LOCUS       NM_001007601             776 bp    mRNA    linear   ROD 04-APR-2024
DEFINITION  Rattus norvegicus pterin-4 alpha-carbinolamine dehydratase 1
            (Pcbd1), mRNA.
ACCESSION   NM_001007601 XM_342135
VERSION     NM_001007601.2
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 776)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   2  (bases 1 to 776)
  AUTHORS   Rho,H., Jones,C.N. and Rose,R.B.
  TITLE     Kinetic stability may determine the interaction dynamics of the
            bifunctional protein DCoH1, the dimerization cofactor of the
            transcription factor HNF-1alpha
  JOURNAL   Biochemistry 49 (47), 10187-10197 (2010)
   PUBMED   21047120
  REMARK    GeneRIF: a point mutation at the DCoH1 tetramer interface, Thr 51
            Ser, overcomes the dissociation barrier of the homotetramer and
            increases the interaction with HNF-1alpha.
REFERENCE   3  (bases 1 to 776)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   4  (bases 1 to 776)
  AUTHORS   Rose,R.B., Pullen,K.E., Bayle,J.H., Crabtree,G.R. and Alber,T.
  TITLE     Biochemical and structural basis for partially redundant enzymatic
            and transcriptional functions of DCoH and DCoH2
  JOURNAL   Biochemistry 43 (23), 7345-7355 (2004)
   PUBMED   15182178
REFERENCE   5  (bases 1 to 776)
  AUTHORS   Bossow,S., Riepl,S. and Igo-Kemenes,T.
  TITLE     Characterization of the chicken and rat DCoH gene domains using an
            improved ligation-mediated PCR method
  JOURNAL   Biol Chem 379 (11), 1359-1365 (1998)
   PUBMED   9865610
REFERENCE   6  (bases 1 to 776)
  AUTHORS   Johnen,G., Kowlessur,D., Citron,B.A. and Kaufman,S.
  TITLE     Characterization of the wild-type form of 4a-carbinolamine
            dehydratase and two naturally occurring mutants associated with
            hyperphenylalaninemia
  JOURNAL   Proc Natl Acad Sci U S A 92 (26), 12384-12388 (1995)
   PUBMED   8618906
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1996 Apr 30;93(9):4519]
REFERENCE   7  (bases 1 to 776)
  AUTHORS   Ficner,R., Sauer,U.H., Stier,G. and Suck,D.
  TITLE     Three-dimensional structure of the bifunctional protein PCD/DCoH, a
            cytoplasmic enzyme interacting with transcription factor HNF1
  JOURNAL   EMBO J 14 (9), 2034-2042 (1995)
   PUBMED   7744010
REFERENCE   8  (bases 1 to 776)
  AUTHORS   Hauer,C.R., Rebrin,I., Thony,B., Neuheiser,F., Curtius,H.C.,
            Hunziker,P., Blau,N., Ghisla,S. and Heizmann,C.W.
  TITLE     Phenylalanine hydroxylase-stimulating protein/pterin-4
            alpha-carbinolamine dehydratase from rat and human liver.
            Purification, characterization, and complete amino acid sequence
  JOURNAL   J Biol Chem 268 (7), 4828-4831 (1993)
   PUBMED   8444860
REFERENCE   9  (bases 1 to 776)
  AUTHORS   Citron,B.A., Davis,M.D., Milstien,S., Gutierrez,J., Mendel,D.B.,
            Crabtree,G.R. and Kaufman,S.
  TITLE     Identity of 4a-carbinolamine dehydratase, a component of the
            phenylalanine hydroxylation system, and DCoH, a transregulator of
            homeodomain proteins
  JOURNAL   Proc Natl Acad Sci U S A 89 (24), 11891-11894 (1992)
   PUBMED   1465414
  REMARK    GeneRIF: Rat Pcbd1 is a moonlighting protein that has dehydratase
            activity in addition to functioning as a cofactor which regulates
            HNF1alpha.
REFERENCE   10 (bases 1 to 776)
  AUTHORS   Mendel,D.B., Khavari,P.A., Conley,P.B., Graves,M.K., Hansen,L.P.,
            Admon,A. and Crabtree,G.R.
  TITLE     Characterization of a cofactor that regulates dimerization of a
            mammalian homeodomain protein
  JOURNAL   Science 254 (5039), 1762-1767 (1991)
   PUBMED   1763325
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM060466.1, FM067129.1 and DV724713.1.
            
            On Jan 23, 2014 this sequence version replaced NM_001007601.1.
            
