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Protein

Glycine receptor subunit alpha-3

Gene

Glra3

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

Functioni

Glycine receptors are ligand-gated chloride channels. Channel opening is triggered by extracellular glycine (PubMed:15131310, PubMed:20978350). Channel characteristics depend on the subunit composition; heteropentameric channels display faster channel closure (By similarity). Plays an important role in the down-regulation of neuronal excitability. Contributes to the generation of inhibitory postsynaptic currents (PubMed:15131310). Contributes to increased pain perception in response to increased prostaglandin E2 levels (PubMed:15131310). Plays a role in the regulation of breathing rhythm, especially of the duration of the postinspiratory phase (PubMed:20978350). Plays a role in cellular responses to ethanol (By similarity).By similarity2 Publications

Enzyme regulationi

Inhibited by prostaglandin E2, probably via PKA-mediated phosphorylation at Ser-379 (PubMed:15131310).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi225ZincBy similarity1
Metal bindingi227ZincBy similarity1
Metal bindingi248ZincBy similarity1
Sitei294Important for obstruction of the ion pore in the closed conformationBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chloride channel, Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Keywords - Ligandi

Chloride, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Glycine receptor subunit alpha-3
Gene namesi
Name:Glra3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:95749. Glra3.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini34 – 255ExtracellularBy similarityAdd BLAST222
Transmembranei256 – 277Helical; Name=1By similarityAdd BLAST22
Topological domaini278 – 282CytoplasmicBy similarity5
Transmembranei283 – 303Helical; Name=2By similarityAdd BLAST21
Topological domaini304 – 314ExtracellularBy similarityAdd BLAST11
Transmembranei315 – 335Helical; Name=3By similarityAdd BLAST21
Topological domaini336 – 430CytoplasmicBy similarityAdd BLAST95
Transmembranei431 – 451Helical; Name=4By similarityAdd BLAST21
Topological domaini452 – 464ExtracellularBy similarityAdd BLAST13

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • dendrite Source: UniProtKB-SubCell
  • GABA-ergic synapse Source: MGI
  • glutamatergic synapse Source: MGI
  • glycine-gated chloride channel complex Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • perikaryon Source: UniProtKB-SubCell
  • postsynaptic membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Disruption phenotypei

Mutant mice are born at the expected Mendelian rate, appear normal and are fertile. They do not display notable alterations in motor coordination and startle response, or other neuromotor defects. Glycinergic postsynaptic inhibitory currents in spinal cord appear unchanged, but are not inhibited by prostaglandin E2, contrary to what is observed with wild-type. Basal nociception is unchanged, but contrary to wild-type, mutant mice do not display increased sensitivity to pain after prostaglandin E2 injection. Likewise, they show a more rapid decrease of the increased pain sensitivity caused by agents that cause local inflammation, such as subcutaneous zymosan injection (PubMed:15131310). Mutant mice display altered phrenic nerve activity, resulting in an irregular breathing rhythm that affects especially the duration of the postinspiratory phase. Contrary to wild-type, their respiratory rhythm is not accelerated by serotonin (PubMed:20978350).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 33Sequence analysisAdd BLAST33
ChainiPRO_000000042034 – 464Glycine receptor subunit alpha-3Add BLAST431

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi71N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi171 ↔ 185By similarity
Disulfide bondi231 ↔ 242By similarity
Modified residuei370PhosphoserineCombined sources1
Modified residuei379Phosphoserine; by PKA1 Publication1

Post-translational modificationi

Phosphorylated by PKA; this causes down-regulation of channel activity. Dephosphorylated in response to activation of HTR1A signaling; this increases channel activity (PubMed:20978350).By similarity1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ91XP5.
PRIDEiQ91XP5.

PTM databases

iPTMnetiQ91XP5.
PhosphoSitePlusiQ91XP5.

Expressioni

Tissue specificityi

Detected in brainstem, also in neurons that control rhythmic breathing (PubMed:20978350). Detected in superficial laminae of the dorsal horn of the thoracic spinal cord (PubMed:15131310). Detected in dentate gyrus in hippocampus, especially in stratum granulare (PubMed:19723286). Detected in the inner plexiform layer in the retina (at protein level) (PubMed:12975813). Detected in midbrain, thalamus, brain cortex, hippocampus, and at lower levels in cerebellum (PubMed:19723286).4 Publications

Gene expression databases

BgeeiENSMUSG00000038257.
CleanExiMM_GLRA3.

Interactioni

Subunit structurei

Homopentamer (in vitro) (By similarity). Heteropentamer composed of GLRA3 and GLRB. Both homopentamers and heteropentamers form functional ion channels, but their characteristics are subtly different (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000000275.

