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Protein

5-hydroxytryptamine receptor 1A-beta

Gene

htr1a-B

Organism
Takifugu rubripes (Japanese pufferfish) (Fugu rubripes)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling inhibits adenylate cyclase activity and activates a phosphatidylinositol-calcium second messenger system that regulates the release of Ca2+ ions from intracellular stores. Plays a role in the regulation of 5-hydroxytryptamine release and in the regulation of dopamine and 5-hydroxytryptamine metabolism. Plays a role in the regulation of dopamine and 5-hydroxytryptamine levels in the brain, and thereby affects neural activity and behavior (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Behavior

Names & Taxonomyi

Protein namesi
Recommended name:
5-hydroxytryptamine receptor 1A-beta
Short name:
5-HT-1A-beta
Short name:
5-HT1A-beta
Alternative name(s):
F1B
Serotonin receptor 1A-beta
Gene namesi
Name:htr1a-B
OrganismiTakifugu rubripes (Japanese pufferfish) (Fugu rubripes)
Taxonomic identifieri31033 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataEupercariaTetraodontiformesTetradontoideaTetraodontidaeTakifugu
Proteomesi
  • UP000005226 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 33ExtracellularBy similarityAdd BLAST33
Transmembranei34 – 59Helical; Name=1By similarityAdd BLAST26
Topological domaini60 – 70CytoplasmicBy similarityAdd BLAST11
Transmembranei71 – 95Helical; Name=2By similarityAdd BLAST25
Topological domaini96 – 107ExtracellularBy similarityAdd BLAST12
Transmembranei108 – 129Helical; Name=3By similarityAdd BLAST22
Topological domaini130 – 149CytoplasmicBy similarityAdd BLAST20
Transmembranei150 – 174Helical; Name=4By similarityAdd BLAST25
Topological domaini175 – 193ExtracellularBy similarityAdd BLAST19
Transmembranei194 – 219Helical; Name=5By similarityAdd BLAST26
Topological domaini220 – 339CytoplasmicBy similarityAdd BLAST120
Transmembranei340 – 361Helical; Name=6By similarityAdd BLAST22
Topological domaini362 – 372ExtracellularBy similarityAdd BLAST11
Transmembranei373 – 397Helical; Name=7By similarityAdd BLAST25
Topological domaini398 – 416CytoplasmicBy similarityAdd BLAST19

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000689241 – 4165-hydroxytryptamine receptor 1A-betaAdd BLAST416

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi5N-linked (GlcNAc...)Sequence analysis1
Glycosylationi6N-linked (GlcNAc...)Sequence analysis1
Glycosylationi18N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi106 ↔ 189PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliO42384.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni109 – 118Agonist bindingBy similarity10
Regioni352 – 356Agonist bindingBy similarity5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi130 – 132DRY motif; important for ligand-induced conformation changesBy similarity3
Motifi390 – 394NPxxY motif; important for ligand-induced conformation changes and signalingBy similarity5

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family. 5-hydroxytryptamine receptor subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

InParanoidiO42384.
KOiK04153.

Family and domain databases

InterProiIPR000610. 5HT1A_rcpt.
IPR002231. 5HT_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00512. 5HT1ARECEPTR.
PR01101. 5HTRECEPTOR.
PR00237. GPCRRHODOPSN.
SMARTiSM01381. 7TM_GPCR_Srsx. 1 hit.
[Graphical view]
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O42384-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGTNNTTGW THFDSTSNRT SKSFDEEVKL SYQVVTSFLL GALILCSIFG
60 70 80 90 100
NACVVAAIAL ERSLQNVANY LIGSLAVTDL MVSVLVLPMA ALYQVLNRWT
110 120 130 140 150
LGQIPCDIFI SLDMLCCTSS ILHLCVIALD RYWAITEPID YMKKRTPRRA
160 170 180 190 200
AVLISVTWLV GFSISIPPML IMRSQPSSMA EDRANSKQCK ITQDPWYTIY
210 220 230 240 250
STFGAFYIPL TLMLVLYGRI FKAARFRIRR TVRKTEKKKV SDTCLALSPA
260 270 280 290 300
MFHRKTPGDA HGKSWKRSVE PRPLPNVNGA VKHAGEGESL DIIEVQSNSR
310 320 330 340 350
CNLPLPNTPG TVPLFENRHE KATETKRKIA LARERKTVKT LGIIMGTFIL
360 370 380 390 400
CWLPFFIVAL VMPFCQESCF MPHWLKDVIN WLGYSNSLLN PIIYAYFNKD
410
FQSAFKKIIK CHFCRA
Length:416
Mass (Da):47,031
Last modified:January 1, 1998 - v1
Checksum:i9B4CC415BEC750FE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95937 Genomic DNA. Translation: CAA65176.1.
RefSeqiXP_003977344.1. XM_003977295.1.

Genome annotation databases

GeneIDi101072291.
KEGGitru:101072291.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95937 Genomic DNA. Translation: CAA65176.1.
RefSeqiXP_003977344.1. XM_003977295.1.

3D structure databases

ProteinModelPortaliO42384.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

GPCRDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi101072291.
KEGGitru:101072291.

Organism-specific databases

CTDi101072291.

Phylogenomic databases

InParanoidiO42384.
KOiK04153.

Family and domain databases

InterProiIPR000610. 5HT1A_rcpt.
IPR002231. 5HT_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00512. 5HT1ARECEPTR.
PR01101. 5HTRECEPTOR.
PR00237. GPCRRHODOPSN.
SMARTiSM01381. 7TM_GPCR_Srsx. 1 hit.
[Graphical view]
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry namei5H1AB_TAKRU
AccessioniPrimary (citable) accession number: O42384
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.