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P17290 (TPH1_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Tryptophan 5-hydroxylase 1
EC=1.14.16.4
Alternative name(s):
Tryptophan 5-monooxygenase 1
Gene names
Name:TPH1
Synonyms:TPH
OrganismOryctolagus cuniculus (Rabbit) [Complete proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length444 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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

Homotetramer. Ref.3

Sequence similarities

Belongs to the biopterin-dependent aromatic amino acid hydroxylase family.

Contains 1 ACT domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 444444Tryptophan 5-hydroxylase 1
PRO_0000205570

Regions

Domain18 – 9275ACT

Sites

Metal binding2721Iron By similarity
Metal binding2771Iron By similarity
Metal binding3171Iron By similarity
Binding site2351Tryptophan By similarity
Binding site2571Tryptophan By similarity
Binding site2651Tryptophan By similarity
Binding site3361Tryptophan By similarity
Binding site3661Tryptophan; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue581Phosphoserine; by PKA Potential

Experimental info

Sequence conflict1021M → L in AAA31487. Ref.1
Sequence conflict1511L → S in AAA67051. Ref.2
Sequence conflict202 – 2032KY → ND in AAA31487. Ref.1
Sequence conflict2071R → Q in AAA67051. Ref.2
Sequence conflict3901T → K in AAA31487. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P17290 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: BF182451B28ECD80

FASTA44451,118
        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

« Hide

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.
[3]"Identification of amino-terminal sequences contributing to tryptophan hydroxylase tetramer formation."
Yohrling G.J. IV, Mockus S.M., Vrana K.E.
J. Mol. Neurosci. 12:23-34(1999) [PubMed: 10636468] [Abstract]
Cited for: SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M17250 mRNA. Translation: AAA31487.1.
L29305 mRNA. Translation: AAA67051.1.
PIRS51199.
RefSeqNP_001075741.1. NM_001082272.1.
NP_001093425.1. NM_001099955.1.
UniGeneOcu.2025.
Ocu.6909.

3D structure databases

ProteinModelPortalP17290.
SMRP17290. Positions 104-439.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009100.
100101558.

Organism-specific databases

CTD121278.
7166.

Phylogenomic databases

HOVERGENHBG006841.

Family and domain databases

InterProIPR002912. 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]
Gene3DG3DSA:1.10.800.10. Aaa_hydroxylase. 1 hit.
PANTHERPTHR11473. Aaa_hydroxylase. 1 hit.
PfamPF01842. ACT. 1 hit.
PF00351. Biopterin_H. 1 hit.
[Graphical view]
PIRSFPIRSF000336. TH. 1 hit.
PRINTSPR00372. FYWHYDRXLASE.
SUPFAMSSF56534. Aaa_hydroxylase. 1 hit.
TIGRFAMsTIGR01270. Trp_5_monoox. 1 hit.
PROSITEPS00367. BH4_AAA_HYDROXYL_1. 1 hit.
PS51410. BH4_AAA_HYDROXYL_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTPH1_RABIT
AccessionPrimary (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: October 19, 2011
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents