P57695 · GLRA1_BOVIN

  • Protein
    Glycine receptor subunit alpha-1
  • Gene
    GLRA1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Glycine receptors are ligand-gated chloride channels. Channel opening is triggered by extracellular glycine. Channel opening is also triggered by taurine and beta-alanine. Channel characteristics depend on the subunit composition; heteropentameric channels are activated by lower glycine levels and display faster desensitization (By similarity).
Plays an important role in the down-regulation of neuronal excitability (PubMed:11178872).
Contributes to the generation of inhibitory postsynaptic currents. Channel activity is potentiated by ethanol (By similarity).
Potentiation of channel activity by intoxicating levels of ethanol contribute to the sedative effects of ethanol (By similarity).

Miscellaneous

The alpha subunit binds strychnine.

Catalytic activity

Features

Showing features for binding site, site.

TypeIDPosition(s)Description
Binding site220Zn2+ (UniProtKB | ChEBI)
Binding site222Zn2+ (UniProtKB | ChEBI)
Binding site230-235strychnine (UniProtKB | ChEBI)
Binding site243Zn2+ (UniProtKB | ChEBI)
Site289Important for obstruction of the ion pore in the closed conformation

GO annotations

AspectTerm
Cellular Componentchloride channel complex
Cellular Componentdendrite
Cellular Componentintracellular membrane-bounded organelle
Cellular Componentneuron projection
Cellular Componentneuronal cell body
Cellular Componentperikaryon
Cellular Componentplasma membrane
Cellular Componentpostsynaptic membrane
Cellular Componentsynapse
Cellular Componenttransmembrane transporter complex
Molecular Functionextracellularly glycine-gated chloride channel activity
Molecular Functionglycine binding
Molecular Functionneurotransmitter receptor activity
Molecular Functiontaurine binding
Molecular Functiontransmembrane signaling receptor activity
Molecular Functiontransmitter-gated monoatomic ion channel activity
Molecular Functionzinc ion binding
Biological Processcellular response to amino acid stimulus
Biological Processcellular response to ethanol
Biological Processcellular response to zinc ion
Biological Processchloride transmembrane transport
Biological Processchloride transport
Biological Processinhibitory postsynaptic potential
Biological Processmonoatomic ion transport
Biological Processmuscle contraction
Biological Processnegative regulation of transmission of nerve impulse
Biological Processneuropeptide signaling pathway
Biological Processresponse to alcohol
Biological Processstartle response
Biological Processsynaptic transmission, glycinergic

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glycine receptor subunit alpha-1
  • Alternative names
    • Glycine receptor 48 kDa subunit
    • Glycine receptor strychnine-binding subunit

Gene names

    • Name
      GLRA1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos

Accessions

  • Primary accession
    P57695
  • Secondary accessions
    • Q9GKE9
    • Q9GKF0

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain29-250Extracellular
Transmembrane251-272Helical; Name=1
Topological domain273-277Cytoplasmic
Transmembrane278-298Helical; Name=2
Topological domain299-309Extracellular
Transmembrane310-330Helical; Name=3
Topological domain331-425Cytoplasmic
Transmembrane426-446Helical; Name=4
Topological domain447-457Extracellular

Keywords

Phenotypes & Variants

Involvement in disease

  • Defects in GLRA1 are the cause of inherited congenital myoclonus of Poll Hereford calves. It is an autosomal recessive disease characterized by hyperesthesia and myoclonic jerks of the skeletal musculature that occur both spontaneously and in response to sensory stimuli

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 49 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond.

TypeIDPosition(s)Description
Signal1-28
ChainPRO_000000041129-457Glycine receptor subunit alpha-1
Glycosylation66N-linked (GlcNAc...) asparagine
Disulfide bond166↔180
Disulfide bond226↔237

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Detected on spinal cord neurons (at protein level). Detected in spinal cord.

Gene expression databases

Interaction

Subunit

Homopentamer (in vitro). Interacts with GLRB to form heteropentameric channels; this is probably the predominant form in vivo. Heteropentamer composed of two GLRA1 and three GLRB. Heteropentamer composed of three GLRA1 and two GLRB. Both homopentamers and heteropentamers form functional ion channels, but their characteristics are subtly different. Interacts with GLRB (By similarity).

