5HT7R_CAVPO
ID 5HT7R_CAVPO Reviewed; 446 AA.
AC P50407;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=5-hydroxytryptamine receptor 7;
DE Short=5-HT-7;
DE Short=5-HT7;
DE AltName: Full=5-HT-X;
DE AltName: Full=Serotonin receptor 7;
GN Name=HTR7;
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].
RC TISSUE=Hippocampus;
RX PubMed=7518496; DOI=10.1046/j.1471-4159.1994.63020456.x;
RA Tsou A., Kosaka A., Bach C., Zuppan P., Yee C., Tom L., Alvarez R.,
RA Ramsey S., Bonhaus D.W., Stefanich E., Jakeman L., Eglen R.M., Chan H.W.;
RT "Cloning and expression of a 5-hydroxytryptamine7 receptor positively
RT coupled to adenylyl cyclase.";
RL J. Neurochem. 63:456-464(1994).
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; U41372; AAA83015.1; -; mRNA.
DR RefSeq; NP_001166435.1; NM_001172964.1.
DR AlphaFoldDB; P50407; -.
DR SMR; P50407; -.
DR STRING; 10141.ENSCPOP00000006750; -.
DR BindingDB; P50407; -.
DR ChEMBL; CHEMBL5494; -.
DR GeneID; 100135549; -.
DR KEGG; cpoc:100135549; -.
DR CTD; 3363; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P50407; -.
DR OrthoDB; 1327781at2759; -.
DR PRO; PR:P50407; -.
DR Proteomes; UP000005447; 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: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; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00652; 5HT7RECEPTR.
DR PRINTS; PR00237; GPCRRHODOPSN.
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..446
FT /note="5-hydroxytryptamine receptor 7"
FT /id="PRO_0000068978"
FT TOPO_DOM 1..82
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 83..109
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 110..119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 120..145
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 146..157
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 158..179
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 180..199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 200..223
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 224..238
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 239..261
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 262..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 330..353
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 354..365
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 366..388
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 389..446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT LIPID 402
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 156..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 446 AA; 49614 MW; B63FA73712F3B088 CRC64;
MMGVNSSGRP DLYGHLHSIL LPGRGLPDWS PDGGADPGVS TWTPRLLSGV PEVAASPSPS
WDGTWDNVSG CGEQINYGRA EKVVIGSILT LITLLTIAGN CLVVISVCFV KKLRQPSNYL
IVSLALADLS VAVAVIPFVS VTDLIGGKWI FGHFFCNVFI AMDVMCCTAS IMTLCVISID
RYLGITRPLT YPVRQNGKCM PKMILSVWLL SASITLPPLF GWAQNVNDDK VCLISQDFGY
TIYSTAVAFY IPMSVMLFMY YRIYKAARKS AAKHKFPGFP RVQPESIISL NGMVKLQKEV
EECANLSRLL KHERKNISIF KREQKAATTL GIIVGAFTVC WLPFFLLSTA RPFICGTACS
CIPLWVERTC LWLGYANSLI NPFIYAFFNR DLRTTYRSLL QCQYRNINRK LSAAGMHEAL
KLAERPERPE CVLQNSDYCR KKGHDS
