DOPR4_CAEEL
ID DOPR4_CAEEL Reviewed; 517 AA.
AC Q18775;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Dopamine receptor 4;
GN Name=dop-4; ORFNames=C52B11.3;
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 [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
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 [2]
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).
CC -!- FUNCTION: Receptor for dopamine. The activity of this receptor is
CC mediated by G proteins which activate adenylyl cyclase. In terms of
CC antagonist responses, would be classed with the D1-like dopamine
CC receptor group. {ECO:0000269|PubMed:16001968}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in pharyngeal neurons I1 and I2, neurons
CC ASG, AVL, CAN, PQR, vulva, intestine, rectal glands and rectal
CC epithelial glands. Also expressed in neurons in ray 8 in males.
CC {ECO:0000269|PubMed:16001968}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; FO080675; CCD65696.1; -; Genomic_DNA.
DR PIR; T15819; T15819.
DR RefSeq; NP_508238.2; NM_075837.2.
DR AlphaFoldDB; Q18775; -.
DR STRING; 6239.C52B11.3; -.
DR PaxDb; Q18775; -.
DR EnsemblMetazoa; C52B11.3.1; C52B11.3.1; WBGene00016872.
DR GeneID; 183715; -.
DR KEGG; cel:CELE_C52B11.3; -.
DR UCSC; C52B11.3; c. elegans.
DR CTD; 183715; -.
DR WormBase; C52B11.3; CE39139; WBGene00016872; dop-4.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000154484; -.
DR HOGENOM; CLU_009579_11_1_1; -.
DR InParanoid; Q18775; -.
DR OMA; YVHEQRA; -.
DR OrthoDB; 1095345at2759; -.
DR PhylomeDB; Q18775; -.
DR Reactome; R-CEL-390666; Serotonin receptors.
DR Reactome; R-CEL-418594; G alpha (i) signalling events.
DR PRO; PR:Q18775; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00016872; Expressed in embryo and 2 other tissues.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IC:WormBase.
DR GO; GO:0004952; F:dopamine neurotransmitter receptor activity; IDA:WormBase.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IBA:GO_Central.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0004989; F:octopamine receptor activity; IBA:GO_Central.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IDA:WormBase.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:UniProtKB.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
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; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..517
FT /note="Dopamine receptor 4"
FT /id="PRO_0000070238"
FT TOPO_DOM 1..46
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..108
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..209
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..442
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..517
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 309..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 517 AA; 58647 MW; 6C6E73F158BE807A CRC64;
MLAYGSDPNA EDLYITMTPS VSTENDTTVW ATEEPAAIVW RHPLLAIALF SICLLTVAGN
CLVVIAVCTK KYLRNPTGYL IISLAIADLI VGVIVMPMNS LFEIANHTWL FGLMMCDVFH
AMDILASTAS IWNLCVISLD RYMAGQDPIG YRDKVSKRRI LMAILSVWVL SAILSFPGII
WWRTSSPHLY EDQSQCLFTD SKMYVSFSSL VSFYIPLFLI LFAYGKVYII ATRHSKGMRM
GIKTVSIKKR NGKKSNTETE SILSSENEPT LRIHFGRGKQ SSSSLRNSRF HARESTRLLL
KQVSCKSLND RGEHNNNNTV RQPLLRGTEG CHSDSISRSS QRNFRGRNVT IGSNCSSTLL
QVDQPDRMSL SSNSQMVMTS PLSTRRKLNV REKSRQMMRY VHEQRAARTL SIVVGAFILC
WTPFFVFTPL TAFCESCFSN KETIFTFVTW AGHLNSMLNP LIYSRFSRDF RRAFKQILTC
QRQQKVKTAF KTPLSLVFTQ LISVTQMWEQ PPNTSIE