5HT1E_CAVPO
ID 5HT1E_CAVPO Reviewed; 365 AA.
AC Q6VB83;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=5-hydroxytryptamine receptor 1E;
DE Short=5-HT-1E;
DE Short=5-HT1E;
DE AltName: Full=Serotonin receptor 1E;
GN Name=5HT1E;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Hartley;
RX PubMed=14744596; DOI=10.1016/j.ejphar.2003.11.019;
RA Bai F., Yin T., Johnstone E.M., Su C., Varga G., Little S.P., Nelson D.L.;
RT "Molecular cloning and pharmacological characterization of the guinea pig
RT 5-HT1E receptor.";
RL Eur. J. Pharmacol. 484:127-139(2004).
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 {ECO:0000269|PubMed:14744596}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14744596};
CC Multi-pass membrane protein {ECO:0000269|PubMed:14744596}.
CC -!- TISSUE SPECIFICITY: Detected in the brain with the greatest abundance
CC in the hippocampus, followed by the olfactory bulb. Lower levels are
CC detected in the cortex, thalamus, pons, hypothalamus, midbrain,
CC striatum, and cerebellum. {ECO:0000269|PubMed:14744596}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY344643; AAR05654.1; -; mRNA.
DR RefSeq; NP_001166222.1; NM_001172751.1.
DR AlphaFoldDB; Q6VB83; -.
DR SMR; Q6VB83; -.
DR STRING; 10141.ENSCPOP00000015883; -.
DR GeneID; 100379275; -.
DR KEGG; cpoc:100379275; -.
DR CTD; 3354; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q6VB83; -.
DR OrthoDB; 703991at2759; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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; ISS:UniProtKB.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
DR InterPro; IPR027425; 5HT1E_rcpt.
DR InterPro; IPR002231; 5HT_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24247:SF33; PTHR24247:SF33; 1.
DR Pfam; PF00001; 7tm_1; 1.
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..365
FT /note="5-hydroxytryptamine receptor 1E"
FT /id="PRO_0000307929"
FT TOPO_DOM 1..22
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 23..47
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 48..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 60..82
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 83..96
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 97..118
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 119..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 139..160
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 161..179
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 180..202
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 203..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 292..314
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 315..324
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 325..347
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 348..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 119..121
FT /note="DRY motif; important for ligand-induced conformation
FT changes"
FT /evidence="ECO:0000250"
FT MOTIF 340..344
FT /note="NPxxY motif; important for ligand-induced
FT conformation changes and signaling"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 107
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 175
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 365 AA; 41653 MW; B07177BAF21A74F6 CRC64;
MNITNCTTDA SMVVRPKTVT EKMLICMTLV IITTLTMLLN SAVIMAICTT KKLHQPANYL
ICSLAVTDLL VAVLVMPLSI MYIVMDSWRL GYFICEVWLS VDMTCCTCSI LHLCVIALDR
YWAITNAIEY ARKRTAKRAG LMILTVWTIS IFISMPPLFW RSHRQLSPPP SQCTIQHDHV
IYTIYSTFGA FYIPLTLILI LYYRIYHAAK SLYQKRGSSR HLSNRSTDSQ NSFASCKLTQ
TFCVSDFSTS DPTTEFEKIH ASIRIPPFDN DLDHPGERQQ ISSTRERKAA RILGLILGAF
ILSWLPFFIK ELIVGLSIYT VSSEVGDFLT WLGYVNSLIN PLLYTSFNED FKLAFKKLIR
CREHT
