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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
 
 
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