TBH1_CAEBR
ID TBH1_CAEBR Reviewed; 585 AA.
AC Q61P40; A8X483;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Tyramine beta-hydroxylase;
DE EC=1.14.17.-;
DE Flags: Precursor;
GN Name=tbh-1; ORFNames=CBG07714;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Converts tyramine into octopamine, a neurotransmitter
CC involved in pharyngeal pumping and egg laying. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250};
CC Note=Binds 2 copper ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the copper type II ascorbate-dependent
CC monooxygenase family. {ECO:0000305}.
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DR EMBL; HE601041; CAP27443.1; -; Genomic_DNA.
DR RefSeq; XP_002645947.1; XM_002645901.1.
DR AlphaFoldDB; Q61P40; -.
DR SMR; Q61P40; -.
DR STRING; 6238.CBG07714; -.
DR EnsemblMetazoa; CBG07714.1; CBG07714.1; WBGene00029677.
DR GeneID; 8587946; -.
DR KEGG; cbr:CBG_07714; -.
DR CTD; 8587946; -.
DR WormBase; CBG07714; CBP16058; WBGene00029677; Cbr-tbh-1.
DR eggNOG; KOG3568; Eukaryota.
DR HOGENOM; CLU_017939_3_0_1; -.
DR InParanoid; Q61P40; -.
DR OMA; CAPEMDN; -.
DR OrthoDB; 1472750at2759; -.
DR Proteomes; UP000008549; Chromosome X.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030667; C:secretory granule membrane; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0004500; F:dopamine beta-monooxygenase activity; IBA:GO_Central.
DR GO; GO:0004836; F:tyramine-beta hydroxylase activity; IEA:EnsemblMetazoa.
DR GO; GO:0042420; P:dopamine catabolic process; IBA:GO_Central.
DR GO; GO:0042421; P:norepinephrine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006589; P:octopamine biosynthetic process; IBA:GO_Central.
DR CDD; cd09631; DOMON_DOH; 1.
DR Gene3D; 2.60.120.230; -; 1.
DR Gene3D; 2.60.120.310; -; 1.
DR InterPro; IPR014784; Cu2_ascorb_mOase-like_C.
DR InterPro; IPR020611; Cu2_ascorb_mOase_CS-1.
DR InterPro; IPR000323; Cu2_ascorb_mOase_N.
DR InterPro; IPR036939; Cu2_ascorb_mOase_N_sf.
DR InterPro; IPR024548; Cu2_monoox_C.
DR InterPro; IPR000945; DBH-like.
DR InterPro; IPR045266; DOH_DOMON.
DR InterPro; IPR005018; DOMON_domain.
DR InterPro; IPR008977; PHM/PNGase_F_dom_sf.
DR InterPro; IPR028460; Tbh/DBH.
DR PANTHER; PTHR10157; PTHR10157; 1.
DR Pfam; PF03712; Cu2_monoox_C; 1.
DR Pfam; PF01082; Cu2_monooxygen; 1.
DR PRINTS; PR00767; DBMONOXGNASE.
DR SUPFAM; SSF49742; SSF49742; 2.
DR PROSITE; PS00084; CU2_MONOOXYGENASE_1; 1.
DR PROSITE; PS50836; DOMON; 1.
PE 3: Inferred from homology;
KW Copper; Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Metal-binding;
KW Monooxygenase; Neurotransmitter biosynthesis; Oxidoreductase;
KW Reference proteome; Signal; Synapse.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..585
FT /note="Tyramine beta-hydroxylase"
FT /id="PRO_0000305214"
FT DOMAIN 31..142
FT /note="DOMON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT ACT_SITE 206
FT /evidence="ECO:0000255"
FT ACT_SITE 386
FT /evidence="ECO:0000255"
FT BINDING 240
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 388
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 461
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 208..258
FT /evidence="ECO:0000250"
FT DISULFID 247..270
FT /evidence="ECO:0000250"
FT DISULFID 365..477
FT /evidence="ECO:0000250"
FT DISULFID 369..534
FT /evidence="ECO:0000250"
FT DISULFID 440..462
FT /evidence="ECO:0000250"
SQ SEQUENCE 585 AA; 67137 MW; 710565E4B385F914 CRC64;
MKCANAAALL FFVLCDIGVH GGEIVAELLH SNVTVKWQTD YERQTVDFSI WFGAKTPDLL
FLGFSDFGDM NSSDVLMYDN VKREIMDSYT NRDYKIIPDL SQDFQQLRRR KDHFVVRRKL
TTCDSRDYAF QRGTTQFYIA ASFGYRNLVD IRDKKWILDK KFGKVIEGPT DQPSTDEGVS
SLERDVQLVI VNSNSPDPVP NVETTYECII RKMPFDTVHK TYHIVRMEPY ITPGNEHLVH
HMEVFLCRDE VEEWSGNCND PKKPKKSKSC SHVIAAWAMG EGPIHYPREA GLPIGGKGKN
EYVMVEIHYN NPELHKGVMD TSGFQFYVTG LLRIYDAGIM ELGLIYSDAN SVPPNQKAWA
MNGYCPSQCT QNLPEEGINI FASQMHAHLT GRKLWTSQYR DGVQIGDVNR DEHYSPHWQH
LQQLRPMVRV MPGDTLVTTC VYDTRRRSNV TFGGYGITDE MCVNYIYYYP ASEVEVCKSA
ISNSTLRAYF SQRHGMDGKT MKISDMYNGV KDWSNGVDEE FYNVLNVGNV NMNCLKSNGE
SFEFKSKDPR QGWENMARPR LFSGSFIRTR DRFQCPAIND MINFE
