[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Wistar; TISSUE=Pineal gland; PubMed=3379411 [NCBI, ExPASy, EBI, Israel, Japan] Darmon M.C., Guibert B., Leviel V., Ehret M., Maitre M., Mallet J.; "Sequence of two mRNAs encoding active rat tryptophan hydroxylase."; J. Neurochem. 51:312-316(1988).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0169-328X(91)90073-7; PubMed=1645430 [NCBI, ExPASy, EBI, Israel, Japan] Kim K.S., Wessel T.C., Stone D.M., Carver C.H., Joh T.H., Park D.H.; "Molecular cloning and characterization of cDNA encoding tryptophan hydroxylase from rat central serotonergic neurons."; Brain Res. Mol. Brain Res. 9:277-283(1991).
[3]	NUCLEOTIDE SEQUENCE [MRNA] OF 167-261. DOI=10.1016/0014-5793(86)81337-0; PubMed=2875901 [NCBI, ExPASy, EBI, Israel, Japan] Darmon M.C., Grima B., Cash C.D., Maitre M., Mallet J.; "Isolation of a rat pineal gland cDNA clone homologous to tyrosine and phenylalanine hydroxylases."; FEBS Lett. 206:43-46(1986).

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

M28000; AAA42262.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X53501; CAA37579.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

JL0034; WHRTW.

NP_001094104.1; -.

3D structure databases

HSSP

P17752; 1MLW. [HSSP ENTRY / PDB]

P09810; 104-393.

PTM databases

P09810; -.

Organism-specific databases

RGD

3895; Tph1.

Gene expression databases

ArrayExpress

P09810; -.

GermOnline

ENSRNOG00000011672; Rattus norvegicus.

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

P09810.

Genome annotation databases

Ensembl

ENSRNOG00000011672; Rattus norvegicus. [Contig view]

GeneID

24848; -.

KEGG

rno:24848; -.

Phylogenomic databases

HOVERGEN

P09810; -.

Other

ProtoNet

P09810.

UniRef

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`	`1 444`	`444`	`Tryptophan 5-hydroxylase 1.`	`PRO_0000205571`
`DOMAIN`	`18 92`	`75`	`ACT.`
`METAL`	`272 272`		`Iron (By similarity).`
`METAL`	`277 277`		`Iron (By similarity).`
`METAL`	`317 317`		`Iron (By similarity).`
`MOD_RES`	`58 58`		`Phosphoserine; by PKA (Potential).`

Sequence information

Length: 444 AA [This is the length of the unprocessed precursor]

Molecular weight: 51068 Da [This is the MW of the unprocessed precursor]

CRC64: C3CF5245727CC825 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIEDNKENKD HSSERGRVTL IFSLKNEVGG LIKALKIFQE NHVNLLHIES RKSKRRNSEF 

        70         80         90        100        110        120 
EIFVDCDINR EQLNDIFPLL KSHTTVLSVD SPDQLPEKED VMETVPWFPK KISDLDFCAN 

       130        140        150        160        170        180 
RVLLYGSELD ADHPGFKDNV YRRRRKYFAE LAMNYKHGDP IPKIEFTEEE IKTWGTIFRE 

       190        200        210        220        230        240 
LNKLYPTHAC REYLRNLPLL SKYCGYREDN VPQLEDVSNF LKERTGFSIR PVAGYLSPRD 

       250        260        270        280        290        300 
FLSGLAFRVF HCTQYVRHSS DPLYTPEPDT CHELLGHVPL LAEPSFAQFS QEIGLASLGA 

       310        320        330        340        350        360 
SEETVQKLAT CYFFTVEFGL CKQDGQLRVF GAGLLSSISE LRHALSGHAK VKPFDPKVAC 

       370        380        390        400        410        420 
KQECLITSFQ DVYFVSESFE DAKEKMREFA KTVKRPFGVK YNPYTQSIQV LRDSKSITSA 

       430        440 
MNELRHDLDV VNDALARVSR WPSV

P09810 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