Phenylalanine-4-hydroxylase - Mus musculus (Mouse)

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P16331 (PH4H_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 121. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Phenylalanine-4-hydroxylase
Short name=PAH
EC=1.14.16.1

Alternative name(s):
Phe-4-monooxygenase

Gene names

Name:

Pah

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Involvement in disease	Note=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.

Ontologies

Keywords
Biological process	Phenylalanine catabolism
Disease	Disease mutation
Ligand	Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	L-phenylalanine catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	phenylalanine 4-monooxygenase activity Inferred from mutant phenotype. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4

Chain

2 – 453

452

Phenylalanine-4-hydroxylase

PRO_0000205549

Regions

Domain

36 – 111

ACT

Sites

Metal binding

285

Iron By similarity

Metal binding

290

Iron By similarity

Metal binding

330

Iron By similarity

Amino acid modifications

Modified residue

N-acetylalanine Ref.4

Modified residue

Phosphoserine; by PKA By similarity

Natural variations

Natural variant

106

V → A in PAH-ENU1; mild PKU phenotype. Ref.7

Natural variant

263

F → S in PAH-ENU2; severe PKU phenotype. Ref.7

Experimental info

Sequence conflict

383

Q → R in CAA36205. Ref.1

Sequence conflict

432

I → N in CAA36205. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P16331 [UniParc].

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

453

51,900

        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' referencesShow '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: 2334400] [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. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6.
[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: 15489334] [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, 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: 7387651] [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: 6098294] [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: 9119379] [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.
IPI	IPI00133549.
PIR	S15758.
RefSeq	NP_032803.2. NM_008777.3.
UniGene	Mm.263539.
3D structure databases
HSSP	HSSP built from PDB template 2PAH based on UniProtKB P00439.
ProteinModelPortal	P16331.
SMR	P16331. Positions 19-427.
ModBase	Search...
Protein-protein interaction databases
STRING	P16331.
PTM databases
PhosphoSite	P16331.
Proteomic databases
PRIDE	P16331.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000020241; ENSMUSP00000020241; ENSMUSG00000020051.
GeneID	18478.
KEGG	mmu:18478.
Organism-specific databases
CTD	5053.
MGI	MGI:97473. Pah.
Phylogenomic databases
eggNOG	roNOG04553.
GeneTree	ENSGT00390000010268.
HOGENOM	HBG484724.
HOVERGEN	HBG006841.
InParanoid	P16331.
OrthoDB	EOG4CNQR1.
Gene expression databases
ArrayExpress	P16331.
Bgee	P16331.
CleanEx	MM_PAH.
Genevestigator	P16331.
GermOnline	ENSMUSG00000020051. Mus musculus.
Family and domain databases
InterPro	IPR002912. ACT-bd. 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]
Gene3D	G3DSA:1.10.800.10. Aaa_hydroxylase. 1 hit.
KO	K00500.
PANTHER	PTHR11473. Aaa_hydroxylase. 1 hit.
Pfam	PF01842. ACT. 1 hit. PF00351. Biopterin_H. 1 hit. [Graphical view]
PIRSF	PIRSF000336. TH. 1 hit.
PRINTS	PR00372. FYWHYDRXLASE.
SUPFAM	SSF56534. Aaa_hydroxylase. 1 hit.
TIGRFAMs	TIGR01268. Phe4hydrox_tetr. 1 hit.
PROSITE	PS00367. BH4_AAA_HYDROXYL_1. 1 hit. PS51410. BH4_AAA_HYDROXYL_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	294182.
SOURCE	Search...

Entry information

Entry name

PH4H_MOUSE

Accession

Primary (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:	December 14, 2011
This is version 121 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents