5HT1D_MOUSE
ID 5HT1D_MOUSE Reviewed; 374 AA.
AC Q61224; Q3ZB48; Q61615; Q8BUW7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=5-hydroxytryptamine receptor 1D;
DE Short=5-HT-1D;
DE Short=5-HT1D;
DE AltName: Full=Serotonin receptor 1D;
GN Name=Htr1d; Synonyms=Gpcr14;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NMRI; TISSUE=Brain;
RX PubMed=8978753; DOI=10.1046/j.1471-4159.1997.68010410.x;
RA Wurch T., Palmier C., Colpaert F.C., Pauwels P.J.;
RT "Sequence and functional analysis of cloned guinea pig and rat serotonin 5-
RT HT1D receptors: common pharmacological features within the 5-HT1D receptor
RT subfamily.";
RL J. Neurochem. 68:410-418(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 135-306.
RC TISSUE=Testis;
RX PubMed=8288218; DOI=10.1006/geno.1993.1452;
RA Wilkie T.M., Chen Y., Gilbert D.J., Moore K.J., Yu L., Simon M.I.,
RA Copeland N.G., Jenkins N.A.;
RT "Identification, chromosomal location, and genome organization of mammalian
RT G-protein-coupled receptors.";
RL Genomics 18:175-184(1993).
RN [7]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=22273508; DOI=10.1016/j.mcn.2012.01.003;
RA Enjin A., Leao K.E., Mikulovic S., Le Merre P., Tourtellotte W.G.,
RA Kullander K.;
RT "Sensorimotor function is modulated by the serotonin receptor 1d, a novel
RT marker for gamma motor neurons.";
RL Mol. Cell. Neurosci. 49:322-332(2012).
CC -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine
CC (serotonin). Also functions as a receptor for various alkaloids and
CC psychoactive substances. Ligand binding causes a conformation change
CC that triggers signaling via guanine nucleotide-binding proteins (G
CC proteins) and modulates the activity of down-stream effectors, such as
CC adenylate cyclase. Signaling inhibits adenylate cyclase activity.
CC Regulates the release of 5-hydroxytryptamine in the brain, and thereby
CC affects neural activity. May also play a role in regulating the release
CC of other neurotransmitters. May play a role in vasoconstriction.
CC -!- SUBUNIT: Homodimer. Heterodimer with HTR1B (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Detected in the motor column in spinal cord, and in
CC several cranial motor nuclei, including nucleus ambiguous,
CC oculomotoris, trochelaris and abducens. Detected in gamma motor neurons
CC in the lumbar spinal cord. Detected in proprioceptive sensory neurons
CC in dorsal root ganglia. {ECO:0000269|PubMed:22273508}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Depending on the task,
CC mutant mice show improved motor coordination, especially in avoiding
CC hind limb slips when crossing a narrow beam and in climbing onto a
CC horizontal hanging wire. {ECO:0000269|PubMed:22273508}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X94908; CAA64395.1; -; Genomic_DNA.
DR EMBL; AK082016; BAC38393.1; -; mRNA.
DR EMBL; AL670673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466552; EDL29938.1; -; Genomic_DNA.
DR EMBL; CH466552; EDL29939.1; -; Genomic_DNA.
DR EMBL; BC103532; AAI03533.1; -; mRNA.
DR EMBL; BC103535; AAI03536.1; -; mRNA.
DR EMBL; BC103536; AAI03537.1; -; mRNA.
DR EMBL; L20335; AAA16847.1; -; mRNA.
DR CCDS; CCDS18806.1; -.
DR PIR; F48909; F48909.
DR RefSeq; NP_001272411.1; NM_001285482.1.
DR RefSeq; NP_001272412.1; NM_001285483.1.
DR RefSeq; NP_001272413.1; NM_001285484.1.
DR RefSeq; NP_032335.2; NM_008309.5.
DR RefSeq; XP_006538640.1; XM_006538577.2.
DR RefSeq; XP_006538641.1; XM_006538578.2.
DR RefSeq; XP_017175475.1; XM_017319986.1.
DR AlphaFoldDB; Q61224; -.
DR SMR; Q61224; -.
DR STRING; 10090.ENSMUSP00000086052; -.
