5HT1A_XENLA
ID 5HT1A_XENLA Reviewed; 408 AA.
AC Q98998;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=5-hydroxytryptamine receptor 1A;
DE Short=5-HT-1A;
DE Short=5-HT1A;
DE Short=x5-HT1A;
DE AltName: Full=Serotonin receptor 1A;
GN Name=htr1a {ECO:0000250|UniProtKB:P08908};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAA69208.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain {ECO:0000312|EMBL:CAA69208.1};
RX PubMed=9221903; DOI=10.1016/s0169-328x(97)00052-1;
RA Marracci S., Cini D., Nardi I.;
RT "Cloning and developmental expression of 5-HT1A receptor gene in Xenopus
RT laevis.";
RL Brain Res. Mol. Brain Res. 47:67-77(1997).
RN [2] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9878840; DOI=10.1016/s0169-328x(98)00305-2;
RA Cappellini C., Malatesta P., Costa B., Marracci S., Nardi I., Martini C.;
RT "Characterization of a cloned Xenopus laevis serotonin 5-HT1A receptor
RT expressed in the NIH-3T3 cell line.";
RL Brain Res. Mol. Brain Res. 63:380-383(1999).
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. Activation of the
CC receptor may play a role in the exit from G0 phase and in promoting DNA
CC synthesis. {ECO:0000269|PubMed:9878840}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9878840};
CC Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:9878840}.
CC Cell projection, dendrite {ECO:0000250|UniProtKB:P19327}.
CC -!- TISSUE SPECIFICITY: First expressed in the rostral part of the brain
CC stem at stage 22. At later stages of development, expression is
CC localized to serotonergic neurons. The expression pattern changes in
CC the tadpole of stage 41 where, in addition to serotonergic neurons,
CC expression is also localized to the inner nuclear layer (INL) of the
CC developing retina. This expression pattern continues through to the
CC start of metamorphosis (stage 46). In adults, expressed in the brain,
CC in particular the telencephalon, diencephalon and mesencephalon. In the
CC telencephalic region, expression is localized to the lateral, dorsal
CC and medial pallium, and in the striatum, septum and amygdala. In the
CC mesencephalic region, expression is strongest in the optic tectum and
CC torus semicircularis with moderate levels of expression in tegmental
CC nuclei. In diencephalon, localized to the dorsal and ventral thalamus
CC and the preoptic area of the hypothalamus.
CC {ECO:0000269|PubMed:9221903}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. 5-
CC hydroxytryptamine receptor subfamily. HTR1A sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y07901; CAA69208.1; -; mRNA.
DR RefSeq; NP_001079299.1; NM_001085830.1.
DR AlphaFoldDB; Q98998; -.
DR SMR; Q98998; -.
DR GeneID; 378605; -.
DR KEGG; xla:378605; -.
DR CTD; 378605; -.
DR Xenbase; XB-GENE-984751; htr1a.L.
DR OrthoDB; 737211at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 378605; Expressed in brain and 2 other tissues.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
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:0006260; P:DNA replication; IDA:UniProtKB.
DR GO; GO:0050795; P:regulation of behavior; IEA:InterPro.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IDA:UniProtKB.
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 PANTHER; PTHR24247:SF20; PTHR24247:SF20; 1.
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 2: Evidence at transcript level;
KW Behavior; Cell membrane; Cell projection; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..408
FT /note="5-hydroxytryptamine receptor 1A"
FT /id="PRO_0000245784"
FT TOPO_DOM 1..30
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 31..56
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 57..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 68..92
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 93..104
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 105..126
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 127..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 147..172
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 173..185
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 186..211
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 212..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 333..354
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 355..365
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 366..389
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 390..408
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 235..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 127..129
FT /note="DRY motif; important for ligand-induced conformation
FT changes"
FT /evidence="ECO:0000250"
FT MOTIF 382..386
FT /note="NPxxY motif; important for ligand-induced
FT conformation changes and signaling"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 115
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 183
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 DISULFID 103..181
FT /evidence="ECO:0000250|UniProtKB:P08908,
FT ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 408 AA; 45788 MW; 2CB6156F7D53B1B5 CRC64;
MDASNNTTSW NILQRGRMGP SWRRCPVSYQ IIASLFLGRS FSAGIFGNAC VIAAIALERS
LQNVANYLIG SLAVTDLMVS VLVLPMAAQN QVLNKWTLGQ VTCDIFISLD VLCCTSSILH
LCAIALDRYW AITDPIDYVN KRTPRRAAVL ISITWIVGFS ISIPPMLGWR TPEDRSDPNA
CRISEDPGYT IYSTFGAFYI PLILMLVLYG KIFKAARFRI RKTVKKAEKK KVADTCLSVS
QQSPKEKQRG AQQELEEVGG AQAQRCVNGA IRHGEEGAVL EIIEVHHYVN SKCHLHCKPV
PPPEQLPPAL KNDRATEAKR KVALARERKT VKTLGIIMGT FILCWLPFFI VALVLPFCET
CHMPHLLFDI ITWLGYSNSL LNPIIYAYFN KDFQSAFKKI IKCKFCRQ
