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5HT1A_GORGO
ID   5HT1A_GORGO             Reviewed;         422 AA.
AC   Q9N297;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 122.
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   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595;
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 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 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; AB041405; BAA94490.1; -; Genomic_DNA.
DR   RefSeq; XP_004058839.1; XM_004058791.2.
DR   AlphaFoldDB; Q9N297; -.
DR   SMR; Q9N297; -.
DR   STRING; 9593.ENSGGOP00000005548; -.
DR   Ensembl; ENSGGOT00000005692; ENSGGOP00000005548; ENSGGOG00000005667.
DR   GeneID; 101145070; -.
DR   KEGG; ggo:101145070; -.
DR   CTD; 3350; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000154484; -.
DR   HOGENOM; CLU_009579_11_1_1; -.
DR   InParanoid; Q9N297; -.
DR   OMA; CAESCYM; -.
DR   OrthoDB; 703991at2759; -.
DR   Proteomes; UP000001519; Chromosome 17.
DR   Bgee; ENSGGOG00000005667; Expressed in prefrontal cortex.
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: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: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:0007214; P:gamma-aminobutyric acid signaling pathway; IEA:Ensembl.
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..422
FT                   /note="5-hydroxytryptamine receptor 1A"
FT                   /id="PRO_0000068902"
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..422
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          235..262
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   422 AA;  46155 MW;  012335E0403F1B90 CRC64;
     MDVLSPGQGN NTTSPPAPFE TGGNTTGISD VTFSYQVITS LLLGTLIFCA VLGNACVVAA
     IALERSLQNV ANYLIGSLAV TDLMVSVLVL PMAALYQVLN KWTLGQVTCD LFIALDVLCC
     TSSILHLCAI ALDRYWAITD PIDYVNKRTP RRAAALISLT WLIGFLISIP PMLGWRTPED
     RSDPDACTIS KDHGYTIYST FGAFYIPLLL MLVLYGRIFR AARFRIRKTV KKVEKTGADT
     RHGASPAPQP KKSVNGESGS RNWRLGVESK AGGALCANGA VRQGDDGAAL EVIEVHRVGN
     SKEHLPLPSE AGPTPCAPAS FERKNERNAE AKRKMALARE RKTVKTLGII MGTFILCWLP
     FFIVALVLPF CESSCHMPTL LGAIINWLGY SNSLLNPVIY AYFNKDFQNA FKKIIKCKFC
     RQ
 
 
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