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UniProtKB/Swiss-Prot entry P49429


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HPPD_MOUSE
Primary accession number P49429
Secondary accession numbers P97322 Q3UEQ0 Q91WV9
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 72)
Name and origin of the protein
Protein name 4-hydroxyphenylpyruvate dioxygenase
Synonyms EC 1.13.11.27
4-hydroxyphenylpyruvic acid oxidase
HPPDase
4HPPD
HPD
F Alloantigen
F protein
Gene name
Name: Hpd
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/c;
TISSUE=Liver;
DOI=10.1016/0888-7543(95)80122-3; PubMed=7774914 [NCBI, ExPASy, EBI, Israel, Japan]
Endo F., Awata H., Katoh H., Matsuda I.;
"A nonsense mutation in the 4-hydroxyphenylpyruvic acid dioxygenase gene (Hpd) causes skipping of the constitutive exon and hypertyrosinemia in mouse strain III.";
Genomics 25:164-169(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Liver;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Salivary gland;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-379, AND VARIANT ASN-104.
STRAIN=CBA;
TISSUE=Liver;
PubMed=1709870 [NCBI, ExPASy, EBI, Israel, Japan]
Schofield J.P., Vijayakumar R.K., Oliveira D.B.G.;
"Sequences of the mouse F protein alleles and identification of a T cell epitope.";
Eur. J. Immunol. 21:1235-1240(1991).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1073/pnas.0609836104; PubMed=17242355 [NCBI, ExPASy, EBI, Israel, Japan]
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D29987; BAA06267.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK149416; BAE28861.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013343; AAH13343.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X59530; CAA42111.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A60236; A60236.
RefSeq NP_032303.1; -.
UniGene Mm.439709
3D structure databases
SMR P49429; 8-366.
ModBase P49429.
PTM databases
PhosphoSite P49429; -.
Organism-specific databases
MGI MGI:96213; Hpd.
Gene expression databases
ArrayExpress P49429; -.
CleanEx MM_HPD; -.
GermOnline ENSMUSG00000029445; Mus musculus.
Ontologies
GO
GO:0016020; Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0003868; Molecular function: 4-hydroxyphenylpyruvate dioxygenase activity (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006559; Biological process: L-phenylalanine catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006572; Biological process: tyrosine catabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR005956; 4OHPhenylPyrv_dOase.
IPR004360; Glyas_bleo-R_dOase.
Graphical view of domain structure.
PANTHER PTHR11959; HPP_dOase; 1.
Pfam PF00903; Glyoxalase; 2.
Pfam graphical view of domain structure.
PIRSF PIRSF009283; HPP_dOase; 1.
TIGRFAMs TIGR01263; 4HPPD; 1.
Genome annotation databases
Ensembl ENSMUSG00000029445; Mus musculus. [Contig view]
GeneID 15445; -.
KEGG mmu:15445; -.
NMPDR fig|10090.3.peg.12411; -.
Phylogenomic databases
HOGENOM P49429; -.
HOVERGEN P49429; -.
Other
NextBio 288240; -.
SOURCE Hpd; Mus musculus.
ProtoNet P49429.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Cytoplasm; Dioxygenase; Iron; Membrane; Metal-binding; Oxidoreductase; Phenylalanine catabolism; Phosphoprotein; Polymorphism; Tyrosine catabolism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   393  392     4-hydroxyphenylpyruvate dioxygenase. PRO_0000088389
METAL   183   183        Iron (By similarity). 
METAL   266   266        Iron (By similarity). 
METAL   349   349        Iron (By similarity). 
MOD_RES   2     2        N-acetylthreonine (By similarity). 
MOD_RES   250   250        Phosphoserine. 
VARIANT   104   104  1     D -> N (in allele F1). 
CONFLICT   2     6        TTYNN -> VDYWD (in Ref. 4). 
CONFLICT   64    64        Q -> R (in Ref. 1; BAA06267). 
CONFLICT   120   121        EP -> DA (in Ref. 4; CAA42111). 
CONFLICT   206   206        F -> S (in Ref. 2; BAE28861). 
Sequence information
Length: 393 AA [This is the length of the unprocessed precursor] Molecular weight: 45054 Da [This is the MW of the unprocessed precursor] CRC64: 70B42A4E4744744A [This is a checksum on the sequence]
        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 

P49429 in FASTA format

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