Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

5-hydroxytryptamine receptor 3A

Gene

Htr3a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-gated ion channel, which when activated causes fast, depolarizing responses in neurons. It is a cation-specific, but otherwise relatively nonselective, ion channel.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
5-hydroxytryptamine receptor 3A
Short name:
5-HT3-A
Short name:
5-HT3A
Alternative name(s):
5-hydroxytryptamine receptor 3
Short name:
5-HT-3
Short name:
5-HT3R
Serotonin receptor 3A
Serotonin-gated ion channel receptor
Gene namesi
Name:Htr3a
Synonyms:5ht3, Htr3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:96282. Htr3a.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini24 – 245ExtracellularSequence analysisAdd BLAST222
Transmembranei246 – 272Helical; Name=1Sequence analysisAdd BLAST27
Topological domaini273 – 277CytoplasmicSequence analysis5
Transmembranei278 – 296Helical; Name=2Sequence analysisAdd BLAST19
Topological domaini297 – 305ExtracellularSequence analysis9
Transmembranei306 – 324Helical; Name=3Sequence analysisAdd BLAST19
Topological domaini325 – 464CytoplasmicSequence analysisAdd BLAST140
Transmembranei465 – 484Helical; Name=4Sequence analysisAdd BLAST20
Topological domaini485 – 487ExtracellularSequence analysis3

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4972.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000000040924 – 4875-hydroxytryptamine receptor 3AAdd BLAST464

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi108N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi161 ↔ 175By similarity
Glycosylationi174N-linked (GlcNAc...)Sequence analysis1
Glycosylationi190N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP23979.
PaxDbiP23979.
PRIDEiP23979.

PTM databases

PhosphoSitePlusiP23979.
SwissPalmiP23979.

Expressioni

Tissue specificityi

Brain, spinal cord, and heart.

Gene expression databases

CleanExiMM_HTR3A.

Interactioni

Subunit structurei

Forms pentahomomeric complex as well as pentaheteromeric complex with HTR3B; homomeric complex is functional but exhibits low conductance with modified voltage dependence, and decreased agonist and antagonist affinity. Interacts with RIC3 (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-48769N.
STRINGi10090.ENSMUSP00000003826.

Chemistry databases

BindingDBiP23979.

Structurei

Secondary structure

1487
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi38 – 46Combined sources9
Beta strandi63 – 78Combined sources16
Turni79 – 82Combined sources4
Beta strandi83 – 95Combined sources13
Beta strandi106 – 108Combined sources3
Beta strandi111 – 115Combined sources5
Helixi116 – 118Combined sources3
Beta strandi124 – 126Combined sources3
Beta strandi129 – 131Combined sources3
Beta strandi140 – 144Combined sources5
Beta strandi148 – 160Combined sources13
Beta strandi166 – 168Combined sources3
Beta strandi172 – 183Combined sources12
Turni186 – 188Combined sources3
Beta strandi189 – 195Combined sources7
Helixi197 – 202Combined sources6
Beta strandi210 – 225Combined sources16
Beta strandi227 – 230Combined sources4
Beta strandi233 – 244Combined sources12
Helixi248 – 268Combined sources21
Turni272 – 274Combined sources3
Helixi276 – 294Combined sources19
Helixi310 – 332Combined sources23
Helixi343 – 349Combined sources7
Helixi352 – 358Combined sources7
Helixi428 – 482Combined sources55

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4PIRX-ray3.50A/B/C/D/E32-485[»]
ProteinModelPortaliP23979.
SMRiP23979.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni423 – 459HA-stretchAdd BLAST37

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3645. Eukaryota.
ENOG410XQGR. LUCA.
HOGENOMiHOG000241519.
HOVERGENiHBG106638.
InParanoidiP23979.
KOiK04819.
PhylomeDBiP23979.

Family and domain databases

Gene3Di1.20.120.370. 2 hits.
2.70.170.10. 1 hit.
InterProiIPR008132. 5HT3_rcpt.
IPR008133. 5HT3_rcpt_A.
IPR027361. Acetylcholine_rcpt_TM.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
[Graphical view]
PANTHERiPTHR18945. PTHR18945. 2 hits.
PfamiPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view]
PRINTSiPR01709. 5HT3ARECEPTR.
PR01708. 5HT3RECEPTOR.
PR00252. NRIONCHANNEL.
SUPFAMiSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.
TIGRFAMsiTIGR00860. LIC. 1 hit.
PROSITEiPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 5-HT3R-A (identifier: P23979-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRLCIPQVLL ALFLSMLTAP GEGSRRRATQ EDTTQPALLR LSDHLLANYK
60 70 80 90 100
KGVRPVRDWR KPTTVSIDVI MYAILNVDEK NQVLTTYIWY RQYWTDEFLQ
110 120 130 140 150
WTPEDFDNVT KLSIPTDSIW VPDILINEFV DVGKSPNIPY VYVHHRGEVQ
160 170 180 190 200
NYKPLQLVTA CSLDIYNFPF DVQNCSLTFT SWLHTIQDIN ITLWRSPEEV
210 220 230 240 250
RSDKSIFINQ GEWELLEVFP QFKEFSIDIS NSYAEMKFYV IIRRRPLFYA
260 270 280 290 300
VSLLLPSIFL MVVDIVGFCL PPDSGERVSF KITLLLGYSV FLIIVSDTLP
310 320 330 340 350
ATIGTPLIGV YFVVCMALLV ISLAETIFIV RLVHKQDLQR PVPDWLRHLV
360 370 380 390 400
LDRIAWILCL GEQPMAHRPP ATFQANKTDD CSGSDLLPAM GNHCSHVGGP
410 420 430 440 450
QDLEKTPRGR GSPLPPPREA SLAVRGLLQE LSSIRHFLEK RDEMREVARD
460 470 480
WLRVGYVLDR LLFRIYLLAV LAYSITLVTL WSIWHYS
Length:487
Mass (Da):56,056
Last modified:March 1, 1992 - v1
Checksum:iD0148867C8536D66
GO
Isoform 5-HT3R-AS (identifier: P23979-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     383-388: Missing.

