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Database: UniProt/SWISS-PROT
Entry: 5HT1A_PANTR
LinkDB: 5HT1A_PANTR
Original site: 5HT1A_PANTR 
ID   5HT1A_PANTR             Reviewed;         422 AA.
AC   Q9N298;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   16-OCT-2019, entry version 119.
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   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15014171; DOI=10.1093/molbev/msh100;
RA   Kitano T., Liu Y.-H., Ueda S., Saitou N.;
RT   "Human-specific amino acid changes found in 103 protein-coding
RT   genes.";
RL   Mol. Biol. Evol. 21:936-944(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
CC       change that triggers signaling via guanine nucleotide-binding
CC       proteins (G proteins) and modulates the activity of down-stream
CC       effectors, such as adenylate cyclase. Beta-arrestin family members
CC       inhibit signaling via G proteins and mediate activation of
CC       alternative signaling pathways. Signaling inhibits adenylate
CC       cyclase activity and activates a phosphatidylinositol-calcium
CC       second messenger system that regulates the release of Ca(2+) ions
CC       from intracellular stores. Plays a role in the regulation of 5-
CC       hydroxytryptamine release and in the regulation of dopamine and 5-
CC       hydroxytryptamine metabolism. Plays a role in the regulation of
CC       dopamine and 5-hydroxytryptamine levels in the brain, and thereby
CC       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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
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}.
DR   EMBL; AB041404; BAA94489.1; -; Genomic_DNA.
DR   RefSeq; NP_001129094.1; NM_001135622.1.
DR   STRING; 9598.ENSPTRP00000028964; -.
DR   PaxDb; Q9N298; -.
DR   Ensembl; ENSPTRT00000031362; ENSPTRP00000028964; ENSPTRG00000016918.
DR   GeneID; 471533; -.
DR   KEGG; ptr:471533; -.
DR   CTD; 3350; -.
DR   VGNC; VGNC:8624; HTR1A.
DR   eggNOG; KOG3656; Eukaryota.
DR   eggNOG; ENOG410XRW9; LUCA.
DR   GeneTree; ENSGT00940000154484; -.
DR   HOGENOM; HOG000239242; -.
DR   InParanoid; Q9N298; -.
DR   KO; K04153; -.
DR   OMA; DPGYTIY; -.
DR   OrthoDB; 703991at2759; -.
DR   Proteomes; UP000002277; Chromosome 5.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
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:0090722; F:receptor-receptor interaction; IEA:Ensembl.
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:0008283; P:cell population proliferation; IEA:InterPro.
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:0042428; P:serotonin metabolic process; ISS:UniProtKB.
DR   GO; GO:0007210; P:serotonin receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0042310; P:vasoconstriction; IEA:InterPro.
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; Complete proteome; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN         1    422       5-hydroxytryptamine receptor 1A.
FT                                /FTId=PRO_0000068905.
FT   TOPO_DOM      1     36       Extracellular. {ECO:0000250}.
FT   TRANSMEM     37     62       Helical; Name=1. {ECO:0000250}.
FT   TOPO_DOM     63     73       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM     74     98       Helical; Name=2. {ECO:0000250}.
FT   TOPO_DOM     99    110       Extracellular. {ECO:0000250}.
FT   TRANSMEM    111    132       Helical; Name=3. {ECO:0000250}.
FT   TOPO_DOM    133    152       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM    153    178       Helical; Name=4. {ECO:0000250}.
FT   TOPO_DOM    179    191       Extracellular. {ECO:0000250}.
FT   TRANSMEM    192    217       Helical; Name=5. {ECO:0000250}.
FT   TOPO_DOM    218    345       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM    346    367       Helical; Name=6. {ECO:0000250}.
FT   TOPO_DOM    368    378       Extracellular. {ECO:0000250}.
FT   TRANSMEM    379    403       Helical; Name=7. {ECO:0000250}.
FT   TOPO_DOM    404    422       Cytoplasmic. {ECO:0000250}.
FT   REGION      112    121       Agonist binding. {ECO:0000250}.
FT   REGION      358    362       Agonist binding. {ECO:0000250}.
FT   MOTIF       133    135       DRY motif; important for ligand-induced
FT                                conformation changes. {ECO:0000250}.
FT   MOTIF       396    400       NPxxY motif; important for ligand-induced
FT                                conformation changes and signaling.
FT                                {ECO:0000250}.
FT   CARBOHYD     10     10       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     11     11       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     24     24       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    109    187       {ECO:0000255|PROSITE-ProRule:PRU00521}.
SQ   SEQUENCE   422 AA;  46172 MW;  FCD989BD0313A1A0 CRC64;
     MDVLSPGQGN NTTSPPAPFE TGGNTSGISD VTFSYQVITS LLLGTLIFCA VLGNACVVAA
     IALERSLQNV ANYLIGSLAV TDLMVSVLVL PMAALYQVLN KWTLGQVTCD LFIALDVLCC
     TSSILHLCAI ALDRYWAITD PIDYVNKRTP RRAAALISLT WLIGFLISIP PMLGWRTPED
     RSDPDACTIS KDHGYTIYST FGAFYIPLLL MLVLYGRIFR AARFRIRKTV KKVEKTGADT
     RHGASPAQQP KKSVNGESGS RNWRLGVESK AGGALCANGA VRQGDDGAAL EVIEVHRVGN
     SKEHLPLPSE AGPTPCAPAS FERKNERNAE AKRKMALARE RKTVKTLGII MGTFILCWLP
     FFIVALVLPF CESSCHMPTL LGAIINWLGY SNSLLNPVIY AYFNKDFQNA FKKIIKCKFC
     RQ
//
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