ID   5HTR_BOMMO              Reviewed;         446 AA.
AC   Q17239;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=5-hydroxytryptamine receptor;
DE            Short=5-HT receptor;
DE   AltName: Full=Serotonin receptor;
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Antenna;
RX   PubMed=9014328; DOI=10.1016/s0965-1748(96)00031-8;
RA   von Nickisch-Rosenegk E., Krieger J., Kubick S., Laage R., Strobel J.,
RA   Strotmann J., Breer H.;
RT   "Cloning of biogenic amine receptors from moths (Bombyx mori and Heliothis
RT   virescens).";
RL   Insect Biochem. Mol. Biol. 26:817-827(1996).
CC   -!- FUNCTION: This is a receptor for 5-hydroxytryptamine (serotonin), a
CC       biogenic hormone that function as a neurotransmitter, a hormone, and a
CC       mitogen. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; X95604; CAA64862.1; -; mRNA.
DR   RefSeq; NP_001037502.1; NM_001044037.1.
DR   AlphaFoldDB; Q17239; -.
DR   SMR; Q17239; -.
DR   STRING; 7091.BGIBMGA006929-TA; -.
DR   GeneID; 693054; -.
DR   KEGG; bmor:693054; -.
DR   CTD; 175322; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   HOGENOM; CLU_009579_11_1_1; -.
DR   OrthoDB; 703991at2759; -.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
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..446
FT                   /note="5-hydroxytryptamine receptor"
FT                   /id="PRO_0000068985"
FT   TOPO_DOM        1..65
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        66..88
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        89..98
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        99..120
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        121..135
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        136..157
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        158..176
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        177..199
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        200..227
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        228..249
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        250..367
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        368..391
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        392..399
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        400..422
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        423..446
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          304..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        23
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        134..214
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   446 AA;  48599 MW;  85D4E52C63726AA4 CRC64;
     MEGAEGQEEL DWEALYLRLP LQNCSWNSTG WEPNWNVTVV PNTTWWQASA PFDTPAALVR
     AAAKAVVLGL LILATVVGNV FVIAAILLER HLRSAANNLI LSLAVADLLV ACLVMPLGAV
     YEVVQRWTLG PELCDMWTSG DVLCCTASIL HLVAIALDRY WAVTNIDYIH ASTAKRVGMM
     IACVWTVSFF VCIAQLLGWK DPDWNQRVSE DLRCVVSQDV GYQIFATASS FYVPVLIILI
     LYWRIYQTAR KRIRRRRGAT ARGGVGPPPV PAGGALVAGG GSGGIAAAVV AVIGRPLPTI
     SETTTTGFTN VSSNNTSPEK QSCANGLEAD PPTTGYGAVA AAYYPSLVRR KPKEAADSKR
     ERKAAKTLAI ITGAFVACWL PFFVLAILVP TCDCEVSPVL TSLSLWLGYF NSTLNPVIYT
     VFSPEFRHAF QRLLCGRRVR RRRAPQ