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Tyramine beta-hydroxylase (EC 1.14.17.-)

 TBH1_DROME              Reviewed;         670 AA.
Q86B61; Q1EC33; Q24549;
02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
22-NOV-2017, entry version 116.
RecName: Full=Tyramine beta-hydroxylase;
EC=1.14.17.-;
Name=Tbh; ORFNames=CG1543;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=Canton-S; TISSUE=Head;
PubMed=8656284;
Monastirioti M., Linn C.E. Jr., White K.;
"Characterization of Drosophila tyramine beta-hydroxylase gene and
isolation of mutant flies lacking octopamine.";
J. Neurosci. 16:3900-3911(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 98-670.
STRAIN=Berkeley;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
FUNCTION.
PubMed=14623230; DOI=10.1016/j.ydbio.2003.07.019;
Monastirioti M.;
"Distinct octopamine cell population residing in the CNS abdominal
ganglion controls ovulation in Drosophila melanogaster.";
Dev. Biol. 264:38-49(2003).
[6]
FUNCTION.
PubMed=14978721; DOI=10.1002/neu.10298;
Saraswati S., Fox L.E., Soll D.R., Wu C.-F.;
"Tyramine and octopamine have opposite effects on the locomotion of
Drosophila larvae.";
J. Neurobiol. 58:425-441(2004).
[7]
FUNCTION.
PubMed=23142736; DOI=10.1016/j.neuropharm.2012.10.013;
Chen J., Wang Y., Zhang Y., Shen P.;
"Mutations in Bacchus reveal a tyramine-dependent nuclear regulator
for acute ethanol sensitivity in Drosophila.";
Neuropharmacology 67:25-31(2013).
-!- FUNCTION: Converts tyramine into octopamine, a neurotransmitter
involved in ovulation and locomotion (PubMed:14623230,
PubMed:14978721, PubMed:8656284). Functions in an amine-mediated
Bacc-dependent signaling pathway that negatively regulates acute
ethanol sensitivity (PubMed:23142736).
{ECO:0000269|PubMed:14623230, ECO:0000269|PubMed:14978721,
ECO:0000269|PubMed:23142736, ECO:0000269|PubMed:8656284}.
-!- COFACTOR:
Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250};
Note=Binds 2 copper ions per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Present in head and in neurons innervating the
oviduct (at protein level). {ECO:0000269|PubMed:8656284}.
-!- DEVELOPMENTAL STAGE: At larval stage, present in cell bodies of
the ventral ganglion and in neuropil (at protein level).
{ECO:0000269|PubMed:8656284}.
-!- DISRUPTION PHENOTYPE: Flies survive to adulthood. Mutant males are
fertile, but mutant females are sterile due to defects in
ovulation. {ECO:0000269|PubMed:8656284}.
-!- SIMILARITY: Belongs to the copper type II ascorbate-dependent
monooxygenase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Z70316; CAA94391.2; -; mRNA.
EMBL; AE014298; AAO41640.1; -; Genomic_DNA.
EMBL; BT025901; ABG02145.1; -; mRNA.
RefSeq; NP_001284996.1; NM_001298067.1.
RefSeq; NP_788884.1; NM_176711.3.
ProteinModelPortal; Q86B61; -.
SMR; Q86B61; -.
BioGrid; 58190; 1.
STRING; 7227.FBpp0089042; -.
PaxDb; Q86B61; -.
PRIDE; Q86B61; -.
EnsemblMetazoa; FBtr0089999; FBpp0089042; FBgn0010329.
EnsemblMetazoa; FBtr0340409; FBpp0309355; FBgn0010329.
GeneID; 31718; -.
KEGG; dme:Dmel_CG1543; -.
CTD; 31718; -.
FlyBase; FBgn0010329; Tbh.
eggNOG; KOG3568; Eukaryota.
eggNOG; ENOG410XR89; LUCA.
InParanoid; Q86B61; -.
KO; K00503; -.
OMA; CDSKMKP; -.
OrthoDB; EOG091G03XS; -.
PhylomeDB; Q86B61; -.
BioCyc; MetaCyc:MONOMER-18080; -.
Reactome; R-DME-209905; Catecholamine biosynthesis.
SignaLink; Q86B61; -.
GenomeRNAi; 31718; -.
PRO; PR:Q86B61; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0010329; -.
ExpressionAtlas; Q86B61; differential.
