TBH1_CAEEL
ID TBH1_CAEEL Reviewed; 657 AA.
AC Q9XTQ6; C6KRQ4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUN-2015, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Tyramine beta-hydroxylase {ECO:0000312|WormBase:H13N06.6b};
DE EC=1.14.17.-;
GN Name=tbh-1 {ECO:0000312|WormBase:H13N06.6b};
GN ORFNames=H13N06.6 {ECO:0000312|WormBase:H13N06.6b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15848803; DOI=10.1016/j.neuron.2005.02.024;
RA Alkema M.J., Hunter-Ensor M., Ringstad N., Horvitz H.R.;
RT "Tyramine functions independently of octopamine in the Caenorhabditis
RT elegans nervous system.";
RL Neuron 46:247-260(2005).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-555, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
RN [4]
RP FUNCTION.
RX PubMed=25723162; DOI=10.1016/j.cell.2015.02.004;
RA Burkewitz K., Morantte I., Weir H.J., Yeo R., Zhang Y., Huynh F.K.,
RA Ilkayeva O.R., Hirschey M.D., Grant A.R., Mair W.B.;
RT "Neuronal CRTC-1 governs systemic mitochondrial metabolism and lifespan via
RT a catecholamine signal.";
RL Cell 160:842-855(2015).
CC -!- FUNCTION: Required for the conversion of tyramine to octopamine, a
CC precursor of octapamine but probably itself a neurotransmitter
CC (PubMed:15848803). Involved in the regulation of egg laying, which is
CC inhibited by tyramine (PubMed:15848803). Due to its involvement in
CC octopamine biosynthesis, also required for crtc-1-dependent regulation
CC of AMPK-mediated longevity (PubMed:25723162).
CC {ECO:0000269|PubMed:15848803, ECO:0000269|PubMed:25723162}.
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: [Isoform b]: Membrane {ECO:0000255}; Single-pass
CC membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:H13N06.6b};
CC IsoId=Q9XTQ6-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:H13N06.6a};
CC IsoId=Q9XTQ6-2; Sequence=VSP_057738;
CC -!- TISSUE SPECIFICITY: Present in synaptic regions of RIC interneurons.
CC Present in gonadal sheath cells of hermaphrodites (at protein level).
CC {ECO:0000269|PubMed:15848803}.
CC -!- DISRUPTION PHENOTYPE: Worms are viable and healthy, but have slightly
CC reduced locomotion rates, and defects in the inhibition of pharyngeal
CC pumping and egg laying in the absence of food.
CC {ECO:0000269|PubMed:15848803}.
CC -!- SIMILARITY: Belongs to the copper type II ascorbate-dependent
CC monooxygenase family. {ECO:0000305}.
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DR EMBL; Z99942; CAB17071.2; -; Genomic_DNA.
DR EMBL; BX284606; CAZ65507.1; -; Genomic_DNA.
DR PIR; T23090; T23090.
DR RefSeq; NP_001257264.1; NM_001270335.1. [Q9XTQ6-1]
DR RefSeq; NP_001257265.1; NM_001270336.1. [Q9XTQ6-2]
DR AlphaFoldDB; Q9XTQ6; -.
DR SMR; Q9XTQ6; -.
DR BioGRID; 46533; 2.
DR STRING; 6239.H13N06.6b; -.
DR iPTMnet; Q9XTQ6; -.
DR EPD; Q9XTQ6; -.
DR PaxDb; Q9XTQ6; -.
DR PeptideAtlas; Q9XTQ6; -.
DR EnsemblMetazoa; H13N06.6a.1; H13N06.6a.1; WBGene00006541. [Q9XTQ6-2]
DR EnsemblMetazoa; H13N06.6b.1; H13N06.6b.1; WBGene00006541. [Q9XTQ6-1]
DR GeneID; 181639; -.
DR UCSC; H13N06.6.2; c. elegans. [Q9XTQ6-1]
DR CTD; 181639; -.
DR WormBase; H13N06.6a; CE31553; WBGene00006541; tbh-1. [Q9XTQ6-2]
DR WormBase; H13N06.6b; CE43881; WBGene00006541; tbh-1. [Q9XTQ6-1]
DR eggNOG; KOG3568; Eukaryota.
DR GeneTree; ENSGT00530000063085; -.
DR HOGENOM; CLU_017939_3_0_1; -.
DR InParanoid; Q9XTQ6; -.
DR OMA; CAPEMDN; -.
DR OrthoDB; 1472750at2759; -.
DR PhylomeDB; Q9XTQ6; -.
DR Reactome; R-CEL-209905; Catecholamine biosynthesis.
DR PRO; PR:Q9XTQ6; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006541; Expressed in adult organism and 3 other tissues.
DR ExpressionAtlas; Q9XTQ6; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030667; C:secretory granule membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IDA:WormBase.
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; IMP:WormBase.
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; IMP:WormBase.
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 1: Evidence at protein level;
KW Alternative splicing; Copper; Disulfide bond; Glycoprotein; Membrane;
KW Metal-binding; Monooxygenase; Neurotransmitter biosynthesis;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..657
FT /note="Tyramine beta-hydroxylase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000305215"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 103..214
FT /note="DOMON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT ACT_SITE 278
FT /evidence="ECO:0000255"
FT ACT_SITE 458
FT /evidence="ECO:0000255"
FT BINDING 312
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 380
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 458
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 460
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 533
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT DISULFID 280..330
FT /evidence="ECO:0000250"
FT DISULFID 319..342
FT /evidence="ECO:0000250"
FT DISULFID 437..549
FT /evidence="ECO:0000250"
FT DISULFID 441..606
FT /evidence="ECO:0000250"
FT DISULFID 512..534
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..72
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_057738"
SQ SEQUENCE 657 AA; 74963 MW; 424CFDBFF2BFCE90 CRC64;
MEPTASQGIQ YLRGGVEWIL KLLNLHILNV KHENKPLLFR LIDLKVYIPS SVSTVRWSSG
ASSYVILGEY RKMRSAVALL FLLVAYCGGV VHAGEIVAEL YHTNVTVKWH TDYERQLVDF
SIWFGASTPD VLFLGFSDFG DTNNSDVLMY YNSKKEIKDA YTNRDFKITS DLQQDFQLLR
KRKDHIVVRR KLTTCDSRDY AFLPGTTQFY IAASWGSTNL VDIRDKRWVV DKKFGKVIEG
PTDQPNIEEE PAALEKDVKV VIVNSNSPDP IPNVETTYKC IIRKMPFDTV NNMYHVVRME
PYVTPGNEHL VHHMEIFMCR DEVEEWSGSC NDPKKPPKSK SCSHVIAAWA MGEGPIHYPK
EAGLPIGGKG KNAYVMVEIH YNNPELHKGV IDSSGFQFFV TGQLRKYDAG IMELGLIYSD
ANSVPPNQKA WAMNGYCPSQ CTKNLPEEGI NIFASQLHAH LTGRKLFTSQ YRSGVRIGDV
NRDEHYSPHW QHLQQLRPVV KVMPGDTLVT TCVYDTRKRS KVTFGGYRIV DEMCVNYIYY
YPASDVEVCK SAISNSTLRA YFSERHGMDG KRMQISDMYS NVKDWGNGVD EEFYNVLNVG
NMNMNCLKSN GEPFEFESKD SRQSWENMAR PTFVSGSFIT TRDRFQCPAI NDMINFE
