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Protein

Tyramine/octopamine receptor

Gene

Oct-TyrR

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Receptor for both octopamine and tyramine, invertebrate neurotransmitters, and neuromodulators. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. The rank order of potency for agonists is tyramine > octopamine > dopamine > epinephrine > norepinephrine > serotonin > histamine. For antagonists, the rank order is yohimbine > chlorpromazine > phentolamine > mianserine > cyproheptadine > dihydroergotamine > clonidine > synephrine. Tyramine has a functional role in the olfactory system as a neurotransmitter or a neuromodulator.1 Publication

GO - Molecular functioni

GO - Biological processi

  • octopamine or tyramine signaling pathway Source: FlyBase
  • positive regulation of phospholipase C-activating G-protein coupled receptor signaling pathway Source: FlyBase
  • regulation of adenylate cyclase activity involved in G-protein coupled receptor signaling pathway Source: FlyBase
  • sensory perception of smell Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiR-DME-390666. Serotonin receptors.
R-DME-418594. G alpha (i) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyramine/octopamine receptor
Alternative name(s):
Tyr/Oct-Dro
Gene namesi
Name:Oct-TyrR
Synonyms:OcR, OctyR99AB, TYR, TyrR
ORF Names:CG7485
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0004514. Oct-TyrR.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini27 – 11286ExtracellularSequence analysisAdd
BLAST
Transmembranei113 – 13523Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini136 – 14510CytoplasmicSequence analysis
Transmembranei146 – 16722Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini168 – 18417ExtracellularSequence analysisAdd
BLAST
Transmembranei185 – 20521Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini206 – 22520CytoplasmicSequence analysisAdd
BLAST
Transmembranei226 – 24823Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini249 – 27325ExtracellularSequence analysisAdd
BLAST
Transmembranei274 – 29522Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini296 – 530235CytoplasmicSequence analysisAdd
BLAST
Transmembranei531 – 55222Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini553 – 56614ExtracellularSequence analysisAdd
BLAST
Transmembranei567 – 58822Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini589 – 60113CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: FlyBase
  • integral component of plasma membrane Source: FlyBase
  • plasma membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence analysisAdd
BLAST
Chaini27 – 601575Tyramine/octopamine receptorPRO_0000012737Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi11 – 111N-linked (GlcNAc...)Sequence analysis
Glycosylationi57 – 571N-linked (GlcNAc...)Sequence analysis
Disulfide bondi182 ↔ 261PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP22270.
PRIDEiP22270.

Expressioni

Tissue specificityi

Preferentially expressed in Drosophila heads.

Gene expression databases

BgeeiP22270.
ExpressionAtlasiP22270. differential.
GenevisibleiP22270. DM.

Interactioni

Protein-protein interaction databases

STRINGi7227.FBpp0078132.

Structurei

3D structure databases

ProteinModelPortaliP22270.
SMRiP22270. Positions 107-318, 518-598.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
GeneTreeiENSGT00760000118795.
InParanoidiP22270.
OMAiLTSWLCC.
OrthoDBiEOG7NCV3Q.
PhylomeDBiP22270.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR002002. Octopmn_rcpt.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00664. OCTOPAMINER.
SMARTiSM01381. 7TM_GPCR_Srsx. 1 hit.
[Graphical view]
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22270-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSADQILFV NVTTTVAAAA LTAAAAVSTT KSGSGNAARG YTDSDDDAGM
60 70 80 90 100
GTEAVANISG SLVEGLTTVT AALSTAQADK DSAGECEGAV EELHASILGL
110 120 130 140 150
QLAVPEWEAL LTALVLSVII VLTIIGNILV ILSVFTYKPL RIVQNFFIVS
160 170 180 190 200
LAVADLTVAL LVLPFNVAYS ILGRWEFGIH LCKLWLTCDV LCCTSSILNL
210 220 230 240 250
CAIALDRYWA ITDPINYAQK RTVGRVLLLI SGVWLLSLLI SSPPLIGWND
260 270 280 290 300
WPDEFTSATP CELTSQRGYV IYSSLGSFFI PLAIMTIVYI EIFVATRRRL
310 320 330 340 350
RERARANKLN TIALKSTELE PMANSSPVAA SNSGSKSRLL ASWLCCGRDR
360 370 380 390 400
AQFATPMIQN DQESISSETH QPQDSSKAGP HGNSDPQQQH VVVLVKKSRR
410 420 430 440 450
AKTKDSIKHG KTRGGRKSQS SSTCEPHGEQ QLLPAGGDGG SCQPGGGHSG
460 470 480 490 500
GGKSDAEIST ESGSDPKGCI QVCVTQADEQ TSLKLTPPQS STGVAAVSVT
510 520 530 540 550
PLQKKTSGVN QFIEEKQKIS LSKERRAART LGIIMGVFVI CWLPFFLMYV
560 570 580 590 600
ILPFCQTCCP TNKFKNFITW LGYINSGLNP VIYTIFNLDY RRAFKRLLGL

