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P28334 (5HT1B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 Ref.3 Ref.4 Ref.5 Ref.6

Subunit structure

Homodimer. Heterodimer with HTR1D By similarity.

Subcellular location

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

Tissue specificity

Predominantly expressed in striatum and Purkinje cells. Ref.1

Domain

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

Post-translational modification

Phosphorylated By similarity.

Palmitoylated By similarity.

Disruption phenotype

Mutant male mice display increased aggressivity towards intruders. Treatment with a Htr1b agonist does not trigger increased locomotor behavior in mutant mice, contrary to what is observed with wild-type mice. Treatment with a Htr1b agonist does not inhibit 5-hydroxytryptamine release in the frontal cortex and hippocampus of mutant mice, contrary to what is observed with wild-type mice. Likewise, Htr1b agonists do not inhibit dopamine and acetylcholine release in brains from mutant mice. Ref.2 Ref.3 Ref.4 Ref.5 Ref.6

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 direct assay PubMed 17325130. Source: UniProtKB

adenylate cyclase-inhibiting serotonin receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

bone remodeling

Inferred from genetic interaction PubMed 19041748. Source: MGI

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 direct assay PubMed 17325130. Source: UniProtKB

feeding behavior

Inferred from electronic annotation. Source: InterPro

negative regulation of serotonin secretion

Inferred from mutant phenotype Ref.4. Source: UniProtKB

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

Inferred from mutant phenotype PubMed 17325130. Source: UniProtKB

regulation of behavior

Inferred from electronic annotation. Source: InterPro

response to drug

Inferred from direct assay PubMed 17325130. Source: UniProtKB

synaptic transmission

Inferred from electronic annotation. Source: InterPro

vasoconstriction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 17325130. Source: UniProtKB

integral component of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 17325130. Source: UniProtKB

   Molecular_functiondrug binding

Inferred from direct assay PubMed 17325130. Source: UniProtKB

serotonin binding

Inferred from direct assay PubMed 17325130. Source: UniProtKB

serotonin receptor activity

Inferred from direct assay PubMed 17325130. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3863865-hydroxytryptamine receptor 1B
PRO_0000068917

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
P28334 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 58F70FBEA770C0B3

FASTA38643,079
        10         20         30         40         50         60 
MEEQGIQCAP PPPAASQTGV PLTNLSHNCS ADGYIYQDSI ALPWKVLLVA LLALITLATT 

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

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

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

       250        260        270        280        290        300 
NKTGKRLTRA QLITDSPGST SSVTSINSRA PDVPSESGSP VYVNQVKVRV SDALLEKKKL 

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

       370        380 
NPIIYTMSNE DFKQAFHKLI RFKCAG 

« Hide

References

[1]"Mouse 5HT1B serotonin receptor: cloning, functional expression, and localization in motor control centers."
Maroteaux L., Saudou F., Amlaiky N., Boschert U., Plassat J.-L., Hen R.
Proc. Natl. Acad. Sci. U.S.A. 89:3020-3024(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"Enhanced aggressive behavior in mice lacking 5-HT1B receptor."
Saudou F., Amara D.A., Dierich A., LeMeur M., Ramboz S., Segu L., Buhot M.C., Hen R.
Science 265:1875-1878(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[3]"Regulation of [3H]5-HT release in raphe, frontal cortex and hippocampus of 5-HT1B knock-out mice."
Pineyro G., Castanon N., Hen R., Blier P.
NeuroReport 7:353-359(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[4]"Regulation of serotonin release in the frontal cortex and ventral hippocampus of homozygous mice lacking 5-HT1B receptors: in vivo microdialysis studies."
Trillat A.C., Malagie I., Scearce K., Pons D., Anmella M.C., Jacquot C., Hen R., Gardier A.M.
J. Neurochem. 69:2019-2025(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[5]"5-HT1B receptors modulate release of [3H]dopamine from rat striatal synaptosomes: further evidence using 5-HT moduline, polyclonal 5-HT1B receptor antibodies and 5-HT1B receptor knock-out mice."
Sarhan H., Grimaldi B., Hen R., Fillion G.
Naunyn Schmiedebergs Arch. Pharmacol. 361:12-18(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[6]"Presynaptic serotonergic modulation of 5-HT and acetylcholine release in the hippocampus and the cortex of 5-HT1B-receptor knockout mice."
Rutz S., Riegert C., Rothmaier A.K., Buhot M.C., Cassel J.C., Jackisch R.
Brain Res. Bull. 70:81-93(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z11597 Genomic DNA. Translation: CAA77678.1.
M85151 Genomic DNA. Translation: AAA83221.1.
PIRA42688.
RefSeqNP_034612.1. NM_010482.1.
UniGeneMm.445308.

3D structure databases

ProteinModelPortalP28334.
SMRP28334. Positions 34-383.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000050898.

Chemistry

BindingDBP28334.
GuidetoPHARMACOLOGY2.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP28334.

Proteomic databases

PRIDEP28334.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000051005; ENSMUSP00000050898; ENSMUSG00000049511.
ENSMUST00000183482; ENSMUSP00000139389; ENSMUSG00000049511.
GeneID15551.
KEGGmmu:15551.
UCSCuc009qvl.1. mouse.

Organism-specific databases

CTD3351.
MGIMGI:96274. Htr1b.

Phylogenomic databases

eggNOGNOG249628.
HOGENOMHOG000239242.
HOVERGENHBG106962.
InParanoidP28334.
KOK04153.
OMAIALPWKV.
OrthoDBEOG7NCV3Q.
PhylomeDBP28334.
TreeFamTF316350.

Gene expression databases

BgeeP28334.
CleanExMM_HTR1B.
GenevestigatorP28334.

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

NextBio288484.
PROP28334.
SOURCESearch...

Entry information

Entry name5HT1B_MOUSE
AccessionPrimary (citable) accession number: P28334
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: April 16, 2014
This is version 110 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries