A5A6S6 · TM38A_RABIT
- ProteinTrimeric intracellular cation channel type A
- GeneTMEM38A
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids295 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
Opened by a change of voltage within the sarcoplasmic reticulum lumen (PubMed:20643059).
Catalytic activity
- K+(in) = K+(out)
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 74 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 122 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 126 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nuclear membrane | |
Cellular Component | sarcoplasmic reticulum membrane | |
Molecular Function | identical protein binding | |
Molecular Function | potassium channel activity | |
Biological Process | regulation of release of sequestered calcium ion into cytosol |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameTrimeric intracellular cation channel type A
- Short namesTRIC-A; TRICA
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Leporidae > Oryctolagus
Accessions
- Primary accessionA5A6S6
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Sarcoplasmic reticulum membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-18 | Lumenal | ||||
Sequence: MELLSALSLGELALSFSR | ||||||
Transmembrane | 19-39 | Helical;Name=1 | ||||
Sequence: VPLFPVFDLSYFIVSILYLKY | ||||||
Topological domain | 40-51 | Cytoplasmic | ||||
Sequence: EPGAVELSRRHP | ||||||
Transmembrane | 52-72 | Helical;Name=2 | ||||
Sequence: VASWLCAMLHCFGSYILADLL | ||||||
Topological domain | 73-85 | Lumenal | ||||
Sequence: LGEPLIDYFSNNS | ||||||
Transmembrane | 86-106 | Helical;Name=3 | ||||
Sequence: SILLASAVWYLIFFCPLDLFY | ||||||
Topological domain | 107-144 | Cytoplasmic | ||||
Sequence: KCVCFLPVKLIFVAMKEVVRVRKIAVGIHHAHHHYHHG | ||||||
Transmembrane | 145-165 | Helical;Name=4 | ||||
Sequence: WFIMIATGWVKGSGVALLSNV | ||||||
Topological domain | 166-178 | Lumenal | ||||
Sequence: EQLLRGVWKPETN | ||||||
Transmembrane | 179-199 | Helical;Name=5 | ||||
Sequence: EILHMSFPTKASLYGAILFTL | ||||||
Topological domain | 200-209 | Cytoplasmic | ||||
Sequence: QQTRWLPVSK | ||||||
Transmembrane | 210-230 | Helical;Name=6 | ||||
Sequence: ASLIFIFTMFMVSCKVFLTAT | ||||||
Topological domain | 231-234 | Lumenal | ||||
Sequence: HSHS | ||||||
Transmembrane | 235-255 | Helical;Name=7 | ||||
Sequence: SPFDVLEAYVCPVLFGTGSGG | ||||||
Topological domain | 256-295 | Cytoplasmic | ||||
Sequence: DHPQDNHGAWPGGPPSGALATKSKEELSEGSRKKKTKKAD |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000309465 | 1-295 | Trimeric intracellular cation channel type A | |||
Sequence: MELLSALSLGELALSFSRVPLFPVFDLSYFIVSILYLKYEPGAVELSRRHPVASWLCAMLHCFGSYILADLLLGEPLIDYFSNNSSILLASAVWYLIFFCPLDLFYKCVCFLPVKLIFVAMKEVVRVRKIAVGIHHAHHHYHHGWFIMIATGWVKGSGVALLSNVEQLLRGVWKPETNEILHMSFPTKASLYGAILFTLQQTRWLPVSKASLIFIFTMFMVSCKVFLTATHSHSSPFDVLEAYVCPVLFGTGSGGDHPQDNHGAWPGGPPSGALATKSKEELSEGSRKKKTKKAD |
Proteomic databases
Interaction
Subunit
Homotrimer; conformation seems to be controled by binding to diacylglycerol (DAG).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | A5A6S6 | TMEM38A A5A6S6 | 3 | EBI-15646422, EBI-15646422 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 256-295 | Disordered | ||||
Sequence: DHPQDNHGAWPGGPPSGALATKSKEELSEGSRKKKTKKAD | ||||||
Compositional bias | 280-295 | Basic and acidic residues | ||||
Sequence: EELSEGSRKKKTKKAD |
Sequence similarities
Belongs to the TMEM38 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length295
- Mass (Da)32,881
- Last updated2007-06-12 v1
- ChecksumC6898995BC411475
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 280-295 | Basic and acidic residues | ||||
Sequence: EELSEGSRKKKTKKAD |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB261160 EMBL· GenBank· DDBJ | BAF62543.1 EMBL· GenBank· DDBJ | mRNA |