Show »
Length:481
Mass (Da):55,474
Checksum:i7A9B7B5C38FEC909
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti31E → AR in CAA51089 (PubMed:7683998).Curated1
Sequence conflicti31E → AR in CAA55870 (PubMed:7854052).Curated1
Sequence conflicti31E → AR in CAA55871 (PubMed:7854052).Curated1
Sequence conflicti74I → V in CAA51089 (PubMed:7683998).Curated1
Sequence conflicti302T → TA in CAA51089 (PubMed:7683998).Curated1
Sequence conflicti302T → TA in CAA55870 (PubMed:7854052).Curated1
Sequence conflicti302T → TA in CAA55871 (PubMed:7854052).Curated1
Sequence conflicti384S → SS in CAA80453 (PubMed:8112471).Curated1
Sequence conflicti393H → T in CAA55870 (PubMed:7854052).Curated1
Sequence conflicti393H → T in CAA55871 (PubMed:7854052).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000079383 – 388Missing in isoform 5-HT3R-AS. Curated6

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74425 mRNA. Translation: AAA37124.1.
Z22772, Z22773 Genomic DNA. Translation: CAA80453.1.
X72395 mRNA. Translation: CAA51089.1.
X79283 Genomic DNA. Translation: CAA55870.1.
X79283 Genomic DNA. Translation: CAA55871.1.
PIRiS41757.
RefSeqiNP_038589.2. NM_013561.2.
UniGeneiMm.4831.

Genome annotation databases

GeneIDi15561.
KEGGimmu:15561.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74425 mRNA. Translation: AAA37124.1.
Z22772, Z22773 Genomic DNA. Translation: CAA80453.1.
X72395 mRNA. Translation: CAA51089.1.
X79283 Genomic DNA. Translation: CAA55870.1.
X79283 Genomic DNA. Translation: CAA55871.1.
PIRiS41757.
RefSeqiNP_038589.2. NM_013561.2.
UniGeneiMm.4831.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4PIRX-ray3.50A/B/C/D/E32-485[»]
ProteinModelPortaliP23979.
SMRiP23979.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48769N.
STRINGi10090.ENSMUSP00000003826.

Chemistry databases

BindingDBiP23979.
ChEMBLiCHEMBL4972.

PTM databases

PhosphoSitePlusiP23979.
SwissPalmiP23979.

Proteomic databases

MaxQBiP23979.
PaxDbiP23979.
PRIDEiP23979.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi15561.
KEGGimmu:15561.

Organism-specific databases

CTDi3359.
MGIiMGI:96282. Htr3a.

Phylogenomic databases

eggNOGiKOG3645. Eukaryota.
ENOG410XQGR. LUCA.
HOGENOMiHOG000241519.
HOVERGENiHBG106638.
InParanoidiP23979.
KOiK04819.
PhylomeDBiP23979.

Miscellaneous databases

PROiP23979.
SOURCEiSearch...

Gene expression databases

CleanExiMM_HTR3A.

Family and domain databases

Gene3Di1.20.120.370. 2 hits.
2.70.170.10. 1 hit.
InterProiIPR008132. 5HT3_rcpt.
IPR008133. 5HT3_rcpt_A.
IPR027361. Acetylcholine_rcpt_TM.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
[Graphical view]
PANTHERiPTHR18945. PTHR18945. 2 hits.
PfamiPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view]
PRINTSiPR01709. 5HT3ARECEPTR.
PR01708. 5HT3RECEPTOR.
PR00252. NRIONCHANNEL.
SUPFAMiSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.
TIGRFAMsiTIGR00860. LIC. 1 hit.
PROSITEiPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry namei5HT3A_MOUSE
AccessioniPrimary (citable) accession number: P23979
Secondary accession number(s): Q61225, Q61226
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: November 2, 2016
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The HA-stretch region of HTR3A seems to be responsible for the low conductance of HTR3A homomers compared to that of HTR3A/HTR3B heteromers.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.