Structurei

3D structure databases

ProteinModelPortaliQ91XP5.
SMRiQ91XP5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni235 – 240Strychnine-bindingBy similarity6

Domaini

The N-terminal domain carries structural determinants essential for agonist and antagonist binding. The channel pore is formed by pentameric assembly of the second transmembrane domain from all five subunits. The cytoplasmic loop is an important determinant of channel inactivation kinetics.By similarity

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3643. Eukaryota.
ENOG410XPWH. LUCA.
HOGENOMiHOG000231336.
HOVERGENiHBG051707.
InParanoidiQ91XP5.
KOiK05195.
PhylomeDBiQ91XP5.

Family and domain databases

Gene3Di2.70.170.10. 1 hit.
InterProiIPR006028. GABAA/Glycine_rcpt.
IPR008127. Glycine_rcpt_A.
IPR008130. Glycine_rcpt_A3.
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]
PRINTSiPR00253. GABAARECEPTR.
PR01673. GLYRALPHA.
PR01676. GLYRALPHA3.
PR00252. NRIONCHANNEL.
SUPFAMiSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.
TIGRFAMsiTIGR00860. LIC. 1 hit.
PROSITEiPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q91XP5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAHVRHFRTL VSGFYFWEAA LLLSLVATKE TNSARSRSAP MSPSDFLDKL
60 70 80 90 100
MGRTSGYDAR IRPNFKGPPV NVTCNIFINS FGSIAETTMD YRVNIFLRQK
110 120 130 140 150
WNDPRLAYSE YPDDSLDLDP SMLDSIWKPD LFFANEKGAN FHEVTTDNKL
160 170 180 190 200
LRIFKNGNVL YSIRLTLTLS CPMDLKNFPM DVQTCIMQLE SFGYTMNDLI
210 220 230 240 250
FEWQDEAPVQ VAEGLTLPQF LLKEEKDLRY CTKHYNTGKF TCIEVRFHLE
260 270 280 290 300
RQMGYYLIQM YIPSLLIVIL SWVSFWINMD AAPARVALGI TTVLTMTTQS
310 320 330 340 350
SGSRASLPKV SYVKAIDIWM AVCLLFVFSA LLEYAAVNFV SRQHKELLRF
360 370 380 390 400
RRKRKNKTEA FALEKFYRFS DTDDEVRESR FSFTAYGMGP CLQAKDGVVP
410 420 430 440 450
KGPNHAVQVM PKSPDEMRKV FIDRAKKIDT ISRACFPLAF LIFNIFYWVI
460
YKILRHEDIH QQQD
Length:464
Mass (Da):53,709
Last modified:May 24, 2005 - v2
Checksum:i0963FD4A3727AA1D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti110Missing in AAK51962 (Ref. 1) Curated1
Sequence conflicti293V → D in AAK51962 (Ref. 1) Curated1
Sequence conflicti461Q → H in AAK51962 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF362764 mRNA. Translation: AAK51962.1.
AY230204 mRNA. Translation: AAP22967.1.
RefSeqiNP_536686.2. NM_080438.2.
UniGeneiMm.307061.

Genome annotation databases

GeneIDi110304.
KEGGimmu:110304.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF362764 mRNA. Translation: AAK51962.1.
AY230204 mRNA. Translation: AAP22967.1.
RefSeqiNP_536686.2. NM_080438.2.
UniGeneiMm.307061.

3D structure databases

ProteinModelPortaliQ91XP5.
SMRiQ91XP5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000000275.

PTM databases

iPTMnetiQ91XP5.
PhosphoSitePlusiQ91XP5.

Proteomic databases

PaxDbiQ91XP5.
PRIDEiQ91XP5.

Protocols and materials databases

DNASUi110304.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi110304.
KEGGimmu:110304.

Organism-specific databases

CTDi8001.
MGIiMGI:95749. Glra3.

Phylogenomic databases

eggNOGiKOG3643. Eukaryota.
ENOG410XPWH. LUCA.
HOGENOMiHOG000231336.
HOVERGENiHBG051707.
InParanoidiQ91XP5.
KOiK05195.
PhylomeDBiQ91XP5.

Miscellaneous databases

PROiQ91XP5.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000038257.
CleanExiMM_GLRA3.

Family and domain databases

Gene3Di2.70.170.10. 1 hit.
InterProiIPR006028. GABAA/Glycine_rcpt.
IPR008127. Glycine_rcpt_A.
IPR008130. Glycine_rcpt_A3.
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]
PRINTSiPR00253. GABAARECEPTR.
PR01673. GLYRALPHA.
PR01676. GLYRALPHA3.
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 nameiGLRA3_MOUSE
AccessioniPrimary (citable) accession number: Q91XP5
Secondary accession number(s): Q7TSQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2005
Last sequence update: May 24, 2005
Last modified: November 2, 2016
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The alpha subunit binds strychnine.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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