ID G5BGB1_HETGA Unreviewed; 421 AA.
AC G5BGB1;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=5-hydroxytryptamine receptor 1A {ECO:0000256|ARBA:ARBA00017605};
DE AltName: Full=Serotonin receptor 1A {ECO:0000256|ARBA:ARBA00032310};
GN Name=HTR1A {ECO:0000313|EMBL:JAN98195.1};
GN ORFNames=GW7_05879 {ECO:0000313|EMBL:EHB08322.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB08322.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB08322.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
RN [2] {ECO:0000313|EMBL:JAN98195.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Hypothalamus {ECO:0000313|EMBL:JAN98195.1};
RA Bens M., Sahm A., Jahn N., Morhart M., Holtze S., Hildebrandt T.B.,
RA Platzer M., Szafranski K.;
RT "FRAMA: From RNA-seq data to annotated mRNA assemblies.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00024768}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cell
CC projection, dendrite {ECO:0000256|ARBA:ARBA00004279}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000256|RuleBase:RU000688}.
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DR EMBL; JH170093; EHB08322.1; -; Genomic_DNA.
DR EMBL; GEBF01005437; JAN98195.1; -; Transcribed_RNA.
DR RefSeq; XP_004862939.1; XM_004862882.2.
DR AlphaFoldDB; G5BGB1; -.
DR STRING; 10181.G5BGB1; -.
DR Ensembl; ENSHGLT00100000301; ENSHGLP00100000274; ENSHGLG00100000235.
DR Ensembl; ENSHGLT00100063392; ENSHGLP00100051759; ENSHGLG00100000235.
DR Ensembl; ENSHGLT00100077033; ENSHGLP00100040223; ENSHGLG00100000235.
DR KEGG; hgl:101718872; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; G5BGB1; -.
DR OMA; CAESCYM; -.
DR OrthoDB; 2999405at2759; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR Bgee; ENSHGLG00000008662; Expressed in hypothalamus and 4 other cell types or tissues.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IEA:Ensembl.
DR GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
DR GO; GO:0035640; P:exploration behavior; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0046883; P:regulation of hormone secretion; IEA:InterPro.
DR GO; GO:0014062; P:regulation of serotonin secretion; IEA:Ensembl.
DR GO; GO:0019229; P:regulation of vasoconstriction; IEA:InterPro.
DR GO; GO:0042428; P:serotonin metabolic process; IEA:Ensembl.
DR GO; GO:0007210; P:serotonin receptor signaling pathway; IEA:Ensembl.
DR CDD; cd15330; 7tmA_5-HT1A_vertebrates; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR000610; 5HT1A_rcpt.
DR InterPro; IPR002231; 5HT_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24248; ADRENERGIC RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
DR PANTHER; PTHR24248:SF191; G-PROTEIN COUPLED RECEPTORS FAMILY 1 PROFILE DOMAIN-CONTAINING PROTEIN; 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 SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW G-protein coupled receptor {ECO:0000256|RuleBase:RU000688};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000688};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW Transducer {ECO:0000256|RuleBase:RU000688};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000688};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 72..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 346..367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 379..402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 52..399
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
FT REGION 240..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 421 AA; 46596 MW; B8AA4B20B5E722F9 CRC64;
MDVLSPGGGN NTTSQGPFGT KANVTRISDV TFSYQVITSL LLGMLIFCAV LGNACVVAAI
ALERSLQNVA NYLIGSLAVT DLMVSVLVLP MAALYQVLNK WTLGQVTCDL FIALDVLCCT
SSILHLCAIA LDRYWAITDP IDYVNKRTPR RAAVLISLTW LIGFLISIPP MLGWRTPEDR
SDADACTISK DHGYTIYSTF GAFYIPLLLM LVLYGRIFRA ARFRIRKTVK KVEKKGVDTR
LGTSLVPPSK RRVNGQPGDR DWRRGVENKA TGAPCANGAL RQGDEGATLE VIEVHRVGNS
KEHLPLPREP SADPGVPTSF ERKNERNAEA KRKMALARER KTVKTLGIIM GTFILCWLPF
FIVALVLPFC ESSCHMPTLL GAIINWLGYS NSLLNPVIYA YFNKDFQNAF KKIIKCKFCR
P
//
