TBH1_DROME
ID TBH1_DROME Reviewed; 670 AA.
AC Q86B61; Q1EC33; Q24549;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Tyramine beta-hydroxylase;
DE EC=1.14.17.-;
GN Name=Tbh; ORFNames=CG1543;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Canton-S; TISSUE=Head;
RX PubMed=8656284; DOI=10.1523/jneurosci.16-12-03900.1996;
RA Monastirioti M., Linn C.E. Jr., White K.;
RT "Characterization of Drosophila tyramine beta-hydroxylase gene and
RT isolation of mutant flies lacking octopamine.";
RL J. Neurosci. 16:3900-3911(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 98-670.
RC STRAIN=Berkeley;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP FUNCTION.
RX PubMed=14623230; DOI=10.1016/j.ydbio.2003.07.019;
RA Monastirioti M.;
RT "Distinct octopamine cell population residing in the CNS abdominal ganglion
RT controls ovulation in Drosophila melanogaster.";
RL Dev. Biol. 264:38-49(2003).
RN [6]
RP FUNCTION.
RX PubMed=14978721; DOI=10.1002/neu.10298;
RA Saraswati S., Fox L.E., Soll D.R., Wu C.-F.;
RT "Tyramine and octopamine have opposite effects on the locomotion of
RT Drosophila larvae.";
RL J. Neurobiol. 58:425-441(2004).
RN [7]
RP FUNCTION.
RX PubMed=23142736; DOI=10.1016/j.neuropharm.2012.10.013;
RA Chen J., Wang Y., Zhang Y., Shen P.;
RT "Mutations in Bacchus reveal a tyramine-dependent nuclear regulator for
RT acute ethanol sensitivity in Drosophila.";
RL Neuropharmacology 67:25-31(2013).
RN [8]
RP INDUCTION.
RX PubMed=25187989; DOI=10.1371/journal.pgen.1004499;
RA Williams M.J., Goergen P., Rajendran J., Zheleznyakova G., Haegglund M.G.,
RA Perland E., Bagchi S., Kalogeropoulou A., Khan Z., Fredriksson R.,
RA Schioeth H.B.;
RT "Obesity-linked homologues TfAP-2 and Twz establish meal frequency in
RT Drosophila melanogaster.";
RL PLoS Genet. 10:e1004499-e1004499(2014).
CC -!- FUNCTION: Converts tyramine into octopamine, a neurotransmitter
CC involved in ovulation and locomotion (PubMed:14623230, PubMed:14978721,
CC PubMed:8656284). Functions in an amine-mediated Bacc-dependent
CC signaling pathway that negatively regulates acute ethanol sensitivity
CC (PubMed:23142736). {ECO:0000269|PubMed:14623230,
CC ECO:0000269|PubMed:14978721, ECO:0000269|PubMed:23142736,
CC ECO:0000269|PubMed:8656284}.
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: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Present in head and in neurons innervating the
CC oviduct (at protein level). {ECO:0000269|PubMed:8656284}.
CC -!- DEVELOPMENTAL STAGE: At larval stage, present in cell bodies of the
CC ventral ganglion and in neuropil (at protein level).
CC {ECO:0000269|PubMed:8656284}.
CC -!- INDUCTION: Slightly down-regulated in adults fed a high calorie diet.
CC {ECO:0000269|PubMed:25187989}.
CC -!- DISRUPTION PHENOTYPE: Flies survive to adulthood. Mutant males are
CC fertile, but mutant females are sterile due to defects in ovulation.
CC {ECO:0000269|PubMed:8656284}.
CC -!- SIMILARITY: Belongs to the copper type II ascorbate-dependent
CC monooxygenase family. {ECO:0000305}.
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DR EMBL; Z70316; CAA94391.2; -; mRNA.
DR EMBL; AE014298; AAO41640.1; -; Genomic_DNA.
DR EMBL; BT025901; ABG02145.1; -; mRNA.
DR RefSeq; NP_001284996.1; NM_001298067.1.
DR RefSeq; NP_788884.1; NM_176711.3.
DR AlphaFoldDB; Q86B61; -.
DR SMR; Q86B61; -.
DR BioGRID; 58190; 2.
DR STRING; 7227.FBpp0089042; -.
DR GlyGen; Q86B61; 2 sites.
DR PaxDb; Q86B61; -.
DR PRIDE; Q86B61; -.
DR EnsemblMetazoa; FBtr0089999; FBpp0089042; FBgn0010329.
DR EnsemblMetazoa; FBtr0340409; FBpp0309355; FBgn0010329.
DR GeneID; 31718; -.
DR KEGG; dme:Dmel_CG1543; -.
DR CTD; 31718; -.
DR FlyBase; FBgn0010329; Tbh.
DR VEuPathDB; VectorBase:FBgn0010329; -.
DR eggNOG; KOG3568; Eukaryota.
DR HOGENOM; CLU_017939_3_0_1; -.
DR InParanoid; Q86B61; -.
DR OMA; CAPEMDN; -.
DR OrthoDB; 1472750at2759; -.
DR PhylomeDB; Q86B61; -.
