYLNQMKLLDFCKSKDIVLVAYGV
                     LGTQRYGGWVDQNSPVLLDEPVLGSMAKKYNRTPALIALRYQLQRGIVVLNTSLKEER
                     IKENMQVFEFQLSSEDMKVLDGLNRNMRYIPAAIFKGHPNWPFLDEY"
     exon            159..326
                     /gene="Akr1c21"
                     /gene_synonym="9430025F20Rik"
                     /inference="alignment:Splign:2.1.0"
     exon            327..443
                     /gene="Akr1c21"
                     /gene_synonym="9430025F20Rik"
                     /inference="alignment:Splign:2.1.0"
     exon            444..521
                     /gene="Akr1c21"
                     /gene_synonym="9430025F20Rik"
                     /inference="alignment:Splign:2.1.0"
     exon            522..644
                     /gene="Akr1c21"
                     /gene_synonym="9430025F20Rik"
                     /inference="alignment:Splign:2.1.0"
     exon            645..754
                     /gene="Akr1c21"
                     /gene_synonym="9430025F20Rik"
                     /inference="alignment:Splign:2.1.0"
     exon            755..920
                     /gene="Akr1c21"
                     /gene_synonym="9430025F20Rik"
                     /inference="alignment:Splign:2.1.0"
     exon            921..1003
                     /gene="Akr1c21"
                     /gene_synonym="9430025F20Rik"
                     /inference="alignment:Splign:2.1.0"
     exon            1004..1209
                     /gene="Akr1c21"
                     /gene_synonym="9430025F20Rik"
                     /inference="alignment:Splign:2.1.0"
     regulatory      1182..1187
                     /regulatory_class="polyA_signal_sequence"
                     /gene="Akr1c21"
                     /gene_synonym="9430025F20Rik"
                     /note="hexamer: AATAAA"
     polyA_site      1209
                     /gene="Akr1c21"
                     /gene_synonym="9430025F20Rik"
                     /note="major polyA site"
ORIGIN      
        1 gagttctcat tactaaagtg atctgtgaag gcaaacatca agctgagcca gcttattttg
       61 aagagggaca cataatgaac tccaaatgtc attgtgtcat attgaatgat ggtaacttca
      121 ttccagtgct gggttttggt actgctcttc ctctagagtg tcccaagagt aaagctaagg
      181 agctcaccaa aatagctata gatgctggtt tccatcactt tgattctgct tctgtctata
      241 atactgaaga tcatgtagga gaggccatca gaagcaagat tgctgatggc actgtaagga
      301 gagaagatat attttacacc tcaaaggttt ggtgtactag ccttcaccca gaacttgtga
      361 gagcttcctt ggaacggtca ctgcaaaaac ttcagttcga ctatgtggac ctgtatctca
      421 ttcattaccc aatggccctg aaaccaggag aagaaaattt tccagtagat gaacatggaa
      481 aattaatatt tgacagagtg gacctctgtg ccacctggga ggccatggag aagtgtaagg
      541 atgcaggact aaccaagtcc attggggtgt ctaactttaa ctatagacag ttggagatga
      601 ttctgaataa gcctgggctc aagtacaagc cggtatgcaa ccaggtagaa tgccatcctt
      661 atctcaacca aatgaaactt ctggatttct gcaaatcaaa agatattgta ttggttgcct
      721 atggtgttct aggaacacaa cgatatggag gatgggtaga ccagaattcc cctgttctct
      781 tggatgaacc agttcttggt tccatggcaa aaaaatataa tcgaactcca gccttgattg
      841 cccttcgcta ccagttacag cgtgggattg tggtcctcaa caccagtctc aaagaggagc
      901 ggatcaaaga gaacatgcag gtttttgaat tccagctgag ttcagaggat atgaaagttc
      961 ttgatggcct gaacagaaat atgcgataca tacctgctgc cattttcaag ggccacccta
     1021 attggccatt tttggatgaa tactagtatg tgaggatgtc tcctgaaaag cctatgggtg
     1081 ggacactgct cagctgctgc catctacaga cttgccactt ctctgtagca attgagaact
     1141 tcttgaagat aacaaaaaga tatcatacca ctctgaaaac aaataaaaga ctcattcttc
     1201 agcacttaaa aaaaaaaaaa aa
//