N
Length:601
Mass (Da):64,674
Last modified:December 1, 2000 - v2
Checksum:i7E7581A11674B4C9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341S → N in AAA28731 (PubMed:2156539).Curated
Sequence conflicti34 – 341S → N in BAB71788 (PubMed:10713442).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60789 mRNA. Translation: AAA28731.1.
X54794 mRNA. Translation: CAA38565.1.
AB073914 mRNA. Translation: BAB71788.1.
AE014296 Genomic DNA. Translation: AAF51802.1.
BT025156 mRNA. Translation: ABE73326.1.
PIRiJH0170.
S12004.
RefSeqiNP_001163494.1. NM_001170023.2.
NP_524419.2. NM_079695.4.
UniGeneiDm.3507.

Genome annotation databases

EnsemblMetazoaiFBtr0078479; FBpp0078132; FBgn0004514.
FBtr0301930; FBpp0291142; FBgn0004514.
GeneIDi42452.
KEGGidme:Dmel_CG7485.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60789 mRNA. Translation: AAA28731.1.
X54794 mRNA. Translation: CAA38565.1.
AB073914 mRNA. Translation: BAB71788.1.
AE014296 Genomic DNA. Translation: AAF51802.1.
BT025156 mRNA. Translation: ABE73326.1.
PIRiJH0170.
S12004.
RefSeqiNP_001163494.1. NM_001170023.2.
NP_524419.2. NM_079695.4.
UniGeneiDm.3507.

3D structure databases

ProteinModelPortaliP22270.
SMRiP22270. Positions 107-318, 518-598.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0078132.

Protein family/group databases

GPCRDBiSearch...

Proteomic databases

PaxDbiP22270.
PRIDEiP22270.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0078479; FBpp0078132; FBgn0004514.
FBtr0301930; FBpp0291142; FBgn0004514.
GeneIDi42452.
KEGGidme:Dmel_CG7485.

Organism-specific databases

CTDi42452.
FlyBaseiFBgn0004514. Oct-TyrR.

Phylogenomic databases

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
GeneTreeiENSGT00760000118795.
InParanoidiP22270.
OMAiLTSWLCC.
OrthoDBiEOG7NCV3Q.
PhylomeDBiP22270.

Enzyme and pathway databases

ReactomeiR-DME-390666. Serotonin receptors.
R-DME-418594. G alpha (i) signalling events.

Miscellaneous databases

GenomeRNAii42452.
PROiP22270.

Gene expression databases

BgeeiP22270.
ExpressionAtlasiP22270. differential.
GenevisibleiP22270. DM.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR002002. Octopmn_rcpt.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00664. OCTOPAMINER.
SMARTiSM01381. 7TM_GPCR_Srsx. 1 hit.
[Graphical view]
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, localization, and permanent expression of a Drosophila octopamine receptor."
    Arakawa S., Gocayne J.D., McCombie W.R., Urquhart D.A., Hall L.M., Fraser C.M., Venter J.C.
    Neuron 4:343-354(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Oregon-R.
  2. "Cloning and characterization of a Drosophila tyramine receptor."
    Saudou F., Amlaiky N., Plassat J.-L., Borelli E., Hen R.
    EMBO J. 9:3611-3617(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Oregon-R.
    Tissue: Head.
  3. "A tyramine receptor gene mutation causes a defective olfactory behavior in Drosophila melanogaster."
    Kutsukake M., Komatsu A., Yamamoto D., Chigusa S.I.
    Gene 245:31-42(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  4. "The genome sequence of Drosophila melanogaster."
    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.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  5. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.

Entry informationi

Entry nameiOAR_DROME
AccessioniPrimary (citable) accession number: P22270
Secondary accession number(s): Q1RKQ4, Q95YF4, Q9VNW3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: December 1, 2000
Last modified: June 8, 2016
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.