DR BioCyc; MetaCyc:MON-18080; -.
DR Reactome; R-DME-209905; Catecholamine biosynthesis.
DR BioGRID-ORCS; 31718; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 31718; -.
DR PRO; PR:Q86B61; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0010329; Expressed in brain and 4 other tissues.
DR ExpressionAtlas; Q86B61; baseline and differential.
DR Genevisible; Q86B61; DM.
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:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0004500; F:dopamine beta-monooxygenase activity; IBA:GO_Central.
DR GO; GO:0016715; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen; IMP:UniProtKB.
DR GO; GO:0002118; P:aggressive behavior; IMP:FlyBase.
DR GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
DR GO; GO:0042420; P:dopamine catabolic process; IBA:GO_Central.
DR GO; GO:0007629; P:flight behavior; IMP:FlyBase.
DR GO; GO:0002121; P:inter-male aggressive behavior; IMP:FlyBase.
DR GO; GO:0008345; P:larval locomotory behavior; IMP:FlyBase.
DR GO; GO:0007612; P:learning; IMP:FlyBase.
DR GO; GO:0040011; P:locomotion; IMP:UniProtKB.
DR GO; GO:0008049; P:male courtship behavior; IMP:FlyBase.
DR GO; GO:0048047; P:mating behavior, sex discrimination; IGI:FlyBase.
DR GO; GO:0007613; P:memory; IMP:FlyBase.
DR GO; GO:0042421; P:norepinephrine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006589; P:octopamine biosynthetic process; IBA:GO_Central.
DR GO; GO:0071927; P:octopamine signaling pathway; IDA:FlyBase.
DR GO; GO:0030728; P:ovulation; IMP:FlyBase.
DR GO; GO:0050795; P:regulation of behavior; IMP:FlyBase.
DR GO; GO:0043059; P:regulation of forward locomotion; IDA:FlyBase.
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 SMART; SM00664; DoH; 1.
DR SUPFAM; SSF49742; SSF49742; 2.
DR PROSITE; PS00084; CU2_MONOOXYGENASE_1; 1.
DR PROSITE; PS50836; DOMON; 1.
PE 1: Evidence at protein level;
KW Copper; Disulfide bond; Glycoprotein; Membrane; Metal-binding;
KW Monooxygenase; Neurotransmitter biosynthesis; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..670
FT /note="Tyramine beta-hydroxylase"
FT /id="PRO_0000305216"
FT TRANSMEM 65..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 104..220
FT /note="DOMON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT REGION 26..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 281
FT /evidence="ECO:0000255"
FT ACT_SITE 461
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 382
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
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 BINDING 463
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 536
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 283..334
FT /evidence="ECO:0000250"
FT DISULFID 319..344
FT /evidence="ECO:0000250"
FT DISULFID 439..552
FT /evidence="ECO:0000250"
FT DISULFID 443..613
FT /evidence="ECO:0000250"
FT DISULFID 515..537
FT /evidence="ECO:0000250"
FT CONFLICT 4
FT /note="I -> M (in Ref. 1; CAA94391)"
FT /evidence="ECO:0000305"
FT CONFLICT 19
FT /note="F -> S (in Ref. 1; CAA94391)"
FT /evidence="ECO:0000305"
FT CONFLICT 36..43
FT /note="Missing (in Ref. 1; CAA94391)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="T -> S (in Ref. 1; CAA94391)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 670 AA; 77729 MW; 5D5D68561E9E1DFA CRC64;
MLKIPLQLSS QDGIWPARFA RRLHHHHQLA YHHHKQEQQQ QQQQQQQQQA KQKQKQNGVQ
QGRSPTFMPV MLLLLMATLL TRPLSAFSNR LSDTKLHEIY LDDKEIKLSW MVDWYKQEVL
FHLQNAFNEQ HRWFYLGFSK RGGLADADIC FFENQNGFFN AVTDTYTSPD GQWVRRDYQQ
DCEVFKMDEF TLAFRRKFDT CDPLDLRLHE GTMYVVWARG ETELALEDHQ FALPNVTAPH
EAGVKMLQLL RADKILIPET ELDHMEITLQ EAPIPSQETT YWCHVQRLEG NLRRRHHIVQ
FEPLIRTPGI VHHMEVFHCE AGEHEEIPLY NGDCEQLPPR AKICSKVMVL WAMGAGTFTY
PPEAGLPIGG PGFNPYVRLE VHFNNPEKQS GLVDNSGFRI KMSKTLRQYD AAVMELGLEY
TDKMAIPPGQ TAFPLSGYCV ADCTRAALPA TGIIIFGSQL HTHLRGVRVL TRHFRGEQEL
REVNRDDYYS NHFQEMRTLH YKPRVLPGDA LVTTCYYNTK DDKTAALGGF SISDEMCVNY
IHYYPATKLE VCKSSVSEET LENYFIYMKR TEHQHGVHLN GARSSNYRSI EWTQPRIDQL
YTMYMQEPLS MQCNRSDGTR FEGRSSWEGV AATPVQIRIP IHRKLCPNYN PLWLKPLEKG
DCDLLGECIY
