5H1AB_TAKRU
ID 5H1AB_TAKRU Reviewed; 416 AA.
AC O42384;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=5-hydroxytryptamine receptor 1A-beta;
DE Short=5-HT-1A-beta;
DE Short=5-HT1A-beta;
DE AltName: Full=F1B;
DE AltName: Full=Serotonin receptor 1A-beta;
GN Name=htr1a-B;
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Testis;
RX PubMed=9218723; DOI=10.1016/s0378-1119(97)00064-4;
RA Yamaguchi F., Brenner S.;
RT "Molecular cloning of 5-hydroxytryptamine (5-HT) type 1 receptor genes from
RT the Japanese puffer fish, Fugu rubripes.";
RL Gene 191:219-223(1997).
CC -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine
CC (serotonin). Also functions as a receptor for various drugs 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. Beta-arrestin family members inhibit signaling via G
CC proteins and mediate activation of alternative signaling pathways.
CC Signaling inhibits adenylate cyclase activity and activates a
CC phosphatidylinositol-calcium second messenger system that regulates the
CC release of Ca(2+) ions from intracellular stores. Plays a role in the
CC regulation of 5-hydroxytryptamine release and in the regulation of
CC dopamine and 5-hydroxytryptamine metabolism. Plays a role in the
CC regulation of dopamine and 5-hydroxytryptamine levels in the brain, and
CC thereby affects neural activity and behavior (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. 5-
CC hydroxytryptamine receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00521}.
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DR EMBL; X95937; CAA65176.1; -; Genomic_DNA.
DR RefSeq; XP_003977344.1; XM_003977295.1.
DR AlphaFoldDB; O42384; -.
DR SMR; O42384; -.
DR STRING; 31033.ENSTRUP00000014451; -.
DR Ensembl; ENSTRUT00000014518; ENSTRUP00000014451; ENSTRUG00000005939.
DR GeneID; 101072291; -.
DR KEGG; tru:101072291; -.
DR CTD; 101072291; -.
DR GeneTree; ENSGT01010000222287; -.
DR InParanoid; O42384; -.
DR OrthoDB; 703991at2759; -.
DR Proteomes; UP000005226; Chromosome 6.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
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:0050795; P:regulation of behavior; IEA:InterPro.
DR GO; GO:0046883; P:regulation of hormone secretion; IEA:InterPro.
DR GO; GO:0019229; P:regulation of vasoconstriction; IEA:InterPro.
DR GO; GO:0007210; P:serotonin receptor signaling pathway; ISS:UniProtKB.
DR InterPro; IPR000610; 5HT1A_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; PR00512; 5HT1ARECEPTR.
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; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..416
FT /note="5-hydroxytryptamine receptor 1A-beta"
FT /id="PRO_0000068924"
FT TOPO_DOM 1..33
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 34..59
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 60..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 71..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 96..107
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 108..129
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 130..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 150..174
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 175..193
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 194..219
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 220..339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 340..361
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 362..372
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 373..397
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 398..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 130..132
FT /note="DRY motif; important for ligand-induced conformation
FT changes"
FT /evidence="ECO:0000250"
FT MOTIF 390..394
FT /note="NPxxY motif; important for ligand-induced
FT conformation changes and signaling"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 118
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 191
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 106..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 416 AA; 47031 MW; 9B4CC415BEC750FE CRC64;
MEGTNNTTGW THFDSTSNRT SKSFDEEVKL SYQVVTSFLL GALILCSIFG NACVVAAIAL
ERSLQNVANY LIGSLAVTDL MVSVLVLPMA ALYQVLNRWT LGQIPCDIFI SLDMLCCTSS
ILHLCVIALD RYWAITEPID YMKKRTPRRA AVLISVTWLV GFSISIPPML IMRSQPSSMA
EDRANSKQCK ITQDPWYTIY STFGAFYIPL TLMLVLYGRI FKAARFRIRR TVRKTEKKKV
SDTCLALSPA MFHRKTPGDA HGKSWKRSVE PRPLPNVNGA VKHAGEGESL DIIEVQSNSR
CNLPLPNTPG TVPLFENRHE KATETKRKIA LARERKTVKT LGIIMGTFIL CWLPFFIVAL
VMPFCQESCF MPHWLKDVIN WLGYSNSLLN PIIYAYFNKD FQSAFKKIIK CHFCRA
