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UniProtKB/Swiss-Prot entry P17276


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

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Entry information
Entry name PH4H_DROME
Primary accession number P17276
Secondary accession numbers O46110 Q27599 Q27600
Integrated into Swiss-Prot on August 1, 1990
Sequence was last modified on December 1, 2000 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 100)
Name and origin of the protein
Protein name Protein henna
Synonyms None
Includes Phenylalanine-4-hydroxylase
     (PAH)
     (EC 1.14.16.1)
     (Phe-4-monooxygenase)
Tryptophan 5-monooxygenase
     (EC 1.14.16.4)
     (Tryptophan 5-hydroxylase)
     (TRH)
Gene name
Name: Hn
Synonyms: pah, Tph
ORFNames: CG7399
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Canton-S, and Oregon-R;
TISSUE=Embryo, and Head;
PubMed=1371286 [NCBI, ExPASy, EBI, Israel, Japan]
Neckameyer W.S., White K.;
"A single locus encodes both phenylalanine hydroxylase and tryptophan hydroxylase activities in Drosophila.";
J. Biol. Chem. 267:4199-4206(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0378-1119(90)90227-I; PubMed=2121612 [NCBI, ExPASy, EBI, Israel, Japan]
Morales G., Requena J.M., Jimenez-Ruiz A., Lopez M.C., Ugarte M., Alonso C.;
"Sequence and expression of the Drosophila phenylalanine hydroxylase mRNA.";
Gene 93:213-219(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Canton-S;
DOI=10.1006/bbrc.1996.1160; PubMed=8769124 [NCBI, ExPASy, EBI, Israel, Japan]
Ruiz-Vazquez P., Moulard M., Silva F.J.;
"Structure of the phenylalanine hydroxylase gene in Drosophila melanogaster and evidence of alternative promoter usage.";
Biochem. Biophys. Res. Commun. 225:238-242(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[5]
GENOME REANNOTATION.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
TISSUE=Head;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 5-93 AND 161-412 (MUTANT HN-R3).
DOI=10.1016/S0965-1748(99)00002-8; PubMed=10333570 [NCBI, ExPASy, EBI, Israel, Japan]
Ruiz-Vazquez P., Silva F.J.;
"Aberrant splicing of the Drosophila melanogaster phenylalanine hydroxylase pre-mRNA caused by the insertion of a B104/roo transposable element in the Henna locus.";
Insect Biochem. Mol. Biol. 29:311-318(1999).
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
M81833; -; NOT_ANNOTATED_CDS; Genomic_RNA.[EMBL / GenBank / DDBJ]
M32802; AAA69513.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X98116; CAA66797.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X98116; CAA66798.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014296; AAF50517.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY069306; AAL39451.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ001718; CAA04950.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ001719; CAB51601.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ001720; CAB51601.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ001722; CAB51599.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ001723; CAB51597.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A42271; A42271.
JC4888; JC4888.
JQ0766; JQ0766.
RefSeq NP_523963.2; -.
UniGene Dm.7375
3D structure databases
HSSP P00439; 2PAH. [HSSP ENTRY / PDB]
ModBase P17276.
Protein-protein interaction databases
DIP DIP:20514N; -.
IntAct P17276; -.
Enzyme and pathway databases
BioCyc DMEL-XXX-02:DMEL-XXX-02-015636-MON; -.
Organism-specific databases
FlyBase FBgn0001208; Hn.
Gene expression databases
ArrayExpress P17276; -.
GermOnline CG7399; Drosophila melanogaster.
Ontologies
GO
GO:0016597; Molecular function: amino acid binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0004505; Molecular function: phenylalanine 4-monooxygenase activity (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004510; Molecular function: tryptophan 5-monooxygenase activity (inferred from electronic annotation from EC).
GO:0006559; Biological process: L-phenylalanine catabolic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006911; Biological process: phagocytosis, engulfment (inferred from mutant phenotype from FlyBase).
GO:0006587; Biological process: serotonin biosynthetic process from tryptophan (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001273; Aaa_hydroxylase.
IPR002912; ACT_bd.
IPR005961; Phe-4-hydroxylase_tetra.
Graphical view of domain structure.
Gene3D G3DSA:1.10.800.10; Aaa_hydroxylase; 1.
PANTHER PTHR11473; Aaa_hydroxylase; 1.
Pfam PF01842; ACT; 1.
PF00351; Biopterin_H; 1.
Pfam graphical view of domain structure.
PRINTS PR00372; FYWHYDRXLASE.
ProDom PD002559; Aaa_hydroxylase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01268; Phe4hydrox_tetr; 1.
PROSITE PS00367; BIOPTERIN_HYDROXYL; 1.
ProtoNet P17276.
Genome annotation databases
Ensembl CG7399; Drosophila melanogaster. [Contig view]
GeneID 38871; -.
NMPDR fig|7227.3.peg.8736; -.
Phylogenomic databases
HOGENOM P17276; -.
Other
NextBio 810779; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Allosteric enzyme; Complete proteome; Iron; Metal-binding; Monooxygenase; Oxidoreductase; Phenylalanine catabolism; Phosphoprotein; Serotonin biosynthesis.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   452  452     Protein henna. PRO_0000205552
DOMAIN   32   108  77     ACT. 
METAL   284   284        Iron (By similarity). 
METAL   289   289        Iron (By similarity). 
METAL   329   329        Iron (By similarity). 
MOD_RES   272   272        Phosphoserine; by CaMK2 (By similarity). 
CONFLICT   28    28        E -> A (in Ref. 2; AAA69513). 
CONFLICT   39    47        KDSSLSSGA -> RIRRCPAEL (in Ref. 2; AAA69513). 
CONFLICT   55    56        FK -> LR (in Ref. 2; AAA69513). 
CONFLICT   63    71        VHIESRSSL -> CILSRILAPWF (in Ref. 2). 
CONFLICT   74   114        PGYEFFVEADGKSGALGKAIEDVKEQCSYFNIISRD YKDNA -> SSCFWRRMENRSLGKSHRGCEGAMLATLTSSCRELQGVMP (in Ref. 2). 
CONFLICT   154   154        R -> A (in Ref. 2; AAA69513). 
CONFLICT   164   164        A -> G (in Ref. 2; AAA69513). 
CONFLICT   171   171        E -> Q (in Ref. 2; AAA69513). 
CONFLICT   264   264        S -> C (in Ref. 2; AAA69513). 
CONFLICT   297   297        A -> S (in Ref. 2; AAA69513). 
CONFLICT   332   332        V -> L (in Ref. 1 and 2). 
CONFLICT   333   335        CRQ -> LAK (in Ref. 2). 
CONFLICT   370   370        V -> S (in Ref. 2; AAA69513). 
CONFLICT   449   452        KLRV -> NCASE (in Ref. 1). 
Sequence information
Length: 452 AA [This is the length of the unprocessed precursor] Molecular weight: 51660 Da [This is the MW of the unprocessed precursor] CRC64: 990F554150056867 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MYQRQVSFDK PTRVEDSAYI VEGVDIKEAR NTCLLFSPKD SSLSSGALAN ILAIFKKHDI 

        70         80         90        100        110        120 
NLVHIESRSS LRVPGYEFFV EADGKSGALG KAIEDVKEQC SYFNIISRDY KDNATAVPWF 

       130        140        150        160        170        180 
PRRIRDLDRF ANQILSYGSE LDADHPGFTD PEYRKRRKYF ADIAYNYKHG EPLPHVDYTK 

       190        200        210        220        230        240 
EEIETWGIIF RNLTKLYKTH ACREYNHVFP LLVDNCGFRE DNIPQLEDVS NFLRDCTGFT 

       250        260        270        280        290        300 
LRPVAGLLSS RDFLAGLAFR VFHSTQYIRH PSKPMYTPEP DVCHELMGHV PLFADPAFAQ 

       310        320        330        340        350        360 
FSQEIGLASL GAPDDYIEKL STIFWFTVEY GVCRQEGELK AYGAGLLSSY GELEYCLTDK 

       370        380        390        400        410        420 
PQLKDFEPEV TGVTKYPITQ FQPLYYVADS FETAKEKTIK FANSIPRPFG VRYNAYTQSV 

       430        440        450 
EVLDSKPQIS NLMDNINSEF QILQNAVAKL RV 

P17276 in FASTA format

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