DOPR3_CAEEL
ID DOPR3_CAEEL Reviewed; 607 AA.
AC Q6RYS9; Q3HKC0; Q3HKC1; Q3HKC2;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Dopamine receptor 3 {ECO:0000312|WormBase:T14E8.3b};
DE AltName: Full=Dopamine D2-like receptor dop-3 {ECO:0000305};
GN Name=dop-3 {ECO:0000312|WormBase:T14E8.3b};
GN ORFNames=T14E8.3 {ECO:0000312|WormBase:T14E8.3b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAR37416.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15378064; DOI=10.1038/nn1316;
RA Chase D.L., Pepper J.S., Koelle M.R.;
RT "Mechanism of extrasynaptic dopamine signaling in Caenorhabditis elegans.";
RL Nat. Neurosci. 7:1096-1103(2004).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS C AND D), FUNCTION, AND MUTAGENESIS OF
RP ASP-102 AND SER-184.
RX PubMed=16001968; DOI=10.1111/j.1471-4159.2005.03268.x;
RA Sugiura M., Fuke S., Suo S., Sasagawa N., Van Tol H.H.M., Ishiura S.;
RT "Characterization of a novel D2-like dopamine receptor with a truncated
RT splice variant and a D1-like dopamine receptor unique to invertebrates from
RT Caenorhabditis elegans.";
RL J. Neurochem. 94:1146-1157(2005).
RN [3]
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 [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19609300; DOI=10.1038/emboj.2009.194;
RA Suo S., Culotti J.G., Van Tol H.H.;
RT "Dopamine counteracts octopamine signalling in a neural circuit mediating
RT food response in C. elegans.";
RL EMBO J. 28:2437-2448(2009).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23166505; DOI=10.1371/journal.pgen.1003015;
RA Correa P., LeBoeuf B., Garcia L.R.;
RT "C. elegans dopaminergic D2-like receptors delimit recurrent cholinergic-
RT mediated motor programs during a goal-oriented behavior.";
RL PLoS Genet. 8:E1003015-E1003015(2012).
RN [6]
RP FUNCTION.
RX PubMed=25536037; DOI=10.1371/journal.pone.0115985;
RA Wang D., Yu Y., Li Y., Wang Y., Wang D.;
RT "Dopamine receptors antagonistically regulate behavioral choice between
RT conflicting alternatives in C. elegans.";
RL PLoS ONE 9:E115985-E115985(2014).
CC -!- FUNCTION: G-protein coupled receptor which binds to the
CC neurotransmitter dopamine with high affinity leading to the activation
CC of an associated G-protein and downstream signaling pathways
CC (PubMed:15378064, PubMed:16001968). Couples to G-proteins to inhibit
CC adenylate cyclase (AC) activity and cAMP production (PubMed:15378064,
CC PubMed:16001968). Antagonizes the D1-like dopamine receptor dop-1 to
CC negatively regulate the rate of locomotion (PubMed:15378064). In
CC GABAergic, RIC, and SIA neurons, antagonizes the function of dop-1 to
CC play a role in behavioral plasticity and regulate the decision-making
CC process when conflicting alternatives are present (PubMed:25536037).
CC Antagonizes octopamine signaling in response to food by promoting the
CC dopamine-mediated suppression of crh-1/CREB1 transcription factor
CC activation in cholinergic SIA neurons (PubMed:19609300). This is most
CC likely in association with the G(o)-alpha G-protein subunit goa-1
CC (PubMed:19609300). Promotes male mating behavior by antagonizing
CC acetylcholine signaling to control the protrusion of copulatory
CC spicules from the tail of males during hermaphrodite vulval location
CC (PubMed:23166505). {ECO:0000269|PubMed:15378064,
CC ECO:0000269|PubMed:16001968, ECO:0000269|PubMed:19609300,
CC ECO:0000269|PubMed:23166505, ECO:0000269|PubMed:25536037}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=b {ECO:0000312|WormBase:T14E8.3b};
CC IsoId=Q6RYS9-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:T14E8.3a};
CC IsoId=Q6RYS9-2; Sequence=VSP_052258;
CC Name=c {ECO:0000312|WormBase:T14E8.3c};
CC IsoId=Q6RYS9-3; Sequence=VSP_052257, VSP_052258;
CC Name=d {ECO:0000312|WormBase:T14E8.3d}; Synonyms=DOP-3nf
CC {ECO:0000303|PubMed:16001968};
CC IsoId=Q6RYS9-4; Sequence=VSP_052257, VSP_052259, VSP_052260;
CC -!- TISSUE SPECIFICITY: Expressed in the neurons of the head, ventral cord
CC and tail with weak expression observed in body wall muscles and PVD
CC neurons (PubMed:15378064). In the ventral cord, expressed strongly in
CC GABAergic neurons with weaker expression in cholinergic motor neurons
CC (PubMed:15378064). Expressed in cholinergic SIA neurons and
CC octopaminergic RIC neurons (PubMed:19609300). In males, expressed in
CC the dorsal and ventral spicule protractor and retractor muscles, and
CC the sensory post-cloacal sensilla B (PCB) neuron (PubMed:23166505).
CC {ECO:0000269|PubMed:15378064, ECO:0000269|PubMed:19609300,
CC ECO:0000269|PubMed:23166505}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY485309; AAR37416.1; -; mRNA.
DR EMBL; BX284606; CCD83404.1; -; Genomic_DNA.
DR EMBL; BX284606; CCD83405.1; -; Genomic_DNA.
DR EMBL; BX284606; CCD83406.1; -; Genomic_DNA.
DR EMBL; BX284606; CCD83407.1; -; Genomic_DNA.
