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P28564 (5HT1B_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
5-hydroxytryptamine receptor 1B

Short name=5-HT-1B
Short name=5-HT1B
Alternative name(s):
Serotonin receptor 1B
Gene names
Name:Htr1b
Synonyms:5ht1b
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length386 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids 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. Signaling inhibits adenylate cyclase activity. Arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Regulates the release of 5-hydroxytryptamine, dopamine and acetylcholine in the brain, and thereby affects neural activity, nociceptive processing, pain perception, mood and behavior. Besides, plays a role in vasoconstriction of cerebral arteries. Ref.1 Ref.2

Subunit structure

Homodimer. Heterodimer with HTR1D By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.1 Ref.2.

Domain

Ligands are bound in a hydrophobic pocket formed by the transmembrane helices By similarity.

Post-translational modification

Phosphorylated By similarity.

Palmitoylated By similarity.

Miscellaneous

A residue in the 7th transmembrane region ('Thr-355' in human, Asn-351 in mouse and rat) is important for species-specific sensitivity to various agonists By similarity.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
   Biological processBehavior
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor internalization

Inferred from electronic annotation. Source: Ensembl

adenylate cyclase-inhibiting serotonin receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

bone remodeling

Inferred from electronic annotation. Source: Ensembl

cellular response to alkaloid

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to drug

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to temperature stimulus

Inferred from electronic annotation. Source: Ensembl

drinking behavior

Inferred from mutant phenotype PubMed 16839853. Source: RGD

feeding behavior

Inferred from mutant phenotype PubMed 12373419. Source: RGD

negative regulation of cAMP biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of serotonin secretion

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of synaptic transmission, GABAergic

Inferred from mutant phenotype PubMed 17229091. Source: RGD

negative regulation of synaptic transmission, glutamatergic

Inferred from mutant phenotype PubMed 17392733. Source: RGD

protein kinase C-activating G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of behavior

Inferred from electronic annotation. Source: InterPro

regulation of dopamine secretion

Inferred from mutant phenotype PubMed 16885935. Source: RGD

response to cocaine

Inferred from direct assay PubMed 17509084. Source: RGD

response to ethanol

Inferred from mutant phenotype PubMed 16212943. Source: RGD

response to mineralocorticoid

Inferred from expression pattern PubMed 11882579. Source: RGD

synaptic transmission

Inferred from direct assay PubMed 15328035. Source: RGD

vasoconstriction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 15328035. Source: RGD

   Molecular_functiondrug binding

Inferred from direct assay PubMed 16546225. Source: RGD

serotonin binding

Inferred from direct assay PubMed 2947981. Source: RGD

serotonin receptor activity

Inferred from direct assay PubMed 15328035. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3863865-hydroxytryptamine receptor 1B
PRO_0000068921

Regions

Topological domain1 – 4545Extracellular By similarity
Transmembrane46 – 7126Helical; Name=1; By similarity
Topological domain72 – 809Cytoplasmic By similarity
Transmembrane81 – 10626Helical; Name=2; By similarity
Topological domain107 – 11913Extracellular By similarity
Transmembrane120 – 14122Helical; Name=3; By similarity
Topological domain142 – 16120Cytoplasmic By similarity
Transmembrane162 – 18322Helical; Name=4; By similarity
Topological domain184 – 20118Extracellular By similarity
Transmembrane202 – 22423Helical; Name=5; By similarity
Topological domain225 – 31187Cytoplasmic By similarity
Transmembrane312 – 33221Helical; Name=6; By similarity
Topological domain333 – 34513Extracellular By similarity
Transmembrane346 – 36722Helical; Name=7; By similarity
Topological domain368 – 38619Cytoplasmic By similarity
Region121 – 13010Agonist binding By similarity
Region323 – 3275Agonist binding By similarity
Motif142 – 1443DRY motif; important for ligand-induced conformation changes and signaling By similarity
Motif361 – 3655NPxxY motif; important for ligand-induced conformation changes and signaling By similarity

