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Pah phenylalanine hydroxylase [ Rattus norvegicus (Norway rat) ]

Gene ID: 24616, updated on 14-Nov-2024

Summary

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Official Symbol
Pahprovided by RGD
Official Full Name
phenylalanine hydroxylaseprovided by RGD
Primary source
RGD:3248
See related
EnsemblRapid:ENSRNOG00000004302 AllianceGenome:RGD:3248
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Rattus norvegicus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Summary
Enables several functions, including identical protein binding activity; iron ion binding activity; and phenylalanine 4-monooxygenase activity. Involved in L-phenylalanine metabolic process; protein hydroxylation; and tyrosine biosynthetic process, by oxidation of phenylalanine. Human ortholog(s) of this gene implicated in intellectual disability and phenylketonuria. Orthologous to human PAH (phenylalanine hydroxylase). [provided by Alliance of Genome Resources, Nov 2024]
Expression
Biased expression in Liver (RPKM 3669.4) and Kidney (RPKM 3394.4) See more
Orthologs
human mouse all
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Genomic context

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See Pah in Genome Data Viewer
Location:
7q13
Exon count:
15
Annotation release Status Assembly Chr Location
RS_2024_02 current GRCr8 (GCF_036323735.1) 7 NC_086025.1 (23793096..23885631)
RS_2023_06 previous assembly mRatBN7.2 (GCF_015227675.2) 7 NC_051342.1 (21933179..21998134)
106 previous assembly Rnor_6.0 (GCF_000001895.5) 7 NC_005106.4 (28066639..28129772)

Chromosome 7 - NC_086025.1Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC120093792 Neighboring gene uncharacterized LOC134479793 Neighboring gene achaete-scute family bHLH transcription factor 1 Neighboring gene mesoderm posterior bHLH transcription factor 2, pseudogene 1 Neighboring gene uncharacterized LOC120093845

Genomic regions, transcripts, and products

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Go to nucleotide: Graphics FASTA GenBank

Expression

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  • Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
  • Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
  • BioProject: PRJNA238328
  • Publication: PMID 24510058
  • Analysis date: Mon Jun 6 17:44:12 2016

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Manipulation of a cation-pi sandwich reveals conformational flexibility in phenylalanine hydroxylase.
    Title: Manipulation of a cation-π sandwich reveals conformational flexibility in phenylalanine hydroxylase.
  2. 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
    Title: Domain Movements upon Activation of Phenylalanine Hydroxylase Characterized by Crystallography and Chromatography-Coupled Small-Angle X-ray Scattering.
  3. The results identify the location of the allosteric site as the interface of the regulatory domain dimer formed in activated PheH.
    Title: Identification of the Allosteric Site for Phenylalanine in Rat Phenylalanine Hydroxylase.
  4. 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
    Title: First structure of full-length mammalian phenylalanine hydroxylase reveals the architecture of an autoinhibited tetramer.
  5. allosteric activation of phenylalanine hydroxylase is linked to dimerization of regulatory domains
    Title: The Amino Acid Specificity for Activation of Phenylalanine Hydroxylase Matches the Specificity for Stabilization of Regulatory Domain Dimers.
  6. Data suggest that phenylalanine [concentration-dependent] activation of phenylalanine hydroxylase does not involve the active site; mutating the active-site residue Arg270 to lysine abolishes phenylalanine-dependent enzyme activation.
    Title: Activation of phenylalanine hydroxylase by phenylalanine does not require binding in the active site.
  7. the conformational change upon phosphorylation of phenylalanine hydroxylase is different from and less extensive than that upon phenylalanine activation.
    Title: Regulation of phenylalanine hydroxylase: conformational changes upon phosphorylation detected by H/D exchange and mass spectrometry.
  8. A new model for allosteric regulation of phenylalanine hydroxylase: implications for disease and therapeutics.
    Title: A new model for allosteric regulation of phenylalanine hydroxylase: implications for disease and therapeutics.
  9. the regulatory domain of phenylalanine hydroxylase can bind phenylalanine
    Title: Direct evidence for a phenylalanine site in the regulatory domain of phenylalanine hydroxylase.
  10. Metal ligand mutants of Pah are characterized.
    Title: Characterization of metal ligand mutants of phenylalanine hydroxylase: Insights into the plasticity of a 2-histidine-1-carboxylate triad.
Submit: New GeneRIF Correction See all GeneRIFs (11)

Pathways from PubChem

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Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Markers

Homology

Gene Ontology Provided by RGD

Function Evidence Code Pubs
enables amino acid binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables identical protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables iron ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables iron ion binding IEA
Inferred from Electronic Annotation
more info
  
enables phenylalanine 4-monooxygenase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables phenylalanine 4-monooxygenase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables phenylalanine 4-monooxygenase activity IEA
Inferred from Electronic Annotation
more info
  
enables phenylalanine 4-monooxygenase activity ISO
Inferred from Sequence Orthology
more info
  
Process Evidence Code Pubs
involved_in L-phenylalanine catabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in L-phenylalanine metabolic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in protein hydroxylation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in tyrosine biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in tyrosine biosynthetic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in tyrosine biosynthetic process, by oxidation of phenylalanine IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in tyrosine biosynthetic process, by oxidation of phenylalanine IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
phenylalanine-4-hydroxylase
Names
phe-4-monooxygenase
NP_036751.2
XP_038934345.1
XP_063119065.1

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_012619.2 → NP_036751.2  phenylalanine-4-hydroxylase

    See identical proteins and their annotated locations for NP_036751.2

    Status: PROVISIONAL

    Source sequence(s)
    BC078881
    UniProtKB/Swiss-Prot
    P04176
    UniProtKB/TrEMBL
    F7FDL3, Q6AYW2
    Related
    ENSRNOP00000005844.4, ENSRNOT00000005844.9
    Conserved Domains (3) summary
    TIGR01268
    Location:20 → 452
    Phe4hydrox_tetr; phenylalanine-4-hydroxylase, tetrameric form
    cd04931
    Location:21 → 110
    ACT_PAH; ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, phenylalanine hydroxylases (PAH)
    pfam00351
    Location:119 → 449
    Biopterin_H; Biopterin-dependent aromatic amino acid hydroxylase

RefSeqs of Annotated Genomes: GCF_036323735.1-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCr8

Genomic

  1. NC_086025.1 Reference GRCr8

    Range
    23793096..23885631
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_063262995.1 → XP_063119065.1  phenylalanine-4-hydroxylase isoform X1

    UniProtKB/TrEMBL
    F7FDL3, Q6AYW2
    Related
    ENSRNOP00000100444.1, ENSRNOT00000141209.1

  2. XM_039078417.2 → XP_038934345.1  phenylalanine-4-hydroxylase isoform X2

    Conserved Domains (1) summary
    pfam00351
    Location:32 → 362
    Biopterin_H; Biopterin-dependent aromatic amino acid hydroxylase
Nucleotide Protein Strain
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P04176.3 GenPept UniProtKB/Swiss-Prot:P04176

Gene LinkOut

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