5H1AA_TAKRU
ID 5H1AA_TAKRU Reviewed; 423 AA.
AC O42385;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=5-hydroxytryptamine receptor 1A-alpha;
DE Short=5-HT-1A-alpha;
DE Short=5-HT1A-alpha;
DE AltName: Full=F1A;
DE AltName: Full=Serotonin receptor 1A-alpha;
GN Name=htr1aa;
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; X95936; CAA65175.1; -; Genomic_DNA.
DR AlphaFoldDB; O42385; -.
DR SMR; O42385; -.
DR Ensembl; ENSTRUT00000006732; ENSTRUP00000057435; ENSTRUG00000002876.
DR GeneTree; ENSGT00940000154484; -.
DR InParanoid; O42385; -.
DR Proteomes; UP000005226; Chromosome 21.
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 GO; GO:0021522; P:spinal cord motor neuron differentiation; IEA:Ensembl.
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; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..423
FT /note="5-hydroxytryptamine receptor 1A-alpha"
FT /id="PRO_0000068909"
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..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 83..107
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 108..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..186
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 187..200
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 201..226
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 227..346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 347..368
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 369..379
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 380..404
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 405..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 311..332
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"
FT /evidence="ECO:0000250"
FT MOTIF 397..401
FT /note="NPxxY motif; important for ligand-induced
FT conformation changes and signaling"
FT /evidence="ECO:0000250"
FT COMPBIAS 311..326
FT /note="Polar 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 198
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 118..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 423 AA; 47001 MW; 7B1308626B40190F CRC64;
MDLRATSSND SNATSGYSDT AAVDWDEGEN ATGSGSLPDP ELSYQIITSL FLGALILCSI
FGNSCVVAAI ALERSLQNVA NYLIGSLAVT DLMVSVLVLP MAALYQVLNK WTLGQDICDL
FIALDVLCCT SSILHLCAIA LDRYWAITDP IDYVNKRTPR RAAVLISVTW LIGFSISIPP
MLGWRSAEDR ANPDACIISQ DPGYTIYSTF GAFYIPLILM LVLYGRIFKA ARFRIRKTVK
KTEKAKASDM CLTLSPAVFH KRANGDAVSA EWKRGYKFKP SSPCANGAVR HGEEMESLEI
IEVNSNSKTH LPLPNTPQSS SHENINEKTT GTRRKIALAR ERKTVKTLGI IMGTFIFCWL
PFFIVALVLP FCAENCYMPE WLGAVINWLG YSNSLLNPII YAYFNKDFQS AFKKILRCKF
HRH