Genevisible; Q86B61; DM.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0030667; C:secretory granule membrane; IBA:GO_Central.
GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
GO; GO:0004500; F:dopamine beta-monooxygenase activity; IBA:GO_Central.
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.
GO; GO:0002118; P:aggressive behavior; IMP:FlyBase.
GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
GO; GO:0042420; P:dopamine catabolic process; IBA:GO_Central.
GO; GO:0007629; P:flight behavior; IMP:FlyBase.
GO; GO:0002121; P:inter-male aggressive behavior; IMP:FlyBase.
GO; GO:0008345; P:larval locomotory behavior; IMP:FlyBase.
GO; GO:0007612; P:learning; IMP:FlyBase.
GO; GO:0040011; P:locomotion; IMP:UniProtKB.
GO; GO:0008049; P:male courtship behavior; IMP:FlyBase.
GO; GO:0048047; P:mating behavior, sex discrimination; IGI:FlyBase.
GO; GO:0007613; P:memory; IMP:FlyBase.
GO; GO:0042421; P:norepinephrine biosynthetic process; IBA:GO_Central.
GO; GO:0006589; P:octopamine biosynthetic process; TAS:FlyBase.
GO; GO:0071927; P:octopamine signaling pathway; IDA:FlyBase.
GO; GO:0030728; P:ovulation; IMP:FlyBase.
GO; GO:0050795; P:regulation of behavior; IMP:FlyBase.
GO; GO:0043059; P:regulation of forward locomotion; IDA:FlyBase.
Gene3D; 2.130.10.10; -; 1.
Gene3D; 2.60.120.230; -; 1.
Gene3D; 2.60.120.310; -; 1.
InterPro; IPR014784; Cu2_ascorb_mOase-like_C.
InterPro; IPR020611; Cu2_ascorb_mOase_CS-1.
InterPro; IPR000323; Cu2_ascorb_mOase_N.
InterPro; IPR036939; Cu2_ascorb_mOase_N_sf.
InterPro; IPR024548; Cu2_monoox_C.
InterPro; IPR005018; DOMON_domain.
InterPro; IPR008977; PHM/PNGase_F_dom_sf.
InterPro; IPR028460; Tbh/DBH.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
Pfam; PF03712; Cu2_monoox_C; 1.
Pfam; PF01082; Cu2_monooxygen; 1.
Pfam; PF03351; DOMON; 1.
PRINTS; PR00767; DBMONOXGNASE.
SMART; SM00664; DoH; 1.
SUPFAM; SSF49742; SSF49742; 2.
PROSITE; PS00084; CU2_MONOOXYGENASE_1; 1.
PROSITE; PS50836; DOMON; 1.
1: Evidence at protein level;
Complete proteome; Copper; Disulfide bond; Glycoprotein; Membrane;
Metal-binding; Monooxygenase; Neurotransmitter biosynthesis;
Oxidoreductase; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 670 Tyramine beta-hydroxylase.
/FTId=PRO_0000305216.
TRANSMEM 65 81 Helical. {ECO:0000255}.
DOMAIN 104 220 DOMON. {ECO:0000255|PROSITE-
ProRule:PRU00246}.
COMPBIAS 24 34 His-rich.
COMPBIAS 36 61 Gln-rich.
ACT_SITE 281 281 {ECO:0000255}.
ACT_SITE 461 461 {ECO:0000255}.
METAL 312 312 Copper A. {ECO:0000250}.
METAL 313 313 Copper A. {ECO:0000250}.
METAL 382 382 Copper A. {ECO:0000250}.
METAL 461 461 Copper B. {ECO:0000250}.
METAL 463 463 Copper B. {ECO:0000250}.
METAL 536 536 Copper B. {ECO:0000250}.
CARBOHYD 235 235 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 614 614 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 283 334 {ECO:0000250}.
DISULFID 319 344 {ECO:0000250}.
DISULFID 439 552 {ECO:0000250}.
DISULFID 443 613 {ECO:0000250}.
DISULFID 515 537 {ECO:0000250}.
CONFLICT 4 4 I -> M (in Ref. 1; CAA94391).
{ECO:0000305}.
CONFLICT 19 19 F -> S (in Ref. 1; CAA94391).
{ECO:0000305}.
CONFLICT 36 43 Missing (in Ref. 1; CAA94391).
{ECO:0000305}.
CONFLICT 260 260 T -> S (in Ref. 1; CAA94391).
{ECO:0000305}.
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


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