ID   5HTR_LYMST              Reviewed;         509 AA.
AC   Q25414;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=5-hydroxytryptamine receptor;
DE            Short=5-HT receptor;
DE   AltName: Full=Serotonin receptor;
OS   Lymnaea stagnalis (Great pond snail) (Helix stagnalis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC   Lymnaeidae; Lymnaea.
OX   NCBI_TaxID=6523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8093556; DOI=10.1073/pnas.90.1.11;
RA   Sugamori K.S., Sunahara R.K., Guan H.-C., Bulloch A.G., Tensen C.P.,
RA   Seeman P., Niznik H.B., van Tol H.H.;
RT   "Serotonin receptor cDNA cloned from Lymnaea stagnalis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:11-15(1993).
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.
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; L06803; AAA29290.1; -; mRNA.
DR   PIR; A47174; A47174.
DR   AlphaFoldDB; Q25414; -.
DR   SMR; Q25414; -.
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; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..509
FT                   /note="5-hydroxytryptamine receptor"
FT                   /id="PRO_0000068987"
FT   TOPO_DOM        1..99
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        100..122
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        123..132
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        133..154
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        155..169
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        170..191
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        192..210
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        211..233
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        234..259
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        260..281
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        282..432
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        433..456
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        457..465
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        466..488
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        489..509
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          323..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..372
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        3
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        78
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        168..246
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   509 AA;  56902 MW;  D283696C8C50B1B8 CRC64;
     MANFTFGDLA LDVARMGGLA STPSGLRSTG LTTPGLSPTG LVTSDFNDSY GLTGQFINGS
     HSSRSRDNAS ANDTSATNMT DDRYWSLTVY SHEHLVLTSV ILGLFVLCCI IGNCFVIAAV
     MLERSLHNVA NYLILSLAVA DLMVAVLVMP LSVVSEISKV WFLHSEVCDM WISVDVLCCT
     ASILHLVAIA MDRYWAVTSI DYIRRRSARR ILLMIMVVWI VALFISIPPL FGWRDPNNDP
     DKTGTCIISQ DKGYTIFSTV GAFYLPMLVM MIIYIRIWLV ARSRIRKDKF QMTKARLKTE
     ETTLVASPKT EYSVVSDCNG CNSPDSTTEK KKRRAPFKSY GCSPRPERKK NRAKKLPENA
     NGVNSNSSSS ERLKQIQIET AEAFANGCAE EASIAMLERQ CNNGKKISSN DTPYSRTREK
     LELKRERKAA RTLAIITGAF LICWLPFFII ALIGPFVDPE GIPPFARSFV LWLGYFNSLL
     NPIIYTIFSP EFRSAFQKIL FGKYRRGHR