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Database: UniProt
Entry: E0V8E1_MICOH
LinkDB: E0V8E1_MICOH
Original site: E0V8E1_MICOH 
ID   E0V8E1_MICOH            Unreviewed;       445 AA.
AC   E0V8E1;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=D(1A) dopamine receptor {ECO:0000256|ARBA:ARBA00020814};
DE   AltName: Full=Dopamine D1 receptor {ECO:0000256|ARBA:ARBA00032831};
GN   Name=DRD1A {ECO:0000313|EMBL:ADN07539.1};
GN   ORFNames=LTLLF_156565 {ECO:0000313|EMBL:KAH0510087.1};
OS   Microtus ochrogaster (Prairie vole).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Arvicolinae; Microtus.
OX   NCBI_TaxID=79684 {ECO:0000313|EMBL:ADN07539.1};
RN   [1] {ECO:0000313|EMBL:ADN07539.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Benjamin B., Blakesley R.W., Bouffard G.G., Brooks S., Chodroff R., Chu G.,
RA   Chub I., Coleman H., Fuksenko T., Gestole M., Gregory M., Guan X.,
RA   Gupta J., Gurson N., Han J., Hansen N., Hargrove A., Hines-Harris K.,
RA   Ho S.-L., Hu P., Hurle B., Idol J.R., Johnson T., Kwong P., Lee-Lin S.-Q.,
RA   Legaspi R., Lovett S., Madden M., Maduro Q.L., Maduro V.B., Margulies E.H.,
RA   Masiello C., Maskeri B., McDowell J., Montemayor C., Mullikin J.C.,
RA   Myrick J., Palumbo A., Park M., Prasad A., Ramsahoye C., Reddix-Dugue N.,
RA   Riebow N., Schandler K., Schmidt B., Schueler M.G., Sison C., Smith L.,
RA   Stantripop S., Thomas J.W., Thomas P.J., Tsipouri V., Young A., Green E.D.;
RT   "NISC Comparative Sequencing Initiative.";
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAH0510087.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LTLLF {ECO:0000313|EMBL:KAH0510087.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:KAH0510087.1};
RA   Glass D.;
RT   "Studies in the Genomics of Life Span.";
RL   Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Dopamine receptor whose activity is mediated by G proteins
CC       which activate adenylyl cyclase. {ECO:0000256|ARBA:ARBA00002363}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cell
CC       projection, cilium membrane {ECO:0000256|ARBA:ARBA00004272}; Multi-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00004272}. Cell projection,
CC       dendritic spine {ECO:0000256|ARBA:ARBA00004552}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000256|RuleBase:RU000688}.
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DR   EMBL; DP001231; ADN07539.1; -; Genomic_DNA.
DR   EMBL; DP001263; ADO17950.1; -; Genomic_DNA.
DR   EMBL; JAATJU010022611; KAH0510087.1; -; Genomic_DNA.
DR   RefSeq; XP_005355247.1; XM_005355190.2.
DR   RefSeq; XP_013204606.1; XM_013349152.1.
DR   AlphaFoldDB; E0V8E1; -.
DR   Ensembl; ENSMOCT00000022908; ENSMOCP00000019101; ENSMOCG00000017186.
DR   GeneID; 101987419; -.
DR   CTD; 1812; -.
DR   OrthoDB; 2900736at2759; -.
DR   Proteomes; UP000710432; Unassembled WGS sequence.
DR   GO; GO:0060170; C:ciliary membrane; IEA:Ensembl.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0097648; C:G protein-coupled receptor complex; IEA:Ensembl.
DR   GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0097730; C:non-motile cilium; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl.
DR   GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl.
DR   GO; GO:1990763; F:arrestin family protein binding; IEA:Ensembl.
DR   GO; GO:0035240; F:dopamine binding; IEA:Ensembl.
DR   GO; GO:0001588; F:dopamine neurotransmitter receptor activity, coupled via Gs; IEA:Ensembl.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0001965; F:G-protein alpha-subunit binding; IEA:Ensembl.
DR   GO; GO:0032795; F:heterotrimeric G-protein binding; IEA:Ensembl.
