Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P09810 (TPH1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length444 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Homotetramer.

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_0000205571

Regions

Domain19 – 9476ACT

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

Sequences

Sequence LengthMass (Da)Tools
P09810 [UniParc].

Last modified October 1, 1989. Version 2.
Checksum: C3CF5245727CC825

FASTA44451,068
        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 

« Hide

References

[1]"Sequence of two mRNAs encoding active rat tryptophan hydroxylase."
Darmon M.C., Guibert B., Leviel V., Ehret M., Maitre M., Mallet J.
J. Neurochem. 51:312-316(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Pineal gland.
[2]"Molecular cloning and characterization of cDNA encoding tryptophan hydroxylase from rat central serotonergic neurons."
Kim K.S., Wessel T.C., Stone D.M., Carver C.H., Joh T.H., Park D.H.
Brain Res. Mol. Brain Res. 9:277-283(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Isolation of a rat pineal gland cDNA clone homologous to tyrosine and phenylalanine hydroxylases."
Darmon M.C., Grima B., Cash C.D., Maitre M., Mallet J.
FEBS Lett. 206:43-46(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 167-261.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M28000 mRNA. Translation: AAA42262.1.
X53501 mRNA. Translation: CAA37579.1.
PIRWHRTW. JL0034.
RefSeqNP_001094104.1. NM_001100634.2.
XP_006229281.1. XM_006229219.1.
XP_006229282.1. XM_006229220.1.
UniGeneRn.94788.

3D structure databases

ProteinModelPortalP09810.
SMRP09810. Positions 104-439.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000052959.

Chemistry

BindingDBP09810.
ChEMBLCHEMBL4809.

PTM databases

PhosphoSiteP09810.

Proteomic databases

PaxDbP09810.
PRIDEP09810.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000056109; ENSRNOP00000052959; ENSRNOG00000011672.
GeneID24848.
KEGGrno:24848.
UCSCRGD:3895. rat.

Organism-specific databases

CTD7166.
RGD3895. Tph1.

Phylogenomic databases

eggNOGCOG3186.
GeneTreeENSGT00390000010268.
HOGENOMHOG000233373.
HOVERGENHBG006841.
InParanoidP09810.
KOK00502.
OMATWGTVFQ.
OrthoDBEOG7KM5T1.
PhylomeDBP09810.
TreeFamTF313327.

Enzyme and pathway databases

SABIO-RKP09810.
UniPathwayUPA00846; UER00799.

Gene expression databases

GenevestigatorP09810.

Family and domain databases

Gene3D1.10.800.10. 1 hit.
InterProIPR002912. ACT_dom.
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]
PANTHERPTHR11473. PTHR11473. 1 hit.
PfamPF01842. ACT. 1 hit.
PF00351. Biopterin_H. 1 hit.
[Graphical view]
PIRSFPIRSF000336. TH. 1 hit.
PRINTSPR00372. FYWHYDRXLASE.
SUPFAMSSF56534. SSF56534. 1 hit.
TIGRFAMsTIGR01270. Trp_5_monoox. 1 hit.
PROSITEPS51671. ACT. 1 hit.
PS00367. BH4_AAA_HYDROXYL_1. 1 hit.
PS51410. BH4_AAA_HYDROXYL_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio604610.
PROP09810.

Entry information

Entry nameTPH1_RAT
AccessionPrimary (citable) accession number: P09810
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1989
Last modified: April 16, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways