[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0888-7543(90)90522-V; PubMed=2110547 [NCBI, ExPASy, EBI, Israel, Japan] Stoll J., Kozak C.A., Goldman D.; "Characterization and chromosomal mapping of a cDNA encoding tryptophan hydroxylase from a mouse mastocytoma cell line."; Genomics 7:88-96(1990).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=C57BL/6; TISSUE=Brain; 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).

Comments

CATALYTIC ACTIVITY: L-tryptophan + tetrahydrobiopterin + O₂ = 5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin.
COFACTOR: Fe(2+) ion.
PATHWAY: Aromatic compound metabolism; serotonin biosynthesis; serotonin from L-tryptophan: step 1/2 .
SUBUNIT: Multimer of identical subunits.
SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid hydroxylase family.
SIMILARITY: Contains 1 ACT domain.

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

J04758; AAA63401.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC072582; AAH72582.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A34582; A34582.

NP_033440.1; -.

3D structure databases

HSSP

P17752; 1MLW. [HSSP ENTRY / PDB]

P17532; 107-396.

PTM databases

P17532; -.

Organism-specific databases

MGI

MGI:98796; Tph1.

Gene expression databases

ArrayExpress

P17532; -.

CleanEx

MM_TPH1; -.

GermOnline

ENSMUSG00000040046; Mus musculus.

Ontologies

GO:0004510;	Molecular function: tryptophan 5-monooxygenase activity (inferred from direct assay from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR001273; Aaa_hydroxylase.
IPR002912; ACT_bd.
IPR005963; Tyr_5_mOase.
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

TIGR01270; Trp_5_monoox; 1.

PROSITE

PS00367; BIOPTERIN_HYDROXYL; 1.

BLOCKS

P17532.

Genome annotation databases

Ensembl

ENSMUSG00000040046; Mus musculus. [Contig view]

GeneID

21990; -.

KEGG

mmu:21990; -.

Phylogenomic databases

HOGENOM

P17532; -.

HOVERGEN

P17532; -.

Other

Tph1; Mus musculus.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Iron; Metal-binding; Monooxygenase; Oxidoreductase; Phosphoprotein; Serotonin biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 447`	`447`	`Tryptophan 5-hydroxylase 1.`	`PRO_0000205569`
`DOMAIN`	`21 95`	`75`	`ACT.`
`METAL`	`275 275`		`Iron (By similarity).`
`METAL`	`280 280`		`Iron (By similarity).`
`METAL`	`320 320`		`Iron (By similarity).`
`MOD_RES`	`61 61`		`Phosphoserine; by PKA (Potential).`

Sequence information

Length: 447 AA [This is the length of the unprocessed precursor]

Molecular weight: 51343 Da [This is the MW of the unprocessed precursor]

CRC64: 16C839F22A138BCA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIEDNKENKE NKDHSSERGR VTLIFSLENE VGGLIKVLKI FQENHVSLLH IESRKSKQRN 

        70         80         90        100        110        120 
SEFEIFVDCD ISREQLNDIF PLLKSHATVL SVDSPDQLTA KEDVMETVPW FPKKISDLDF 

       130        140        150        160        170        180 
CANRVLLYGS ELDADHPGFK DNVYRRRRKY FAELAMNYKH GDPIPKIEFT EEEIKTWGTI 

       190        200        210        220        230        240 
FRELNKLYPT HACREYLRNL PLLSKYCGYR EDNIPQLEDV SNFLKERTGF SIRPVAGYLS 

       250        260        270        280        290        300 
PRDFLSGLAF RVFHCTQYVR HSSDPLYTPE PDTCHELLGH VPLLAEPSFA QFSQEIGLAS 

       310        320        330        340        350        360 
LGASEETVQK LATCYFFTVE FGLCKQDGQL RVFGAGLLSS ISELKHALSG HAKVKPFDPK 

       370        380        390        400        410        420 
IACKQECLIT SFQDVYFVSE SFEDAKEKMR EFAKTVKRPF GLKYNPYTQS VQVLRDTKSI 

       430        440 
TSAMNELRYD LDVISDALAR VTRWPSV

P17532 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools