A5A6S6 · TM38A_RABIT

Function

function

Intracellular monovalent cation channel required for maintenance of rapid intracellular calcium release. Acts as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores (PubMed:17611541).
Opened by a change of voltage within the sarcoplasmic reticulum lumen (PubMed:20643059).

Catalytic activity

Activity regulation

Channel activity is activated by a change of voltage within the sarcoplasmic reticulum lumen and blocked by luminal high Ca2+ levels.

Features

Showing features for binding site.

129520406080100120140160180200220240260280
TypeIDPosition(s)Description
Binding site74Ca2+ (UniProtKB | ChEBI)
Binding site122a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) (UniProtKB | ChEBI)
Binding site126a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentnuclear membrane
Cellular Componentsarcoplasmic reticulum membrane
Molecular Functionidentical protein binding
Molecular Functionpotassium channel activity
Biological Processregulation of release of sequestered calcium ion into cytosol

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Trimeric intracellular cation channel type A
  • Short names
    TRIC-A; TRICA
  • Alternative names
    • Mitsugumin-33A
    • Transmembrane protein 38A

Gene names

    • Name
      TMEM38A
    • Synonyms
      MG33A

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Leporidae > Oryctolagus

Accessions

  • Primary accession
    A5A6S6

Proteomes

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-18Lumenal
Transmembrane19-39Helical;Name=1
Topological domain40-51Cytoplasmic
Transmembrane52-72Helical;Name=2
Topological domain73-85Lumenal
Transmembrane86-106Helical;Name=3
Topological domain107-144Cytoplasmic
Transmembrane145-165Helical;Name=4
Topological domain166-178Lumenal
Transmembrane179-199Helical;Name=5
Topological domain200-209Cytoplasmic
Transmembrane210-230Helical;Name=6
Topological domain231-234Lumenal
Transmembrane235-255Helical;Name=7
Topological domain256-295Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003094651-295Trimeric intracellular cation channel type A

Proteomic databases

Interaction

Subunit

Homotrimer; conformation seems to be controled by binding to diacylglycerol (DAG).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY A5A6S6TMEM38A A5A6S63EBI-15646422, EBI-15646422

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region256-295Disordered
Compositional bias280-295Basic and acidic residues

Sequence similarities

Belongs to the TMEM38 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    295
  • Mass (Da)
    32,881
  • Last updated
    2007-06-12 v1
  • Checksum
    C6898995BC411475
MELLSALSLGELALSFSRVPLFPVFDLSYFIVSILYLKYEPGAVELSRRHPVASWLCAMLHCFGSYILADLLLGEPLIDYFSNNSSILLASAVWYLIFFCPLDLFYKCVCFLPVKLIFVAMKEVVRVRKIAVGIHHAHHHYHHGWFIMIATGWVKGSGVALLSNVEQLLRGVWKPETNEILHMSFPTKASLYGAILFTLQQTRWLPVSKASLIFIFTMFMVSCKVFLTATHSHSSPFDVLEAYVCPVLFGTGSGGDHPQDNHGAWPGGPPSGALATKSKEELSEGSRKKKTKKAD

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias280-295Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB261160
EMBL· GenBank· DDBJ
BAF62543.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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