DR BindingDB; Q61224; -.
DR ChEMBL; CHEMBL4297; -.
DR GlyGen; Q61224; 3 sites.
DR PhosphoSitePlus; Q61224; -.
DR PaxDb; Q61224; -.
DR PRIDE; Q61224; -.
DR DNASU; 15552; -.
DR Ensembl; ENSMUST00000088677; ENSMUSP00000086052; ENSMUSG00000070687.
DR Ensembl; ENSMUST00000117699; ENSMUSP00000112840; ENSMUSG00000070687.
DR Ensembl; ENSMUST00000121571; ENSMUSP00000112402; ENSMUSG00000070687.
DR GeneID; 15552; -.
DR KEGG; mmu:15552; -.
DR UCSC; uc008vic.3; mouse.
DR CTD; 3352; -.
DR MGI; MGI:96276; Htr1d.
DR VEuPathDB; HostDB:ENSMUSG00000070687; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01010000222287; -.
DR HOGENOM; CLU_009579_11_1_1; -.
DR InParanoid; Q61224; -.
DR OMA; YTAFNEE; -.
DR OrthoDB; 703991at2759; -.
DR PhylomeDB; Q61224; -.
DR TreeFam; TF316350; -.
DR Reactome; R-MMU-390666; Serotonin receptors.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 15552; 4 hits in 75 CRISPR screens.
DR PRO; PR:Q61224; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q61224; protein.
DR Bgee; ENSMUSG00000070687; Expressed in paraventricular nucleus of thalamus and 95 other tissues.
DR Genevisible; Q61224; MM.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IDA:MGI.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0051378; F:serotonin binding; IDA:MGI.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR GO; GO:0014827; P:intestine smooth muscle contraction; ISO:MGI.
DR GO; GO:0050795; P:regulation of behavior; IEA:InterPro.
DR GO; GO:0040012; P:regulation of locomotion; IEA:InterPro.
DR GO; GO:0009636; P:response to toxic substance; IDA:MGI.
DR GO; GO:0042310; P:vasoconstriction; IEA:InterPro.
DR InterPro; IPR000505; 5HT1D_rcpt.
DR InterPro; IPR002231; 5HT_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24247:SF17; PTHR24247:SF17; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00514; 5HT1DRECEPTR.
DR PRINTS; PR01101; 5HTRECEPTOR.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..374
FT /note="5-hydroxytryptamine receptor 1D"
FT /id="PRO_0000068928"
FT TOPO_DOM 1..35
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 36..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 62..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 73..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 96..109
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 110..131
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 132..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 152..173
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 174..191
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 192..214
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 215..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 300..323
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 324..332
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 333..357
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 358..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 132..134
FT /note="DRY motif; important for ligand-induced conformation
FT changes"
FT /evidence="ECO:0000250"
FT MOTIF 349..353
FT /note="NPxxY motif; important for ligand-induced
FT conformation changes and signaling"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 120
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 187
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 17
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 108..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 3
FT /note="P -> L (in Ref. 1; CAA64395)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="V -> A (in Ref. 1; CAA64395, 4; EDL29938/EDL29939
FT and 5; AAI03533/AAI03536/AAI03537)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="I -> A (in Ref. 1; CAA64395)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 374 AA; 41594 MW; 2FE947DF7DBEF14D CRC64;
MSPPNQSLEG LPQEASNRSL NVTGAWDPEV LQALRISLVV VLSVITLATV LSNAFVLTTI
LLTKKLHTPA NYLIGSLATT DLLVSILVMP ISIAYTTTRT WNFGQILCDI WVSSDITCCT
ASILHLCVIA LDRYWAITDA LEYSKRRTAG HAAAMIAAVW IISICISIPP LFWRQATAHE
EMSDCLVNTS QISYTIYSTC GAFYIPSILL IILYGRIYVA ARSRILNPPS LYGKRFTTAQ
LITGSAGSSL CSLNPSLHES HTHTVGSPLF FNQVKIKLAD SILERKRISA ARERKATKTL
GIILGAFIIC WLPFFVVSLV LPICRDSCWI HPALFDFFTW LGYLNSLINP VIYTVFNEDF
RQAFQKVVHF RKIS
