5HT1E_PANTR
ID 5HT1E_PANTR Reviewed; 363 AA.
AC Q9N2B6;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=5-hydroxytryptamine receptor 1E;
DE Short=5-HT-1E;
DE Short=5-HT1E;
DE AltName: Full=Serotonin receptor 1E;
DE Flags: Fragment;
GN Name=HTR1E;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate 220;
RX PubMed=15014171; DOI=10.1093/molbev/msh100;
RA Kitano T., Liu Y.-H., Ueda S., Saitou N.;
RT "Human-specific amino acid changes found in 103 protein-coding genes.";
RL Mol. Biol. Evol. 21:936-944(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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AB041374; BAA94459.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9N2B6; -.
DR SMR; Q9N2B6; -.
DR STRING; 9598.ENSPTRP00000056988; -.
DR PaxDb; Q9N2B6; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q9N2B6; -.
DR Proteomes; UP000002277; Unplaced.
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; ISS:UniProtKB.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0051378; F:serotonin binding; IBA:GO_Central.
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 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 3: Inferred from homology;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..>363
FT /note="5-hydroxytryptamine receptor 1E"
FT /id="PRO_0000068934"
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..159
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 160..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..>363
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"
FT NON_TER 363
SQ SEQUENCE 363 AA; 41444 MW; 7D783A3F74832C8E CRC64;
MNITNCTTEA SMAIRPKTIT EKMLICMTLV VITTLTTLLN LAVIMAIGTT KKLHQPANYL
ICSLAVTDLL VAVLVMPLSI IYIVMDRWKL GYFLCEVWLS VDMTCCTCSI LHLCVIALDR
YWAITNAIEY ARKRTAKRAA LMILTVWTIS IFISMPPLFW RSHRRLSPPP SQCTIQHDHV
IYTIYSTLGA FYIPLTLILI LYYRIYHAAK SLYQKRGSSR HLSNRSTDSQ NSFASCKLTQ
TFCVSDFSTS DPTTEFEKFH ASIRIPPFDN DLDHPGERQQ ISSTRERKAA RILGLILGAF
ILSWLPFFIK ELIVGLSIYT VSSEVADFLT WLGYVNSLIN PLLYTSFNED FKLAFKKLIR
CRE