Sites

Site3511Important for species-specific agonist sensitivity By similarity

Amino acid modifications

Lipidation3841S-palmitoyl cysteine Potential
Glycosylation241N-linked (GlcNAc...) Potential
Glycosylation281N-linked (GlcNAc...) Potential
Disulfide bond118 ↔ 195 By similarity

Sequences

Sequence LengthMass (Da)Tools
P28564 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 4F4E9AC1C9AED214

FASTA38643,163
        10         20         30         40         50         60 
MEEQGIQCAP PPPATSQTGV PLANLSHNCS ADDYIYQDSI ALPWKVLLVA LLALITLATT 

        70         80         90        100        110        120 
LSNAFVIATV YRTRKLHTPA NYLIASLAVT DLLVSILVMP ISTMYTVTGR WTLGQVVCDF 

       130        140        150        160        170        180 
WLSSDITCCT ASIMHLCVIA LDRYWAITDA VDYSAKRTPK RAAIMIVLVW VFSISISLPP 

       190        200        210        220        230        240 
FFWRQAKAEE EVLDCFVNTD HVLYTVYSTV GAFYLPTLLL IALYGRIYVE ARSRILKQTP 

       250        260        270        280        290        300 
NKTGKRLTRA QLITDSPGST SSVTSINSRV PEVPSESGSP VYVNQVKVRV SDALLEKKKL 

       310        320        330        340        350        360 
MAARERKATK TLGIILGAFI VCWLPFFIIS LVMPICKDAC WFHMAIFDFF NWLGYLNSLI 

       370        380 
NPIIYTMSNE DFKQAFHKLI RFKCTG 

« Hide

References

[1]"Distinct 5-HT1B and 5-HT1D serotonin receptors in rat: structural and pharmacological comparison of the two cloned receptors."
Hamblin M.W., McGuffin R.W., Metcalf M.A., Dorsa D.M., Merchant K.M.
Mol. Cell. Neurosci. 3:578-587(1992)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
[2]"Molecular cloning and characterization of a rat brain cDNA encoding a 5-hydroxytryptamine1B receptor."
Voigt M.M., Laurie D.J., Seeburg P.H., Bach A.
EMBO J. 10:4017-4023(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M89954 Genomic DNA. Translation: AAA40613.1.
X62944 mRNA. Translation: CAA44716.1.
PIRS18637.
RefSeqNP_071561.1. NM_022225.1.
UniGeneRn.138109.

3D structure databases

ProteinModelPortalP28564.
SMRP28564. Positions 130-161.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000017411.

Chemistry

BindingDBP28564.
ChEMBLCHEMBL2095159.
GuidetoPHARMACOLOGY2.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP28564.

Proteomic databases

PRIDEP28564.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000017411; ENSRNOP00000017411; ENSRNOG00000013042.
GeneID25075.
KEGGrno:25075.
UCSCRGD:2846. rat.

Organism-specific databases

CTD3351.
RGD2846. Htr1b.

Phylogenomic databases

eggNOGNOG249628.
GeneTreeENSGT00750000117301.
HOGENOMHOG000239242.
HOVERGENHBG106962.
InParanoidP28564.
KOK04153.
OMAIALPWKV.
OrthoDBEOG7NCV3Q.
PhylomeDBP28564.
TreeFamTF316350.

Gene expression databases

GenevestigatorP28564.

Family and domain databases

Gene3D1.20.1070.10. 2 hits.
InterProIPR002147. 5HT1B_rcpt.
IPR002231. 5HT_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERPTHR24247:SF16. PTHR24247:SF16. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00513. 5HT1BRECEPTR.
PR01101. 5HTRECEPTOR.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio605318.
PROP28564.

Entry information

Entry name5HT1B_RAT
AccessionPrimary (citable) accession number: P28564
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: April 16, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries