LOCUS       NM_012619               2040 bp    mRNA    linear   ROD 11-DEC-2024
DEFINITION  Rattus norvegicus phenylalanine hydroxylase (Pah), mRNA.
ACCESSION   NM_012619
VERSION     NM_012619.2
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 2040)
  AUTHORS   Arturo,E.C., Merkel,G.W., Hansen,M.R., Lisowski,S., Almeida,D.,
            Gupta,K. and Jaffe,E.K.
  TITLE     Manipulation of a cation-pi sandwich reveals conformational
            flexibility in phenylalanine hydroxylase
  JOURNAL   Biochimie 183, 63-77 (2021)
   PUBMED   33221376
  REMARK    GeneRIF: Manipulation of a cation-pi sandwich reveals
            conformational flexibility in phenylalanine hydroxylase.
REFERENCE   2  (bases 1 to 2040)
  AUTHORS   Meisburger,S.P., Taylor,A.B., Khan,C.A., Zhang,S., Fitzpatrick,P.F.
            and Ando,N.
  TITLE     Domain Movements upon Activation of Phenylalanine Hydroxylase
            Characterized by Crystallography and Chromatography-Coupled
            Small-Angle X-ray Scattering
  JOURNAL   J Am Chem Soc 138 (20), 6506-6516 (2016)
   PUBMED   27145334
  REMARK    GeneRIF: results support a model for allostery in PheH in which
            phenylalanine stabilizes the dimerization of the regulatory domains
            and exposes the active site for substrate binding and other
            structural changes needed for activity
REFERENCE   3  (bases 1 to 2040)
  AUTHORS   Zhang,S. and Fitzpatrick,P.F.
  TITLE     Identification of the Allosteric Site for Phenylalanine in Rat
            Phenylalanine Hydroxylase
  JOURNAL   J Biol Chem 291 (14), 7418-7425 (2016)
   PUBMED   26823465
  REMARK    GeneRIF: The results identify the location of the allosteric site
            as the interface of the regulatory domain dimer formed in activated
            PheH.
REFERENCE   4  (bases 1 to 2040)
  AUTHORS   Arturo,E.C., Gupta,K., Heroux,A., Stith,L., Cross,P.J.,
            Parker,E.J., Loll,P.J. and Jaffe,E.K.
  TITLE     First structure of full-length mammalian phenylalanine hydroxylase
            reveals the architecture of an autoinhibited tetramer
  JOURNAL   Proc Natl Acad Sci U S A 113 (9), 2394-2399 (2016)
   PUBMED   26884182
  REMARK    GeneRIF: use of SAXS and X-ray crystallography together to inspect
            PAH structure provides, to our knowledge, the first complete view
            of the enzyme in a tetrameric form that was not possible with prior
            partial crystal structures
REFERENCE   5  (bases 1 to 2040)
  AUTHORS   Zhang,S., Hinck,A.P. and Fitzpatrick,P.F.
  TITLE     The Amino Acid Specificity for Activation of Phenylalanine
            Hydroxylase Matches the Specificity for Stabilization of Regulatory
            Domain Dimers
  JOURNAL   Biochemistry 54 (33), 5167-5174 (2015)
   PUBMED   26252467
  REMARK    GeneRIF: allosteric activation of phenylalanine hydroxylase is
            linked to dimerization of regulatory domains
REFERENCE   6  (bases 1 to 2040)
  AUTHORS   Eisensmith,R.C. and Woo,S.L.
  TITLE     Updated listing of haplotypes at the human phenylalanine
            hydroxylase (PAH) locus
  JOURNAL   Am J Hum Genet 51 (6), 1445-1448 (1992)
   PUBMED   1361103
REFERENCE   7  (bases 1 to 2040)
  AUTHORS   McDonald,J.D., Bode,V.C., Dove,W.F. and Shedlovsky,A.
  TITLE     Pahhph-5: a mouse mutant deficient in phenylalanine hydroxylase
  JOURNAL   Proc Natl Acad Sci U S A 87 (5), 1965-1967 (1990)
   PUBMED   2308957
REFERENCE   8  (bases 1 to 2040)
  AUTHORS   DiLella,A.G., Marvit,J., Brayton,K. and Woo,S.L.
