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P16331 (PH4H_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phenylalanine-4-hydroxylase

Short name=PAH
EC=1.14.16.1
Alternative name(s):
Phe-4-monooxygenase
Gene names
Name:Pah
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length453 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin.

Cofactor

Fe2+ ion.

Enzyme regulation

N-terminal region of PAH is thought to contain allosteric binding sites for phenylalanine and to constitute an "inhibitory" domain that regulates the activity of a catalytic domain in the C-terminal portion of the molecule.

Pathway

Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 1/6.

Subunit structure

Homodimer and homotetramer By similarity.

Post-translational modification

Phosphorylation at Ser-16 increases basal activity and facilitates activation by the substrate phenylalanine By similarity.

Involvement in disease

Mouse strains deficient in phenylalanine hydroxylase (Pah) were created as models of phenylketonuria (PKU).

Sequence similarities

Belongs to the biopterin-dependent aromatic amino acid hydroxylase family.

Contains 1 ACT domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 453452Phenylalanine-4-hydroxylase
PRO_0000205549

Regions

Domain36 – 11479ACT

Sites

Metal binding2851Iron By similarity
Metal binding2901Iron By similarity
Metal binding3301Iron By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.4
Modified residue161Phosphoserine; by PKA By similarity

Natural variations

Natural variant1061V → A in PAH-ENU1; mild PKU phenotype. Ref.7
Natural variant2631F → S in PAH-ENU2; severe PKU phenotype. Ref.7

Experimental info

Sequence conflict3831Q → R in CAA36205. Ref.1
Sequence conflict4321I → N in CAA36205. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P16331 [UniParc].

Last modified July 27, 2011. Version 4.
Checksum: 551F181FA59DEA5B

FASTA45351,900
        10         20         30         40         50         60 
MAAVVLENGV LSRKLSDFGQ ETSYIEDNSN QNGAVSLIFS LKEEVGALAK VLRLFEENEI 

        70         80         90        100        110        120 
NLTHIESRPS RLNKDEYEFF TYLDKRSKPV LGSIIKSLRN DIGATVHELS RDKEKNTVPW 

       130        140        150        160        170        180 
FPRTIQELDR FANQILSYGA ELDADHPGFK DPVYRARRKQ FADIAYNYRH GQPIPRVEYT 

       190        200        210        220        230        240 
EEERKTWGTV FRTLKALYKT HACYEHNHIF PLLEKYCGFR EDNIPQLEDV SQFLQTCTGF 

       250        260        270        280        290        300 
RLRPVAGLLS SRDFLGGLAF RVFHCTQYIR HGSKPMYTPE PDICHELLGH VPLFSDRSFA 

       310        320        330        340        350        360 
QFSQEIGLAS LGAPDEYIEK LATIYWFTVE FGLCKEGDSI KAYGAGLLSS FGELQYCLSD 

       370        380        390        400        410        420 
KPKLLPLELE KTACQEYTVT EFQPLYYVAE SFNDAKEKVR TFAATIPRPF SVRYDPYTQR 

       430        440        450 
VEVLDNTQQL KILADSINSE VGILCHALQK IKS 

« Hide

References

« Hide 'large scale' references
[1]"Mouse phenylalanine hydroxylase. Homology and divergence from human phenylalanine hydroxylase."
Ledley F.D., Grenett H.E., Dunbar B.S., Woo S.L.C.
Biochem. J. 267:399-406(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
Tissue: Liver.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney.
[4]Bienvenut W.V.
Submitted (JUL-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-13; 54-68; 160-169 AND 253-261, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Liver.
[5]"Amino acid sequence at the phosphorylated site of rat liver phenylalanine hydroxylase and phosphorylation of a corresponding synthetic peptide."
Wretborn M., Humble E., Ragnarsson U., Engstrom L.
Biochem. Biophys. Res. Commun. 93:403-408(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 12-21.
[6]"Sequence comparison of rat liver phenylalanine hydroxylase and its cDNA clones."
Robson K.J.H., Beattie W., James R.J., Cotton R.C.H., Morgan F.J., Woo S.L.C.
Biochemistry 23:5671-5675(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 277-294.
[7]"Characterization of mutations at the mouse phenylalanine hydroxylase locus."
McDonald J.D., Charlton C.K.
Genomics 39:402-405(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PAH-ENU1 ALA-106 AND PAH-ENU2 SER-263.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X51942 mRNA. Translation: CAA36205.1.
AC122360 Genomic DNA. No translation available.
BC013458 mRNA. Translation: AAH13458.1.
PIRS15758.
RefSeqNP_032803.2. NM_008777.3.
UniGeneMm.263539.

3D structure databases

ProteinModelPortalP16331.
SMRP16331. Positions 19-427.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP16331. 3 interactions.
MINTMINT-1855311.
STRING10090.ENSMUSP00000020241.

PTM databases

PhosphoSiteP16331.

Proteomic databases

PaxDbP16331.
PRIDEP16331.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020241; ENSMUSP00000020241; ENSMUSG00000020051.
GeneID18478.
KEGGmmu:18478.
UCSCuc007gqt.2. mouse.

Organism-specific databases

CTD5053.
MGIMGI:97473. Pah.

Phylogenomic databases

eggNOGCOG3186.
GeneTreeENSGT00390000010268.
HOGENOMHOG000233373.
HOVERGENHBG006841.
InParanoidQ91WV1.
KOK00500.
OMARYNAYTQ.
OrthoDBEOG7KM5T1.
TreeFamTF313327.

Enzyme and pathway databases

UniPathwayUPA00139; UER00337.

Gene expression databases

ArrayExpressP16331.
BgeeP16331.
CleanExMM_PAH.
GenevestigatorP16331.

Family and domain databases

Gene3D1.10.800.10. 1 hit.
InterProIPR002912. ACT_dom.
IPR001273. ArAA_hydroxylase.
IPR018301. ArAA_hydroxylase_Fe/CU_BS.
IPR019774. Aromatic-AA_hydroxylase_C.
IPR005961. Phe-4-hydroxylase_tetra.
IPR019773. Tyrosine_3-monooxygenase-like.
[Graphical view]
PANTHERPTHR11473. PTHR11473. 1 hit.
PfamPF01842. ACT. 1 hit.
PF00351. Biopterin_H. 1 hit.
[Graphical view]
PIRSFPIRSF000336. TH. 1 hit.
PRINTSPR00372. FYWHYDRXLASE.
SUPFAMSSF56534. SSF56534. 1 hit.
TIGRFAMsTIGR01268. Phe4hydrox_tetr. 1 hit.
PROSITEPS51671. ACT. 1 hit.
PS00367. BH4_AAA_HYDROXYL_1. 1 hit.
PS51410. BH4_AAA_HYDROXYL_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPAH. mouse.
NextBio294182.
PROP16331.
SOURCESearch...

Entry information

Entry namePH4H_MOUSE
AccessionPrimary (citable) accession number: P16331
Secondary accession number(s): Q91WV1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 141 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot