Q9XTQ6 · TBH1_CAEEL
- ProteinTyramine beta-hydroxylase
- Genetbh-1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids657 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for the conversion of tyramine to octopamine, a precursor of octapamine but probably itself a neurotransmitter (PubMed:15848803).
Involved in the regulation of egg laying, which is inhibited by tyramine (PubMed:15848803).
Due to its involvement in octopamine biosynthesis, also required for crtc-1-dependent regulation of AMPK-mediated longevity (PubMed:25723162).
Involved in the regulation of egg laying, which is inhibited by tyramine (PubMed:15848803).
Due to its involvement in octopamine biosynthesis, also required for crtc-1-dependent regulation of AMPK-mediated longevity (PubMed:25723162).
Catalytic activity
- L-ascorbate + O2 + tyramine = (R)-octopamine + H2O + L-dehydroascorbateThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 2 copper ions per subunit.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 278 | |||||
Sequence: Y | ||||||
Binding site | 312 | Cu2+ A (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 313 | Cu2+ A (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 380 | Cu2+ A (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 458 | |||||
Sequence: H | ||||||
Binding site | 458 | Cu2+ B (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 460 | Cu2+ B (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 533 | Cu2+ B (UniProtKB | ChEBI) | ||||
Sequence: M |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular space | |
Cellular Component | secretory granule membrane | |
Cellular Component | synapse | |
Molecular Function | copper ion binding | |
Molecular Function | dopamine beta-monooxygenase activity | |
Molecular Function | tyramine-beta hydroxylase activity | |
Biological Process | dopamine catabolic process | |
Biological Process | norepinephrine biosynthetic process | |
Biological Process | octopamine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTyramine beta-hydroxylase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionQ9XTQ6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Isoform b
Membrane ; Single-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 77-97 | Helical | ||||
Sequence: VALLFLLVAYCGGVVHAGEIV |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Worms are viable and healthy, but have slightly reduced locomotion rates, and defects in the inhibition of pharyngeal pumping and egg laying in the absence of food.
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000305215 | 1-657 | Tyramine beta-hydroxylase | |||
Sequence: MEPTASQGIQYLRGGVEWILKLLNLHILNVKHENKPLLFRLIDLKVYIPSSVSTVRWSSGASSYVILGEYRKMRSAVALLFLLVAYCGGVVHAGEIVAELYHTNVTVKWHTDYERQLVDFSIWFGASTPDVLFLGFSDFGDTNNSDVLMYYNSKKEIKDAYTNRDFKITSDLQQDFQLLRKRKDHIVVRRKLTTCDSRDYAFLPGTTQFYIAASWGSTNLVDIRDKRWVVDKKFGKVIEGPTDQPNIEEEPAALEKDVKVVIVNSNSPDPIPNVETTYKCIIRKMPFDTVNNMYHVVRMEPYVTPGNEHLVHHMEIFMCRDEVEEWSGSCNDPKKPPKSKSCSHVIAAWAMGEGPIHYPKEAGLPIGGKGKNAYVMVEIHYNNPELHKGVIDSSGFQFFVTGQLRKYDAGIMELGLIYSDANSVPPNQKAWAMNGYCPSQCTKNLPEEGINIFASQLHAHLTGRKLFTSQYRSGVRIGDVNRDEHYSPHWQHLQQLRPVVKVMPGDTLVTTCVYDTRKRSKVTFGGYRIVDEMCVNYIYYYPASDVEVCKSAISNSTLRAYFSERHGMDGKRMQISDMYSNVKDWGNGVDEEFYNVLNVGNMNMNCLKSNGEPFEFESKDSRQSWENMARPTFVSGSFITTRDRFQCPAINDMINFE | ||||||
Glycosylation | 104 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 143 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 280↔330 | |||||
Sequence: CIIRKMPFDTVNNMYHVVRMEPYVTPGNEHLVHHMEIFMCRDEVEEWSGSC | ||||||
Disulfide bond | 319↔342 | |||||
Sequence: CRDEVEEWSGSCNDPKKPPKSKSC | ||||||
Disulfide bond | 437↔549 | |||||
Sequence: CPSQCTKNLPEEGINIFASQLHAHLTGRKLFTSQYRSGVRIGDVNRDEHYSPHWQHLQQLRPVVKVMPGDTLVTTCVYDTRKRSKVTFGGYRIVDEMCVNYIYYYPASDVEVC | ||||||
Disulfide bond | 441↔606 | |||||
Sequence: CTKNLPEEGINIFASQLHAHLTGRKLFTSQYRSGVRIGDVNRDEHYSPHWQHLQQLRPVVKVMPGDTLVTTCVYDTRKRSKVTFGGYRIVDEMCVNYIYYYPASDVEVCKSAISNSTLRAYFSERHGMDGKRMQISDMYSNVKDWGNGVDEEFYNVLNVGNMNMNC | ||||||
Disulfide bond | 512↔534 | |||||
Sequence: CVYDTRKRSKVTFGGYRIVDEMC | ||||||
Glycosylation | 555 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Present in synaptic regions of RIC interneurons. Present in gonadal sheath cells of hermaphrodites (at protein level).
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 103-214 | DOMON | ||||
Sequence: TNVTVKWHTDYERQLVDFSIWFGASTPDVLFLGFSDFGDTNNSDVLMYYNSKKEIKDAYTNRDFKITSDLQQDFQLLRKRKDHIVVRRKLTTCDSRDYAFLPGTTQFYIAAS |
Sequence similarities
Belongs to the copper type II ascorbate-dependent monooxygenase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9XTQ6-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Nameb
- Length657
- Mass (Da)74,963
- Last updated2015-06-24 v3
- Checksum424CFDBFF2BFCE90
Q9XTQ6-2
- Namea
- Differences from canonical
- 1-72: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0K3ATC0 | A0A0K3ATC0_CAEEL | tbh-1 | 606 |
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_057738 | 1-72 | in isoform a | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z99942 EMBL· GenBank· DDBJ | CAB17071.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
BX284606 EMBL· GenBank· DDBJ | CAZ65507.1 EMBL· GenBank· DDBJ | Genomic DNA |