  TITLE     An amino-acid substitution involved in phenylketonuria is in
            linkage disequilibrium with DNA haplotype 2
  JOURNAL   Nature 327 (6120), 333-336 (1987)
   PUBMED   2884570
REFERENCE   9  (bases 1 to 2040)
  AUTHORS   Dahl,H.H. and Mercer,J.F.
  TITLE     Isolation and sequence of a cDNA clone which contains the complete
            coding region of rat phenylalanine hydroxylase. Structural homology
            with tyrosine hydroxylase, glucocorticoid regulation, and use of
            alternate polyadenylation sites
  JOURNAL   J Biol Chem 261 (9), 4148-4153 (1986)
   PUBMED   2869038
REFERENCE   10 (bases 1 to 2040)
  AUTHORS   Robson,K.J., Beattie,W., James,R.J., Cotton,R.C., Morgan,F.J. and
            Woo,S.L.
  TITLE     Sequence comparison of rat liver phenylalanine hydroxylase and its
            cDNA clones
  JOURNAL   Biochemistry 23 (24), 5671-5675 (1984)
   PUBMED   6098294
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078881.1.
            
            On Oct 13, 2007 this sequence version replaced NM_012619.1.
            
            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 :: BC078881.1, M12337.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [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..2040
                     /organism="Rattus norvegicus"
                     /mol_type="mRNA"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q13"
     gene            1..2040
                     /gene="Pah"
                     /note="phenylalanine hydroxylase"
                     /db_xref="GeneID:24616"
                     /db_xref="RGD:3248"
     exon            1..149
                     /gene="Pah"
                     /inference="alignment:Splign:2.1.0"
     CDS             90..1451
                     /gene="Pah"
                     /EC_number="1.14.16.1"
                     /note="phe-4-monooxygenase"
                     /codon_start=1
                     /product="phenylalanine-4-hydroxylase"
                     /protein_id="NP_036751.2"
                     /db_xref="GeneID:24616"
                     /db_xref="RGD:3248"
                     /translation="MAAVVLENGVLSRKLSDFGQETSYIEDNSNQNGAISLIFSLKEE
                     VGALAKVLRLFEENDINLTHIESRPSRLNKDEYEFFTYLDKRSKPVLGSIIKSLRNDI
                     GATVHELSRDKEKNTVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQ
                     FADIAYNYRHGQPIPRVEYTEEEKQTWGTVFRTLKALYKTHACYEHNHIFPLLEKYCG
                     FREDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPM
                     YTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLC
                     KEGDSIKAYGAGLLSSFGELQYCLSDKPKLLPLELEKIACQEYSVTEFQPLYYVAESF
                     SDAKEKVRTFAATIPRPFSVRYDPYTQRVEVLDNTQQLKILADSINSEVGILCNALQK
                     IKS"
     exon            150..257
                     /gene="Pah"
                     /inference="alignment:Splign:2.1.0"
     exon            258..441
                     /gene="Pah"
                     /inference="alignment:Splign:2.1.0"
     exon            442..530
                     /gene="Pah"
                     /inference="alignment:Splign:2.1.0"
     exon            531..598
                     /gene="Pah"
                     /inference="alignment:Splign:2.1.0"
     exon            599..795
                     /gene="Pah"
                     /inference="alignment:Splign:2.1.0"
     exon            796..931