            Summary: This gene encodes a member of the
            pterin-4-alpha-carbinolamine dehydratase family. The encoded
            protein has been identified as a moonlighting protein based on its
            ability to perform mechanistically distinct functions. The encoded
            protein functions as both a dehydratase involved in
            tetrahydrobiopterin biosynthesis, and as a cofactor for
            HNF1A-dependent transcription. [provided by RefSeq, Jan 2014].
            
            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 :: FM060466.1, FM067129.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            multifunctional gene product(s) :: PMID: 1465414
            RefSeq Select criteria          :: based on conservation,
                                               expression, longest protein
            ##RefSeq-Attributes-END##
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-23                FM060466.1         1-23
            24-628              FM067129.1         1-605
            629-776             DV724713.1         438-585
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Rattus norvegicus"
                     /mol_type="mRNA"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q11"
     gene            1..776
                     /gene="Pcbd1"
                     /gene_synonym="DCoH; Pcbd; Pcd; Phs; TCF1"
                     /note="pterin-4 alpha-carbinolamine dehydratase 1"
                     /db_xref="GeneID:29700"
                     /db_xref="RGD:3263"
     exon            1..41
                     /gene="Pcbd1"
                     /gene_synonym="DCoH; Pcbd; Pcd; Phs; TCF1"
                     /inference="alignment:Splign:2.1.0"
     CDS             39..353
                     /gene="Pcbd1"
                     /gene_synonym="DCoH; Pcbd; Pcd; Phs; TCF1"
                     /EC_number="4.2.1.96"
                     /note="dimerization cofactor of HNF1; pterin carbinolamine
                     dehydratase; 4-alpha-hydroxy-tetrahydropterin dehydratase;
                     phenylalanine hydroxylase-stimulating protein;
                     6-pyruvoyl-tetrahydropterin synthase/dimerization cofactor
                     of hepatocyte nuclear factor 1 alpha (TCF1); pterin-4
                     alpha-carbinolamine dehydratase/dimerization cofactor of
                     hepatocyte nuclear factor 1 alpha"
                     /codon_start=1
                     /product="pterin-4-alpha-carbinolamine dehydratase"
                     /protein_id="NP_001007602.1"
                     /db_xref="GeneID:29700"
                     /db_xref="RGD:3263"
                     /translation="MAGKAHRLSAEERDQLLPNLRAVGWNELEGRDAIFKQFHFKDFN
                     RAFGFMTRVALQAEKLDHHPEWFNVYNKVHITLSTHECAGLSERDINLASFIEQVAVS
                     MT"
     exon            42..173
                     /gene="Pcbd1"
                     /gene_synonym="DCoH; Pcbd; Pcd; Phs; TCF1"
                     /inference="alignment:Splign:2.1.0"
     exon            174..254
                     /gene="Pcbd1"
                     /gene_synonym="DCoH; Pcbd; Pcd; Phs; TCF1"
                     /inference="alignment:Splign:2.1.0"
     exon            255..776
                     /gene="Pcbd1"
                     /gene_synonym="DCoH; Pcbd; Pcd; Phs; TCF1"
                     /inference="alignment:Splign:2.1.0"
ORIGIN      
        1 ctctccctcg ctgacgccac ctgcttcccg cactggacat ggctggcaag gcacacaggc
       61 tgagtgctga ggaacgggac cagctgctgc caaacctgcg ggctgtgggg tggaatgaac
      121 tggaaggccg agatgccatc ttcaaacagt tccattttaa agacttcaac agggcttttg
      181 gcttcatgac aagagtcgcc ctgcaggctg aaaagctgga ccaccatccc gagtggttta
      241 acgtgtacaa caaggtccat atcaccttga gcacccacga atgtgccggt ctttctgaac
      301 gggatataaa cctggccagc ttcatcgaac aagttgccgt gtctatgaca tagatctacc
      361 ctgcctccta tttccttagg ggaaaggaga aggagtgact ggaggaggaa cccagggagg
      421 gaaccaagga ggctggccct tgctccctga ctcttgcggt gaccaccatc tccgtcaggg
      481 aggggtatga gtccctccct gtgcagaacg atgcccatgt tcctggtgcc agcctcctca
      541 ctggggctct gccatgttat aatttgaata agctctccca ttttctatag agttcctagc
      601 ctcagttgtg tcccaggctg cctcttgctc cttgtctacc ggttctagtt aattttccaa
      661 gtagctgtga taaagcatga cagaaagtcc aattcagacc ctactaaaac aaaccccaat
      721 atattatgga aacagtgctt ttatgcctcc aataaaacca tgctatcgat gggctc
//
