5HT1B_SPAEH
ID 5HT1B_SPAEH Reviewed; 386 AA.
AC P56496;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=5-hydroxytryptamine receptor 1B;
DE Short=5-HT-1B;
DE Short=5-HT1B;
DE AltName: Full=Serotonin receptor 1B;
GN Name=HTR1B; Synonyms=5HT1B;
OS Spalax ehrenbergi (Middle East blind mole rat) (Nannospalax ehrenbergi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Spalacidae; Spalacinae; Nannospalax.
OX NCBI_TaxID=30637;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Devor E.J., Nevo E.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Heterodimer with HTR1D (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
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; AF027184; AAB82748.1; -; Genomic_DNA.
DR AlphaFoldDB; P56496; -.
DR SMR; P56496; -.
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 3: Inferred from homology;
KW Behavior; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..386
FT /note="5-hydroxytryptamine receptor 1B"
FT /id="PRO_0000068922"
FT TOPO_DOM 1..45
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 46..71
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 72..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 81..106
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 107..119
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 120..141
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 142..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 162..183
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 184..201
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 202..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 225..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 312..332
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 333..345
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 346..367
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 368..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 142..144
FT /note="DRY motif; important for ligand-induced conformation
FT changes and signaling"
FT /evidence="ECO:0000250"
FT MOTIF 361..365
FT /note="NPxxY motif; important for ligand-induced
FT conformation changes and signaling"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..17
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 125
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 130
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 197
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT SITE 351
FT /note="Important for species-specific agonist sensitivity"
FT /evidence="ECO:0000250"
FT LIPID 384
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 118..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 386 AA; 43102 MW; 7A006E021A44B7F4 CRC64;
MEEPGARCAP PPPAGSQTQT PSSNLSHNCS ADSYIYQDSI ALPWKVLLVA LLALITLATT
LSNAFVIATV YRTRKLHTPA NYLIASLAVT DLLVSILVMP ISTMYTVTGR WTLGQVVCDF
WLSSDITCCT ASIMHLCVIA LDRYWAITDA VEYSAKRTPR RAAVMIALVW VFSISISLPR
FFWRQAKAEE EVLDCLVNTD HVLYTVYSTV GAFYLPTLLL IALYGRIYVE ARSRILKQTP
NKTGKRLSRA QLISDSPGST SSVTSINSRV PDVPSESGSP VYVNQVKVRV SDALLEKKKL
MAARERKATK TLGIILGAFI VCWLPFFIIS LVMPICKDAC WFHMAIFDFF NWLGYLNSLI
NPIIYTMPNE DFKQAFHKLI RFKCTG
