ID   HPPD_MOUSE              Reviewed;         393 AA.
AC   P49429; P97322; Q3UEQ0; Q91WV9;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 76.
DE   RecName: Full=4-hydroxyphenylpyruvate dioxygenase;
DE            EC=1.13.11.27;
DE   AltName: Full=4-hydroxyphenylpyruvic acid oxidase;
DE            Short=HPPDase;
DE            Short=4HPPD;
DE            Short=HPD;
DE   AltName: Full=F Alloantigen;
DE            Short=F protein;
GN   Name=Hpd;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   MEDLINE=95293368; PubMed=7774914; DOI=10.1016/0888-7543(95)80122-3;
RA   Endo F., Awata H., Katoh H., Matsuda I.;
RT   "A nonsense mutation in the 4-hydroxyphenylpyruvic acid dioxygenase
RT   gene (Hpd) causes skipping of the constitutive exon and
RT   hypertyrosinemia in mouse strain III.";
RL   Genomics 25:164-169(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-379, AND VARIANT ASN-104.
RC   STRAIN=CBA; TISSUE=Liver;
RX   MEDLINE=91243739; PubMed=1709870; DOI=10.1002/eji.1830210521;
RA   Schofield J.P., Vijayakumar R.K., Oliveira D.B.G.;
RT   "Sequences of the mouse F protein alleles and identification of a T
RT   cell epitope.";
RL   Eur. J. Immunol. 21:1235-1240(1991).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- CATALYTIC ACTIVITY: 4-hydroxyphenylpyruvate + O(2) = homogentisate
CC       + CO(2).
CC   -!- COFACTOR: Binds 1 iron ion per subunit (By similarity).
CC   -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC       acetoacetic acid and fumarate from L-phenylalanine: step 3/6.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane;
CC       Peripheral membrane protein (By similarity).
CC   -!- POLYMORPHISM: There are two alleles (F1 and F2), F2 has Asp-104
CC       and F1 has Asn-104. Mice are completely tolerant to the self form
CC       of the protein, but make a good antibody response to immunization
CC       with the non-self form.
CC   -!- DISEASE: Defects in Hpd are the cause of tyrosinemia type III.
CC   -!- SIMILARITY: Belongs to the 4HPPD family.
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DR   EMBL; D29987; BAA06267.1; -; mRNA.
DR   EMBL; AK149416; BAE28861.1; -; mRNA.
DR   EMBL; BC013343; AAH13343.1; -; mRNA.
DR   EMBL; X59530; CAA42111.1; -; mRNA.
DR   IPI; IPI00554931; -.
DR   PIR; A60236; A60236.
DR   RefSeq; NP_032303.1; -.
DR   UniGene; Mm.439709; -.
DR   SMR; P49429; 8-366.
DR   PhosphoSite; P49429; -.
DR   Ensembl; ENSMUSG00000029445; Mus musculus.
DR   GeneID; 15445; -.
DR   KEGG; mmu:15445; -.
DR   NMPDR; fig|10090.3.peg.12411; -.
DR   MGI; MGI:96213; Hpd.
DR   HOGENOM; P49429; -.
DR   HOVERGEN; P49429; -.
DR   OMA; P49429; VQDRPTV.
DR   BRENDA; 1.13.11.27; 244.
DR   NextBio; 288240; -.
DR   ArrayExpress; P49429; -.
DR   Bgee; P49429; -.
DR   CleanEx; MM_HPD; -.
DR   GermOnline; ENSMUSG00000029445; Mus musculus.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003868; F:4-hydroxyphenylpyruvate dioxygenase activity; IEA:EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005956; 4OHPhenylPyrv_dOase.
DR   InterPro; IPR004360; Glyas_bleo-R_dOase.
DR   PANTHER; PTHR11959; HPP_dOase; 1.
DR   Pfam; PF00903; Glyoxalase; 2.
DR   PIRSF; PIRSF009283; HPP_dOase; 1.
DR   TIGRFAMs; TIGR01263; 4HPPD; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Dioxygenase; Iron; Membrane; Metal-binding;
KW   Oxidoreductase; Phenylalanine catabolism; Phosphoprotein;
KW   Polymorphism; Tyrosine catabolism.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    393       4-hydroxyphenylpyruvate dioxygenase.
FT                                /FTId=PRO_0000088389.
FT   METAL       183    183       Iron (By similarity).
FT   METAL       266    266       Iron (By similarity).
FT   METAL       349    349       Iron (By similarity).
FT   MOD_RES       2      2       N-acetylthreonine (By similarity).
FT   MOD_RES     250    250       Phosphoserine.
FT   VARIANT     104    104       D -> N (in allele F1).
FT   CONFLICT      2      6       TTYNN -> VDYWD (in Ref. 4).
FT   CONFLICT     64     64       Q -> R (in Ref. 1; BAA06267).
FT   CONFLICT    120    121       EP -> DA (in Ref. 4; CAA42111).
FT   CONFLICT    206    206       F -> S (in Ref. 2; BAE28861).
SQ   SEQUENCE   393 AA;  45054 MW;  70B42A4E4744744A CRC64;
     MTTYNNKGPK PERGRFLHFH SVTFWVGNAK QAASFYCNKM GFEPLAYRGL ETGSREVVSH
     VIKQGKIVFV LCSALNPWNK EMGDHLVKHG DGVKDIAFEV EDCDHIVQKA RERGAKIVRE
     PWVEQDKFGK VKFAVLQTYG DTTHTLVEKI NYTGRFLPGF EAPTYKDTLL PKLPRCNLEI
     IDHIVGNQPD QEMQSASEWY LKNLQFHRFW SVDDTQVHTE YSSLRSIVVT NYEESIKMPI
     NEPAPGRKKS QIQEYVDYNG GAGVQHIALK TEDIITAIRH LRERGTEFLA APSSYYKLLR
     ENLKSAKIQV KESMDVLEEL HILVDYDEKG YLLQIFTKPM QDRPTLFLEV IQRHNHQGFG
     AGNFNSLFKA FEEEQALRGN LTDLEPNGVR SGM
//