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5HT7R_XENLA
ID   5HT7R_XENLA             Reviewed;         425 AA.
AC   Q91559;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=5-hydroxytryptamine receptor 7;
DE            Short=5-HT-7;
DE            Short=5-HT7;
DE   AltName: Full=Serotonin receptor 7;
GN   Name=htr7; Synonyms=5ht7;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skin;
RX   PubMed=8589994;
RA   Nelson C.S., Cone R.D., Robbins L.S., Allen C.N., Adelman J.P.;
RT   "Cloning and expression of a 5HT7 receptor from Xenopus laevis.";
RL   Recept. Channels 3:61-70(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   -!- 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; U10161; AAA96812.1; -; mRNA.
DR   RefSeq; NP_001079253.1; NM_001085784.1.
DR   AlphaFoldDB; Q91559; -.
DR   SMR; Q91559; -.
DR   GeneID; 378527; -.
DR   KEGG; xla:378527; -.
DR   CTD; 378527; -.
DR   Xenbase; XB-GENE-5959536; htr7l.S.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 378527; Expressed in camera-type eye and 3 other tissues.
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:InterPro.
DR   GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
DR   GO; GO:0007623; P:circadian rhythm; IEA:InterPro.
DR   GO; GO:0006939; P:smooth muscle contraction; IEA:InterPro.
DR   GO; GO:0042310; P:vasoconstriction; IEA:InterPro.
DR   InterPro; IPR001069; 5HT_7_rcpt.
DR   InterPro; IPR002231; 5HT_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00652; 5HT7RECEPTR.
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   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..425
FT                   /note="5-hydroxytryptamine receptor 7"
FT                   /id="PRO_0000068982"
FT   TOPO_DOM        1..70
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        71..97
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        98..107
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        108..133
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        134..145
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        146..167
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        168..187
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        188..211
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        212..226
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        227..249
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        250..324
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        325..348
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        349..360
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        361..383
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        384..425
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   LIPID           397
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        14
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        144..220
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   425 AA;  48017 MW;  C42C75ACB4A1A255 CRC64;
     MLIQVQPSHL TDTNLSLHSA KPSSDHQNLL PSEFMTERPL NTTEQDLTAL NHTEKPDCGK
     ELLLYGDTEK IVIGVVLSII TLFTIAGNAL VIISVCIVKK LRQPSNYLVV SLAAADLSVA
     VAVMPFVIIT DLVGGEWLFG KVFCNVFIAM DVMCCTASIM TLCVISVDRY LGITRPLTYP
     ARQNGKLMAK MVFIVWLLSA SITLPPLFGW AKNVNVERVC LISQDFGYTV YSTAVAFYIP
     MTVMLVMYQR IFVAAKISAE KHKFVNIPRL YEQEGIYCLE DKLPPKKNSK KKKAVEEFAS
     LSKLIRQDRK NISIFKREQK AARTLGIIVG AFTFCWLPFF LLSTARPFIC GIMCSCMPLR
     LERTLLWLGY TNSLINPLIY AFFNRDLRTT FWNLLRCKYT NINRRLSAAS MHEALKVTER
     HEGIL
 
 
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