Reviewed, UniProtKB/Swiss-Prot P49429 (HPPD_MOUSE)

Names and origin

Protein names

Recommended name:
    4-hydroxyphenylpyruvate dioxygenase
    EC=1.13.11.27
Alternative name(s):
    4-hydroxyphenylpyruvic acid oxidase
      Short name=HPPDase
      Short name=4HPPD
      Short name=HPD
    F Alloantigen
      Short name=F protein

Gene names

Name:

Hpd

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

Protein attributes

Sequence length	393 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	4-hydroxyphenylpyruvate + O(2) = homogentisate + CO(2).
Cofactor	Binds 1 iron ion per subunit By similarity.
Pathway	Amino-acid degradation; L-phenylalanine degradation; acetoacetic acid and fumarate from L-phenylalanine: step 3/6.
Subunit structure	Homodimer By similarity.
Subcellular location	CytoplasmBy similarity. Membrane; Peripheral membrane proteinBy similarity.
Polymorphism	There are two alleles (F1 and F2), F2 has Asp-104 and F1 has Asn-104. Mice are completely tolerant to the self form of the protein, but make a good antibody response to immunization with the non-self form.
Involvement in disease	Defects in Hpd are the cause of tyrosinemia type III.
Sequence similarities	Belongs to the 4HPPD family.

Ontologies

Keywords
Biological process	Phenylalanine catabolism Tyrosine catabolism
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Polymorphism
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	L-phenylalanine catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tyrosine catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4-hydroxyphenylpyruvate dioxygenase activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 393	392	4-hydroxyphenylpyruvate dioxygenase		PRO_0000088389
Sites
	Metal binding	183	1	Iron By similarity
	Metal binding	266	1	Iron By similarity
	Metal binding	349	1	Iron By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylthreonine By similarity
	Modified residue	250	1	Phosphoserine
Natural variations
	Natural variant	104	1	D → N in allele F1.
Experimental info
	Sequence conflict	2 – 6	5	TTYNN → VDYWD Ref.4
	Sequence conflict	64	1	Q → R in BAA06267. Ref.1
	Sequence conflict	120 – 121	2	EP → DA in CAA42111. Ref.4
	Sequence conflict	206	1	F → S in BAE28861. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P49429-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 70B42A4E4744744A	FASTA	393	45,054
	10 20 30 40 50 60 MTTYNNKGPK PERGRFLHFH SVTFWVGNAK QAASFYCNKM GFEPLAYRGL ETGSREVVSH 70 80 90 100 110 120 VIKQGKIVFV LCSALNPWNK EMGDHLVKHG DGVKDIAFEV EDCDHIVQKA RERGAKIVRE 130 140 150 160 170 180 PWVEQDKFGK VKFAVLQTYG DTTHTLVEKI NYTGRFLPGF EAPTYKDTLL PKLPRCNLEI 190 200 210 220 230 240 IDHIVGNQPD QEMQSASEWY LKNLQFHRFW SVDDTQVHTE YSSLRSIVVT NYEESIKMPI 250 260 270 280 290 300 NEPAPGRKKS QIQEYVDYNG GAGVQHIALK TEDIITAIRH LRERGTEFLA APSSYYKLLR 310 320 330 340 350 360 ENLKSAKIQV KESMDVLEEL HILVDYDEKG YLLQIFTKPM QDRPTLFLEV IQRHNHQGFG 370 380 390 AGNFNSLFKA FEEEQALRGN LTDLEPNGVR SGM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A nonsense mutation in the 4-hydroxyphenylpyruvic acid dioxygenase gene (Hpd) causes skipping of the constitutive exon and hypertyrosinemia in mouse strain III." Endo F., Awata H., Katoh H., Matsuda I. Genomics 25:164-169(1995) [PubMed: 7774914] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Liver.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Liver.
[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: Salivary gland.
[4]	"Sequences of the mouse F protein alleles and identification of a T cell epitope." Schofield J.P., Vijayakumar R.K., Oliveira D.B.G. Eur. J. Immunol. 21:1235-1240(1991) [PubMed: 1709870] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-379, VARIANT ASN-104. Strain: CBA. Tissue: Liver.
[5]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D29987 mRNA. Translation: BAA06267.1. AK149416 mRNA. Translation: BAE28861.1. BC013343 mRNA. Translation: AAH13343.1. X59530 mRNA. Translation: CAA42111.1.
PIR	A60236.
RefSeq	NP_032303.1.
UniGene	Mm.439709
3D structure databases
SMR	P49429. Positions 8-366.
ModBase	Search...
PTM databases
PhosphoSite	P49429.
Genome annotation databases
Ensembl	ENSMUSG00000029445. Mus musculus. [Contig view]
GeneID	15445.
KEGG	mmu:15445.
NMPDR	fig|10090.3.peg.12411.
Organism-specific databases
MGI	MGI:96213. Hpd.
Phylogenomic databases
HOGENOM	P49429.
HOVERGEN	P49429.
Gene expression databases
ArrayExpress	P49429.
CleanEx	MM_HPD.
GermOnline	ENSMUSG00000029445. Mus musculus.
Family and domain databases
InterPro	IPR005956. 4OHPhenylPyrv_dOase. IPR004360. Glyas_bleo-R_dOase. [Graphical view]
PANTHER	PTHR11959. HPP_dOase. 1 hit.
Pfam	PF00903. Glyoxalase. 2 hits. [Graphical view]
PIRSF	PIRSF009283. HPP_dOase. 1 hit.
TIGRFAMs	TIGR01263. 4HPPD. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	288240.
SOURCE	Search...

Entry information

Entry name

HPPD_MOUSE

Accession

Primary (citable) accession number: P49429
Secondary accession number(s): P97322, Q3UEQ0, Q91WV9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 72 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)