DR RefSeq; NP_001024907.2; NM_001029736.4. [Q6RYS9-2]
DR RefSeq; NP_001024908.2; NM_001029737.2. [Q6RYS9-1]
DR RefSeq; NP_001033560.1; NM_001038471.3.
DR RefSeq; NP_001033561.1; NM_001038472.3. [Q6RYS9-4]
DR AlphaFoldDB; Q6RYS9; -.
DR SMR; Q6RYS9; -.
DR STRING; 6239.T14E8.3b; -.
DR PaxDb; Q6RYS9; -.
DR PRIDE; Q6RYS9; -.
DR EnsemblMetazoa; T14E8.3a.1; T14E8.3a.1; WBGene00020506. [Q6RYS9-2]
DR EnsemblMetazoa; T14E8.3b.1; T14E8.3b.1; WBGene00020506. [Q6RYS9-1]
DR EnsemblMetazoa; T14E8.3c.1; T14E8.3c.1; WBGene00020506. [Q6RYS9-3]
DR EnsemblMetazoa; T14E8.3d.1; T14E8.3d.1; WBGene00020506. [Q6RYS9-4]
DR GeneID; 188499; -.
DR KEGG; cel:CELE_T14E8.3; -.
DR UCSC; T14E8.3a; c. elegans. [Q6RYS9-1]
DR CTD; 188499; -.
DR WormBase; T14E8.3a; CE39178; WBGene00020506; dop-3. [Q6RYS9-2]
DR WormBase; T14E8.3b; CE39179; WBGene00020506; dop-3. [Q6RYS9-1]
DR WormBase; T14E8.3c; CE39180; WBGene00020506; dop-3. [Q6RYS9-3]
DR WormBase; T14E8.3d; CE39181; WBGene00020506; dop-3. [Q6RYS9-4]
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000164988; -.
DR InParanoid; Q6RYS9; -.
DR OMA; APMDPLN; -.
DR OrthoDB; 1215361at2759; -.
DR PhylomeDB; Q6RYS9; -.
DR Reactome; R-CEL-390651; Dopamine receptors.
DR Reactome; R-CEL-418594; G alpha (i) signalling events.
DR PRO; PR:Q6RYS9; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00020506; Expressed in larva and 2 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IC:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IC:WormBase.
DR GO; GO:0004952; F:dopamine neurotransmitter receptor activity; IDA:WormBase.
DR GO; GO:0001591; F:dopamine neurotransmitter receptor activity, coupled via Gi/Go; IDA:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007195; P:adenylate cyclase-inhibiting dopamine receptor signaling pathway; IDA:WormBase.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; IMP:WormBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; IMP:WormBase.
DR GO; GO:1902437; P:positive regulation of male mating behavior; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0040012; P:regulation of locomotion; IDA:UniProtKB.
DR GO; GO:0032094; P:response to food; IMP:WormBase.
DR GO; GO:1990834; P:response to odorant; IMP:WormBase.
DR GO; GO:0034609; P:spicule insertion; IMP:UniProtKB.
DR GO; GO:0034608; P:vulval location; IMP:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Membrane; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..607
FT /note="Dopamine receptor 3"
FT /id="PRO_0000270582"
FT TOPO_DOM 1..23
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..96
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..182
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..544
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 545..558
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 559..579
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 580..607
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 402..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 95..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 1..15
FT /note="Missing (in isoform c and isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_052257"
FT VAR_SEQ 170..171
FT /note="Missing (in isoform a and isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_052258"
FT VAR_SEQ 260
FT /note="T -> V (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_052259"
FT VAR_SEQ 261..607
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_052260"
FT MUTAGEN 102
FT /note="D->N: Decreased inhibition of forskolin-stimulated
FT cAMP formation in response to dopamine but not in response
FT to 5-HT."
FT /evidence="ECO:0000269|PubMed:16001968"
FT MUTAGEN 184
FT /note="S->A: Decreased inhibition of forskolin-stimulated
FT cAMP formation in response to dopamine but not in response
FT to 5-HT."
FT /evidence="ECO:0000269|PubMed:16001968"
SQ SEQUENCE 607 AA; 68421 MW; 03F122D10D3FE58A CRC64;
MLAGQHHVTD IESPLMVVLW RVAAGVFLPL VPTMAVFGNV LVIMSVFRER SLQTVTNMLI
VSLAVSDFMV AIGVMSFGVY YEWNDFKWGL GSFFCHVYQA LDVACSTASI LNLLAISLDR
YIAIGHPISY AQYGARGGRA MISITIVWGV SVAVALPLLL GVNPMEENDL QECELANPYF
NMISSIFSFF IPCIAMIILY TIIFRRLRQR ERARSLRQAQ RSENDKISSA LLGGAQIARQ
MGKHFKNRTD QILLEISFQT SSFPTMSESS EDASTISPMI NSFNNFLPKK TPYPSTSIPA
IPECGSMPNL TIIERPEAEK EKEISIMDLR DTVEMLDDKY SSAILTSFQT SRSFGEELEE
ILPFIDGSNS VKHSREQLHT TRSNTSTTRL LDVKPELRSI SVPSIQDEKK LSQKSNDLPF
SHQNGTHKQK LLPNPGILMK SKSTTLLKTN GYMDTDSLNR NSHKKSLADL LANDEFSFSD
SMRVYKNRLF KSLSRATSGW NKPRPSRHMV KKATKQMRRE HKATVTLAVV LAVFLFCWLP
FFVLHLSNSI CLIIDENSAC VGFLPLYLAT WLGYLNSSLN PLIYTVFDQR FRNAFRNILS
CGIFKKR
