Reviewed, UniProtKB/Swiss-Prot P17290 (TPH1_RABIT)

Names and origin

Protein names

Recommended name:
    Tryptophan 5-hydroxylase 1
    EC=1.14.16.4
Alternative name(s):
    Tryptophan 5-monooxygenase 1

Gene names

Name:	TPH1
Synonyms:	TPH

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	444 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	L-tryptophan + tetrahydrobiopterin + O2 = 5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin.
Cofactor	Fe2+ ion.
Pathway	Aromatic compound metabolism; serotonin biosynthesis; serotonin from L-tryptophan: step 1/2.
Subunit structure	Multimer of identical subunits.
Sequence similarities	Belongs to the biopterin-dependent aromatic amino acid hydroxylase family. Contains 1 ACT domain.

Ontologies

Keywords
Biological process	Serotonin biosynthesis
Ligand	Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	aromatic amino acid family metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW serotonin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	amino acid binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW tryptophan 5-monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 444	444	Tryptophan 5-hydroxylase 1		PRO_0000205570
Regions
	Domain	18 – 92	75	ACT
Sites
	Metal binding	272	1	Iron By similarity
	Metal binding	277	1	Iron By similarity
	Metal binding	317	1	Iron By similarity
Amino acid modifications
	Modified residue	58	1	Phosphoserine; by PKA Potential
Experimental info
	Sequence conflict	102	1	M → L in AAA31487. Ref.1
	Sequence conflict	151	1	L → S in AAA67051. Ref.2
	Sequence conflict	202 – 203	2	KY → ND in AAA31487. Ref.1
	Sequence conflict	207	1	R → Q in AAA67051. Ref.2
	Sequence conflict	390	1	T → K in AAA31487. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P17290-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: BF182451B28ECD80	FASTA	444	51,118
	10 20 30 40 50 60 MIEDNKENKD HSLERGRATL IFSLKNEVGG LIKALKIFQE KHVNLLHIES RKSKRRNSEF 70 80 90 100 110 120 EIFVDCDTNR EQLNDIFHLL KSHTNVLSVT PPDNFTMKEE GMESVPWFPK KISDLDHCAN 130 140 150 160 170 180 RVLMYGSELD ADHPGFKDNV YRKRRKYFAD LAMSYKYGDP IPKVEFTEEE IKTWGTVFRE 190 200 210 220 230 240 LNKLYPTHAC REYLKNLPLL SKYCGYREDN IPQLEDISNF LKERTGFSIR PVAGYLSPRD 250 260 270 280 290 300 FLSGLAFRVF HCTQYVRHSS DPFYTPEPDT CHELLGHVPL LAEPSFAQFS QEIGLASLGA 310 320 330 340 350 360 SEEAVQKLAT CYFFTVEFGL CKQDGQLRVF GAGLLSSISE LKHVLSGHAK VKPFDPKITY 370 380 390 400 410 420 KQECLITTFQ DVYFVSESFE DAKEKMREFT KTIKRPFGVK YNPYTRSIQI LKDAKSITNA 430 440 MNELRHDLDV VSDALGKVSR QLSV

References

[1]	"Full-length cDNA for rabbit tryptophan hydroxylase: functional domains and evolution of aromatic amino acid hydroxylases." Grenett H.E., Ledley F.D., Reed L.L., Woo S.L.C. Proc. Natl. Acad. Sci. U.S.A. 84:5530-5534(1987) [PubMed: 3475690] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning and expression of rabbit and human brain tryptophan hydroxylase cDNA in Escherichia coli." Tipper J.P., Citron B.A., Ribeiro P., Kaufman S. Arch. Biochem. Biophys. 315:445-453(1994) [PubMed: 7986090] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M17250 mRNA. Translation: AAA31487.1. L29305 mRNA. Translation: AAA67051.1.
PIR	S51199.
RefSeq	NP_001075741.1. NP_001093425.1.
UniGene	Ocu.2025 Ocu.6909
3D structure databases
SMR	P17290. Positions 16-87, 104-439.
ModBase	Search...
Genome annotation databases
GeneID	100009100. 100101558.
Organism-specific databases
CTD	100009100. 100101558.
Phylogenomic databases
HOVERGEN	P17290.
Enzyme and pathway databases
BRENDA	1.14.16.4. 255.
Family and domain databases
InterPro	IPR002912. ACT_bd. IPR001273. ArAA_hydroxylase. IPR018301. ArAA_hydroxylase_Fe/CU_BS. IPR019774. Aromatic-AA_hydroxylase_C. IPR005963. Trp_5_mOase. IPR019773. Tyrosine_3-monooxygenase-like. [Graphical view]
Gene3D	G3DSA:1.10.800.10. Aaa_hydroxylase. 1 hit.
PANTHER	PTHR11473. Aaa_hydroxylase. 1 hit.
Pfam	PF01842. ACT. 1 hit. PF00351. Biopterin_H. 1 hit. [Graphical view]
PIRSF	PIRSF000336. TH. 1 hit.
PRINTS	PR00372. FYWHYDRXLASE.
TIGRFAMs	TIGR01270. Trp_5_monoox. 1 hit.
PROSITE	PS00367. BIOPTERIN_HYDROXYL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TPH1_RABIT

Accession

Primary (citable) accession number: P17290
Secondary accession number(s): Q29523

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	November 1, 1997
Last modified:	February 9, 2010
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)