DR   GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0007628; P:adult walking behavior; IEA:Ensembl.
DR   GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
DR   GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
DR   GO; GO:0048148; P:behavioral response to cocaine; IEA:Ensembl.
DR   GO; GO:0021853; P:cerebral cortex GABAergic interneuron migration; IEA:Ensembl.
DR   GO; GO:0001661; P:conditioned taste aversion; IEA:Ensembl.
DR   GO; GO:0021542; P:dentate gyrus development; IEA:Ensembl.
DR   GO; GO:0015872; P:dopamine transport; IEA:Ensembl.
DR   GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IEA:Ensembl.
DR   GO; GO:0046323; P:glucose import; IEA:Ensembl.
DR   GO; GO:0007625; P:grooming behavior; IEA:Ensembl.
DR   GO; GO:0046959; P:habituation; IEA:Ensembl.
DR   GO; GO:0060292; P:long-term synaptic depression; IEA:Ensembl.
DR   GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
DR   GO; GO:0042711; P:maternal behavior; IEA:Ensembl.
DR   GO; GO:0007617; P:mating behavior; IEA:Ensembl.
DR   GO; GO:0007613; P:memory; IEA:Ensembl.
DR   GO; GO:0099010; P:modification of postsynaptic structure; IEA:Ensembl.
DR   GO; GO:0019228; P:neuronal action potential; IEA:Ensembl.
DR   GO; GO:0035106; P:operant conditioning; IEA:Ensembl.
DR   GO; GO:0030432; P:peristalsis; IEA:Ensembl.
DR   GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:2001224; P:positive regulation of neuron migration; IEA:Ensembl.
DR   GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
DR   GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
DR   GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IEA:Ensembl.
DR   GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR   GO; GO:0042053; P:regulation of dopamine metabolic process; IEA:Ensembl.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0046960; P:sensitization; IEA:Ensembl.
DR   GO; GO:0021756; P:striatum development; IEA:Ensembl.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IEA:Ensembl.
DR   GO; GO:0001659; P:temperature homeostasis; IEA:Ensembl.
DR   GO; GO:0042311; P:vasodilation; IEA:InterPro.
DR   GO; GO:0008542; P:visual learning; IEA:Ensembl.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR001413; Dopamine_D1_rcpt.
DR   InterPro; IPR000929; Dopamine_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24248; ADRENERGIC RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR24248:SF139; D(1A) DOPAMINE RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00565; DOPAMINED1AR.
DR   PRINTS; PR00242; DOPAMINER.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   G-protein coupled receptor {ECO:0000256|RuleBase:RU000688};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000688};
KW   Reference proteome {ECO:0000313|Proteomes:UP000710432};
KW   Transducer {ECO:0000256|RuleBase:RU000688};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000688};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        23..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        60..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        97..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        139..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          39..331
FT                   /note="G-protein coupled receptors family 1 profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50262"
SQ   SEQUENCE   445 AA;  49353 MW;  2256AAFC68C1197C CRC64;
     MALNTSTMDG AGLAVERDFS FRILTACFLS LLILSTLLGN TLVCAAVIRF RHLRSKVTNF
     FVISLAVSDL LVAVLVMPWK AVAEIAGFWP FGSFCNIWVA FDIMCSTASI LNLCVISVDR
     YWAISSPFQY ERKMTPKAAF ILISVAWTLS VLISFIPVQL SWHKAKPTWP LDDNATFLED
     TEDANCDTRL SRTYAISSSL ISFYIPVAIM IVTYTSIYRI AQKQIRRISA LERAAVHAKN
     CQTTTGNGNP VECSQSESSF KMSFKRETKV LKTLSVIMGV FVCCWLPFFI SNCMVPFCGS
     EETQPFCIDS ITFDVFVWFG WANSSLNPII YAFNADFQKA FSTLLGCYRL CPTTNNAIET
     VSINNNGAVF SSHHEPRGSI SKDCNLVYLI PHAVGSSEDL KKEEAGGIAK PLEKLSPALS
     VILDYDTDVS LEKIQPVTHS GQHPT
//
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