                     /gene="Pah"
                     /inference="alignment:Splign:2.1.0"
     exon            932..1001
                     /gene="Pah"
                     /inference="alignment:Splign:2.1.0"
     exon            1002..1058
                     /gene="Pah"
                     /inference="alignment:Splign:2.1.0"
     exon            1059..1154
                     /gene="Pah"
                     /inference="alignment:Splign:2.1.0"
     exon            1155..1288
                     /gene="Pah"
                     /inference="alignment:Splign:2.1.0"
     exon            1289..1404
                     /gene="Pah"
                     /inference="alignment:Splign:2.1.0"
     exon            1405..2017
                     /gene="Pah"
                     /inference="alignment:Splign:2.1.0"
ORIGIN      
        1 caagttaaaa ccatcagccc tcccatcctg agtgcctacc tttcccaacc ccgctgctaa
       61 gctagacacc tcactcactg agagccagca tggcagctgt tgtcctggag aatggagtcc
      121 tgagcagaaa actctcagac tttgggcagg aaacaagcta tattgaagac aactccaatc
      181 aaaatggtgc catatctctg atattctcac tcaaagagga agttggtgcc ctagccaagg
      241 tcctgcgctt atttgaggag aacgatatca acctgacaca cattgaatcc agaccttctc
      301 gtttaaacaa agatgagtat gagttcttca cttatctgga taagcgtagc aaacctgttc
      361 tgggcagcat catcaagagc ctgaggaatg acattggtgc cactgtccac gagctttccc
      421 gagacaagga aaagaacaca gtgccctggt tcccaaggac cattcaggag ttggaccgat
      481 tcgccaatca gattctcagc tatggagccg aactggatgc ggaccaccca ggctttaaag
      541 atcctgtgta ccgggcgaga cgaaagcagt ttgctgacat tgcctacaac taccgccatg
      601 gccagcccat ccctcgggtg gaatacacag aggaagagaa gcagacctgg ggaacggtgt
      661 tcaggacctt gaaggccttg tataaaacac atgcctgcta cgagcacaac cacattttcc
      721 cacttctgga aaagtactgc ggtttccgtg aagacaacat tccacagctg gaagatgttt
      781 ctcaatttct gcagacttgt actggtttcc gcctccgacc tgttgctggc ttactgtcat
      841 ctcgagattt cttgggtggc ctggccttcc gagtcttcca ctgcacacag tacattaggc
      901 atggatcgaa gcccatgtac acacctgaac ctgacatctg ccatgaactc ttgggacatg
      961 tgcctttgtt ttcagatcgc agctttgccc agttttctca ggaaattggg cttgcatcac
     1021 tgggggcacc tgatgagtac attgagaaac tggccacaat ttactggttt actgtggagt
     1081 ttgggctttg caaggaagga gattctataa aggcatatgg tgctgggctc ttgtcatcct
     1141 ttggagaatt acagtactgt ttatcagaca agccaaagct cctccccctg gagctagaga
     1201 agatagcctg ccaggagtat tctgtcacag agttccagcc cttgtactac gtggcggaga
     1261 gtttcagtga tgccaaggag aaagtgagga cttttgctgc cacgatccct cggcccttct
     1321 cggttcgcta tgacccttac actcaaaggg ttgaggtcct ggacaatact cagcagttga
     1381 agattttagc tgactccatt aatagtgagg tcggaatcct ttgcaatgcc ctgcagaaga
     1441 taaagtcgtg agcagaaaat gacgtcatgg gcagaactta ggaggtcaac cagaaatcgg
     1501 tcgatagaag tatagtaact gcctttgttc ccctgaagaa aaaaagtttt atttgaaacg
     1561 tcagctttta ttatttttgc taacacagtg gagcatcacc aaataaatca aagttctctg
     1621 aaatgaaagt gtgttaaaac cctccagggg tagatctttc agaatcacat ttgatttaga
     1681 taatctcata gcttcaattt ggtttaaaat gtaattttct cagctctcat caacattcat
     1741 caaatttggg gcttgtgtca ttggggcttc atccgttcat ttttaacctc tcaggtaagc
     1801 tctgaaggaa cacatttggc tgagtgtaaa atgtaagact gccatcaggg atgaatcatt
     1861 ccgttcagta cagattgtaa tctacaaagg gtagttttca ccttcgttca ttatggctct
     1921 gagaactgct ttgttagcct gcttacataa atctcccctg atcggagacc ctattaagat
     1981 agttacaagc aataaagttt tagagcatta tataaaaaaa aaaaaaaaaa aaaaaaaaaa
//
