5HT1B_RABIT
ID 5HT1B_RABIT Reviewed; 390 AA.
AC P49144;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=5-hydroxytryptamine receptor 1B;
DE Short=5-HT-1B;
DE Short=5-HT1B;
DE AltName: Full=Serotonin 1D beta receptor;
DE Short=5-HT-1D-beta;
DE AltName: Full=Serotonin receptor 1B;
GN Name=HTR1B;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=8543023; DOI=10.1016/0014-5793(95)01308-3;
RA Harwood G.S., Lockyer M., Giles H., Fairweather N.;
RT "Cloning and characterisation of the rabbit 5-HT1D alpha and 5-HT1D beta
RT receptors.";
RL FEBS Lett. 377:73-76(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=New Zealand white; TISSUE=Saphenous vein;
RA Wurch T., Cathala C., Palmer C., Valentin J.P., John G., Colpaert F.C.,
RA Pauwels P.J.;
RT "Molecular cloning and identification of a rabbit saphenous vein 5-HT 1DB
RT receptor gene.";
RL Neurosci. Res. Commun. 18:155-162(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=New Zealand white;
RX PubMed=8878052; DOI=10.1007/bf00171053;
RA Bard J.A., Kucharewicz S.A., Zgombick J.M., Weinshank R.L., Branchek T.A.,
RA Cohen M.L.;
RT "Differences in ligand binding profiles between cloned rabbit and human 5-
RT HT1D alpha and 5-HT1D beta receptors: ketanserin and methiothepin
RT distinguish rabbit 5-HT1D receptor subtypes.";
RL Naunyn Schmiedebergs Arch. Pharmacol. 354:237-244(1996).
CC -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine
CC (serotonin). Also functions as a receptor for various alkaloids and
CC psychoactive substances. Ligand binding causes a conformation change
CC that triggers signaling via guanine nucleotide-binding proteins (G
CC proteins) and modulates the activity of down-stream effectors, such as
CC adenylate cyclase. Signaling inhibits adenylate cyclase activity.
CC Arrestin family members inhibit signaling via G proteins and mediate
CC activation of alternative signaling pathways. Regulates the release of
CC 5-hydroxytryptamine, dopamine and acetylcholine in the brain, and
CC thereby affects neural activity, nociceptive processing, pain
CC perception, mood and behavior. Besides, plays a role in
CC vasoconstriction of cerebral arteries.
CC -!- SUBUNIT: Homodimer. Heterodimer with HTR1D (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- DOMAIN: Ligands are bound in a hydrophobic pocket formed by the
CC transmembrane helices. {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- PTM: Palmitoylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: A residue in the 7th transmembrane region ('Thr-355' in
CC human, 'Asn-351' in mouse and rat) is important for species-specific
CC sensitivity to various agonists. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; Z50163; CAA90531.1; -; Genomic_DNA.
DR EMBL; X89731; CAA61883.1; -; mRNA.
DR EMBL; U60826; AAB58467.1; -; Genomic_DNA.
DR PIR; S58126; S58126.
DR PIR; S68422; S68422.
DR RefSeq; NP_001076259.1; NM_001082790.1.
DR AlphaFoldDB; P49144; -.
DR SMR; P49144; -.
DR STRING; 9986.ENSOCUP00000016295; -.
DR BindingDB; P49144; -.
DR ChEMBL; CHEMBL5717; -.
DR GeneID; 100009594; -.
DR KEGG; ocu:100009594; -.
DR CTD; 3351; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P49144; -.
DR OrthoDB; 703991at2759; -.
DR TreeFam; TF316350; -.
DR PRO; PR:P49144; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; ISS:UniProtKB.
DR GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
DR GO; GO:0046849; P:bone remodeling; IEA:InterPro.
DR GO; GO:0071312; P:cellular response to alkaloid; ISS:UniProtKB.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
DR GO; GO:0014063; P:negative regulation of serotonin secretion; ISS:UniProtKB.
DR GO; GO:0050795; P:regulation of behavior; IEA:InterPro.
DR GO; GO:0042310; P:vasoconstriction; IEA:InterPro.
DR InterPro; IPR002147; 5HT1B_rcpt.
DR InterPro; IPR002231; 5HT_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24247:SF16; PTHR24247:SF16; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00513; 5HT1BRECEPTR.
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 Behavior; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..390
FT /note="5-hydroxytryptamine receptor 1B"
FT /id="PRO_0000068920"
FT TOPO_DOM 1..49
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 50..75
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 76..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 85..110
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 111..123
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 124..145
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 146..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 166..187
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 188..205
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 206..228
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 229..315
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 316..336
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 337..349
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 350..371
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 372..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 260..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 146..148
FT /note="DRY motif; important for ligand-induced conformation
FT changes and signaling"
FT /evidence="ECO:0000250"
FT MOTIF 365..369
FT /note="NPxxY motif; important for ligand-induced
FT conformation changes and signaling"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 134
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 201
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT SITE 355
FT /note="Important for species-specific agonist sensitivity"
FT /evidence="ECO:0000250"
FT LIPID 388
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 122..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 5
FT /note="G -> S (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 7
FT /note="Q -> R (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="Missing (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="R -> A (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 43496 MW; C22EBC077C6C897D CRC64;
MEEPGAQCAP PLAAGSQIAV PQANLSAAHS HNCSAEGYIY QDSIALPWKV LLVLLLALFT
LATTLSNAFV VATVYRTRKL HTPANYLIAS LAVTDLLVSI LVMPISTMYT VTGRWTLGQV
VCDLWLSSDI TCCTASIMHL CVIALDRYWA ITDAVEYSAK RTPKRAAIMI RLVWVFSICI
SLPPFFWRQA KAEEEVSECL VNTDHVLYTV YSTVGAFYLP TLLLIALYGR IYVEARSRIL
KQTPNRTGKR LTRAQLITDS PGSTTSVTSI NSRAPDVPSE SGSPVYVNQV KVRVSDALLE
KKKLMAARER KATKTLGIIL GVFIVCWLPF FIISLVMPIC KDACWFHQAI FDFFTWLGYV
NSLINPIIYT MSNEDFKQAF HKLIRFKCTS
