Reviewed,
UniProtKB/Swiss-Prot P17290 (TPH1_RABIT)
Last modified
June 16, 2009.
Version 72.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
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 |
| ||||
| 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. |
| Sequence processing | The displayed sequence is not processed. |
| 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 | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW serotonin biosynthetic process from tryptophanInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | amino acid binding Inferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW tryptophan 5-monooxygenase activityInferred 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
| ||||||||||||||||||
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 | |
|---|---|
| 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 | |
| HSSP | HSSP built from PDB template 1MLW based on UniProtKB P17752. |
| SMR | P17290. Positions 104-393. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 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. |
| ProDom | PD002559. Aaa_hydroxylase. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| 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 |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