Protein-protein interaction databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region391-410Disordered

Domain

The channel pore is formed by pentameric assembly of the second transmembrane domain from all five subunits. Channel opening is effected by an outward rotation of the transmembrane domains that increases the diameter of the pore.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 2 isoforms produced by Alternative splicing.

P57695-1

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.

  • Length
    457
  • Mass (Da)
    52,614
  • Last updated
    2000-12-08 v1
  • Checksum
    0C60A814C8ADFDDE
MYSFNTLRLYLWETIVFFSLAASKEAEAARSASKPMSPSDFLDKLMGRTSGYDARIRPNFKGPPVNVSCNIFINSFGSIAETTMDYRVNIFLRQQWNDPRLAYNEYPDDSLDLDPSMLDSIWKPDLFFANEKGAHFHEITTDNKLLRISRNGNVLYSIRITLTLACPMDLKNFPMDVQTCIMQLESFGYTMNDLIFEWQEQGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFTCIEARFHLERQMGYYLIQMYIPSLLIVILSWISFWINMDAAPARVGLGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMAVCLLFVFSALLEYAAVNFVSRQHKELLRFRRKRRHHKSPMLNLFQEDEAGEGRFNFSAYGMGPACLQAKDGISVKGANNSNTTNPPPAPSKSPEEMRKLFIQRAKKIDKISRIGFPMAFLIFNMFYWIIYKIVRREDVHNQ

P57695-2

  • Name
    b
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_021141354-361in isoform b

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF268375
EMBL· GenBank· DDBJ
AAG14346.1
EMBL· GenBank· DDBJ
mRNA
AF268366
EMBL· GenBank· DDBJ
AAG41140.1
EMBL· GenBank· DDBJ
Genomic DNA
AF268358
EMBL· GenBank· DDBJ
AAG41140.1
EMBL· GenBank· DDBJ
Genomic DNA
AF268360
EMBL· GenBank· DDBJ
AAG41140.1
EMBL· GenBank· DDBJ
Genomic DNA
AF268361
EMBL· GenBank· DDBJ
AAG41140.1
EMBL· GenBank· DDBJ
Genomic DNA
AF268359
EMBL· GenBank· DDBJ
AAG41140.1
EMBL· GenBank· DDBJ
Genomic DNA
AF268362
EMBL· GenBank· DDBJ
AAG41140.1
EMBL· GenBank· DDBJ
Genomic DNA
AF268364
EMBL· GenBank· DDBJ
AAG41140.1
EMBL· GenBank· DDBJ
Genomic DNA
AF268365
EMBL· GenBank· DDBJ
AAG41140.1
EMBL· GenBank· DDBJ
Genomic DNA
AF268363
EMBL· GenBank· DDBJ
AAG41140.1
EMBL· GenBank· DDBJ
Genomic DNA
AF268366
EMBL· GenBank· DDBJ
AAG41141.1
EMBL· GenBank· DDBJ
Genomic DNA
AF268358
EMBL· GenBank· DDBJ
AAG41141.1
EMBL· GenBank· DDBJ
Genomic DNA
AF268360
EMBL· GenBank· DDBJ
AAG41141.1
EMBL· GenBank· DDBJ
Genomic DNA
AF268361
EMBL· GenBank· DDBJ
AAG41141.1
EMBL· GenBank· DDBJ
Genomic DNA
AF268359
EMBL· GenBank· DDBJ
AAG41141.1
EMBL· GenBank· DDBJ
Genomic DNA
AF268362
EMBL· GenBank· DDBJ
AAG41141.1
EMBL· GenBank· DDBJ
Genomic DNA
AF268364
EMBL· GenBank· DDBJ
AAG41141.1
EMBL· GenBank· DDBJ
Genomic DNA
AF268365
EMBL· GenBank· DDBJ
AAG41141.1
EMBL· GenBank· DDBJ
Genomic DNA
AF268363
EMBL· GenBank· DDBJ
AAG41141.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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