5HT4R_CAVPO
ID 5HT4R_CAVPO Reviewed; 388 AA.
AC O70528;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=5-hydroxytryptamine receptor 4;
DE Short=5-HT-4;
DE Short=5-HT4;
DE AltName: Full=Serotonin receptor 4;
GN Name=HTR4;
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].
RA Van den Wyngaert I., Gommeren W., Jurzak M., Verhasselt P., Gordon R.,
RA Leysen J., Luyten W., Bender E.;
RT "Cloning and expression of 5-HT4 receptor species and splice variants.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This is one of the several different receptors for 5-
CC hydroxytryptamine (serotonin), a biogenic hormone that functions as a
CC neurotransmitter, a hormone, and a mitogen. The activity of this
CC receptor is mediated by G proteins that stimulate adenylate cyclase (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: May interact with PATJ, MAGI2, MPP3, NOS1, SLC9A3R1, SEC23A
CC and SNX27. May form a complex including SLC9A3R1 and EZR (By
CC similarity). Interacts (via C-terminus 330-346 AA) with GRK5; this
CC interaction is promoted by 5-HT (serotonin) (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Endosome. Note=Interaction with SNX27 mediates recruitment to early
CC endosomes, while interaction with SLC9A3R1 and EZR might target the
CC protein to specialized subcellular regions, such as microvilli.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced.;
CC Name=1;
CC IsoId=O70528-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; Y13585; CAA73912.1; -; mRNA.
DR RefSeq; NP_001166434.1; NM_001172963.1. [O70528-1]
DR AlphaFoldDB; O70528; -.
DR SMR; O70528; -.
DR STRING; 10141.ENSCPOP00000011183; -.
DR BindingDB; O70528; -.
DR ChEMBL; CHEMBL5017; -.
DR DrugCentral; O70528; -.
DR Ensembl; ENSCPOT00000012547; ENSCPOP00000011183; ENSCPOG00000012428. [O70528-1]
DR GeneID; 100135548; -.
DR KEGG; cpoc:100135548; -.
DR CTD; 3360; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000155983; -.
DR HOGENOM; CLU_009579_11_0_1; -.
DR InParanoid; O70528; -.
DR OMA; AHQIRIL; -.
DR OrthoDB; 750855at2759; -.
DR TreeFam; TF316350; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000012428; Expressed in frontal cortex.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
DR GO; GO:0032098; P:regulation of appetite; IEA:InterPro.
DR InterPro; IPR001520; 5HT4_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01059; 5HT4RECEPTR.
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 Alternative splicing; Cell membrane; Disulfide bond; Endosome;
KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..388
FT /note="5-hydroxytryptamine receptor 4"
FT /id="PRO_0000068964"
FT TOPO_DOM 1..19
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 20..40
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 41..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 59..79
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 80..93
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 94..116
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 117..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 138..158
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 159..192
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 193..213
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 214..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 261..281
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 282..294
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 295..315
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 316..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT LIPID 329
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 93..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 388 AA; 43726 MW; 3D45B3A37F60D02B CRC64;
MDKLDANVSS KEGFGSVEKV VLLTFLSAVI LMAILGNLLV MVAVCRDRQL RKIKTNYFIV
SLAFADLLVS VLVMPFGAIE LVQDIWVYGE MFCLVRTSLD VLLTTASIFH LCCISLDRYY
AICCQPLVYR NKMTPLRIAL MLGGCWVIPM FISFLPIMQG WNNIGIVDLI EKRKFNQNSN
STYCVFMVNK PYAITCSVVA FYIPFLLMVL AYYRIYVTAK EHARQIQVLQ RAGAPAEGRP
QPADQHSTHR MRTETKAAKT LCIIMGCFCL CWAPFFVTNI VDPFIDYTVP GQLWTAFLWL
GYINSGLNPF LYAFLNKSFR RAFLIILCCD DERYRRPSIL GQTVPCSTTT INGSTHVLRD
TVECGGQWES QCHPAASSPL VAAQPIDT
