5HT1A_CANLF
ID 5HT1A_CANLF Reviewed; 423 AA.
AC Q6XXX9;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=5-hydroxytryptamine receptor 1A;
DE Short=5-HT-1A;
DE Short=5-HT1A;
DE AltName: Full=Serotonin receptor 1A;
GN Name=HTR1A;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15220384; DOI=10.1093/jhered/esh033;
RA Kukekova A.V., Trut L.N., Oskina I.N., Kharlamova A.V., Shikhevich S.G.,
RA Kirkness E.F., Aguirre G.D., Acland G.M.;
RT "A marker set for construction of a genetic map of the silver fox (Vulpes
RT vulpes).";
RL J. Hered. 95:185-194(2004).
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, mood and behavior. Plays a role in the
CC response to anxiogenic stimuli (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes with GPER1 (By similarity).
CC Interacts with YIF1B (By similarity). {ECO:0000250|UniProtKB:P08908,
CC ECO:0000250|UniProtKB:P19327}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P19327};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P19327}. Cell
CC projection, dendrite {ECO:0000250|UniProtKB:P19327}.
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}.
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DR EMBL; AY204570; AAP12467.1; -; Genomic_DNA.
DR RefSeq; NP_001012397.1; NM_001012397.1.
DR AlphaFoldDB; Q6XXX9; -.
DR SMR; Q6XXX9; -.
DR STRING; 9615.ENSCAFP00000037035; -.
DR PaxDb; Q6XXX9; -.
DR GeneID; 487230; -.
DR KEGG; cfa:487230; -.
DR CTD; 3350; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q6XXX9; -.
DR OrthoDB; 703991at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
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:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0051378; F:serotonin binding; IBA:GO_Central.
DR GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0001662; P:behavioral fear response; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0035640; P:exploration behavior; ISS:UniProtKB.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR GO; GO:0050795; P:regulation of behavior; IEA:InterPro.
DR GO; GO:0042053; P:regulation of dopamine metabolic process; ISS:UniProtKB.
DR GO; GO:0046883; P:regulation of hormone secretion; IEA:InterPro.
DR GO; GO:0014062; P:regulation of serotonin secretion; ISS:UniProtKB.
DR GO; GO:0019229; P:regulation of vasoconstriction; IEA:InterPro.
DR GO; GO:0042428; P:serotonin metabolic process; ISS:UniProtKB.
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 3: Inferred from homology;
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..423
FT /note="5-hydroxytryptamine receptor 1A"
FT /id="PRO_0000068901"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 37..62
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 63..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 74..98
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 99..110
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 111..132
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 133..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 153..178
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 179..191
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 192..217
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 218..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 346..367
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 368..378
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 379..403
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 404..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 235..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 133..135
FT /note="DRY motif; important for ligand-induced conformation
FT changes"
FT /evidence="ECO:0000250"
FT MOTIF 396..400
FT /note="NPxxY motif; important for ligand-induced
FT conformation changes and signaling"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 121
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 189
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT CARBOHYD 10
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 109..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 423 AA; 46356 MW; 0E397FD4AE673269 CRC64;
MEGLSPRQGN NTTSSEGPFG TLGNATGISD VTFSYQVITS LLLGTLIFCA VLGNACVVAA
IALERSLQNV ANYLIGSLAV TDLMVSVLVL PMAALYQVLN KWTLGQVTCD LFIALDVLCC
TSSILHLCAI ALDRYWAITD PIDYVNKRTP RRAAALISLT WLIGFLISIP PMLGWRTPED
RSDPDACTIS KDHGYTIYST FGAFYIPLLL MLVLYGRIFR AARFRIRKTV KKAERKGADA
RSGVSPAPQP RKSVNGEPGG REWRQGPGSQ AGGPLCTNGA VRRGDDGAAL EVIEVHRVGS
SKEHLPLPCE AGAIPCAPAS FEKKNERNAE AKRKMALARE RKTVKTLGII MGTFILCWLP
FFIVALVLPF CESSCHMPTL LGAIINWLGY SNSLLNPVIY AYFNKDFQNA FKKIVRCKFC
RRR
