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Protein

5-hydroxytryptamine receptor 1B

Gene

HTR1B

Organism
Gorilla gorilla gorilla (Western lowland gorilla)
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 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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei355Important for species-specific agonist sensitivityBy similarity1

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 1B
Short name:
5-HT-1B
Short name:
5-HT1B
Alternative name(s):
Serotonin receptor 1B
Gene namesi
Name:HTR1B
OrganismiGorilla gorilla gorilla (Western lowland gorilla)
Taxonomic identifieri9595 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeGorilla
Proteomesi
  • UP000001519 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 49ExtracellularBy similarityAdd BLAST49
Transmembranei50 – 75Helical; Name=1By similarityAdd BLAST26
Topological domaini76 – 84CytoplasmicBy similarity9
Transmembranei85 – 110Helical; Name=2By similarityAdd BLAST26
Topological domaini111 – 123ExtracellularBy similarityAdd BLAST13
Transmembranei124 – 145Helical; Name=3By similarityAdd BLAST22
Topological domaini146 – 165CytoplasmicBy similarityAdd BLAST20
Transmembranei166 – 187Helical; Name=4By similarityAdd BLAST22
Topological domaini188 – 205ExtracellularBy similarityAdd BLAST18
Transmembranei206 – 228Helical; Name=5By similarityAdd BLAST23
Topological domaini229 – 315CytoplasmicBy similarityAdd BLAST87
Transmembranei316 – 336Helical; Name=6By similarityAdd BLAST21
Topological domaini337 – 349ExtracellularBy similarityAdd BLAST13
Transmembranei350 – 371Helical; Name=7By similarityAdd BLAST22
Topological domaini372 – 390CytoplasmicBy similarityAdd BLAST19

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2304408.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000689151 – 3905-hydroxytryptamine receptor 1BAdd BLAST390

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi24N-linked (GlcNAc...)Sequence analysis1
Glycosylationi32N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi122 ↔ 199PROSITE-ProRule annotation
Lipidationi388S-palmitoyl cysteineSequence analysis1

Post-translational modificationi

Phosphorylated.By similarity
Palmitoylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Interactioni

Subunit structurei

Homodimer. Heterodimer with HTR1D (By similarity).By similarity

Chemistry databases

BindingDBiQ9N2B7.

Structurei

3D structure databases

ProteinModelPortaliQ9N2B7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni125 – 134Agonist bindingBy similarity10
Regioni327 – 331Agonist bindingBy similarity5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi146 – 148DRY motif; important for ligand-induced conformation changes and signalingBy similarity3
Motifi365 – 369NPxxY motif; important for ligand-induced conformation changes and signalingBy similarity5

Domaini

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

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG106962.
InParanoidiQ9N2B7.

Family and domain databases

InterProiIPR002147. 5HT1B_rcpt.
IPR002231. 5HT_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24247:SF16. PTHR24247:SF16. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00513. 5HT1BRECEPTR.
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.

Q9N2B7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEPGAQCAP PXPAGSETWV PQANLSSAPS QNCSAKDYIY QDSIALPWKV
60 70 80 90 100
LLVMLLALIT LATTLSNAFV IATVYRTRKL HTPANYLIAS LAVTDLLVSI
110 120 130 140 150
LVMPISTMYT VTGRWTLGQV VCDFWLSSDI TCCTASILHL CVIALDRYWA
160 170 180 190 200
ITDAVEYSAK RTPKRAAVMI ALVWVFSISI SLPPFFWRQA KAEEEVSECV
210 220 230 240 250
VNTDHILYTV YSTVGAFYFP TLLLIALYGR IYVEARSRIL KQTPNRTGKR
260 270 280 290 300
LTRAQLITDS PGSTSSVTSI NSRVPDVPSE SGSPVYVNQV KVRVSDALLE
310 320 330 340 350
KKKLMAARER KATKTLGIIL GAFIVCWLPF FIISLVMPIC KDACWFHLAI
360 370 380 390
FDFFTWLGYL NSLINPIIYT MSNEDFKQAF HKLIRFKCTS
Length:390
Mass (Da):43,566
Last modified:October 1, 2000 - v1
Checksum:i37D54B95E3277FC3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB041372 Genomic DNA. Translation: BAA94457.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB041372 Genomic DNA. Translation: BAA94457.1.

3D structure databases

ProteinModelPortaliQ9N2B7.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiQ9N2B7.
ChEMBLiCHEMBL2304408.

Protein family/group databases

GPCRDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG106962.
InParanoidiQ9N2B7.

Family and domain databases

InterProiIPR002147. 5HT1B_rcpt.
IPR002231. 5HT_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24247:SF16. PTHR24247:SF16. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00513. 5HT1BRECEPTR.
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 namei5HT1B_GORGO
AccessioniPrimary (citable) accession number: Q9N2B7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: October 1, 2000
Last modified: October 5, 2016
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

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.