5HT4R_PIG
ID 5HT4R_PIG Reviewed; 137 AA.
AC Q29006;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=5-hydroxytryptamine receptor 4;
DE Short=5-HT-4;
DE Short=5-HT4;
DE AltName: Full=Serotonin receptor 4;
DE Flags: Fragment;
GN Name=HTR4;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7656980; DOI=10.1016/0014-5793(95)00828-w;
RA Ullmer C., Schmuck K., Kalkman H.O., Luebbert H.;
RT "Expression of serotonin receptor mRNAs in blood vessels.";
RL FEBS Lett. 370:215-221(1995).
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.
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). {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 Interacts (via C-terminus) with GRK5; this interaction is promoted by
CC 5-HT (serotonin). {ECO:0000250}.
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; Z48175; CAA88198.1; -; mRNA.
DR PIR; S66487; S66487.
DR AlphaFoldDB; Q29006; -.
DR SMR; Q29006; -.
DR STRING; 9823.ENSSSCP00000015354; -.
DR BindingDB; Q29006; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_11_0_1; -.
DR InParanoid; Q29006; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; Q29006; SS.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IBA:GO_Central.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0051378; F:serotonin binding; IBA:GO_Central.
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: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 PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Endosome; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN <1..>137
FT /note="5-hydroxytryptamine receptor 4"
FT /id="PRO_0000068967"
FT TOPO_DOM <1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 16..36
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 37..70
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 71..91
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 92..>137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 112..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_TER 1
FT NON_TER 137
SQ SEQUENCE 137 AA; 15622 MW; C9D60744DA4D0263 CRC64;
CCQPLVYRNK MTPLRVAVLL AGCWAIPVLI SFLPIMQGWN NIGITDLIEK RKFHQNSNST
YCIFMVNKPY AITCSVVAFY IPFLLMVLAY WRIYVTAKEH AHQIQMLQRA GAPAEGRPPS
ADQHSTHRMR TETKAAK
