GRAMD2A | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Aliases | GRAMD2A, GRAMD2, GRAM domain containing 2A | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | MGI: 3528937 HomoloGene: 52791 GeneCards: GRAMD2A | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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GRAM domain-containing 2A protein (GRAMD2A; formerly GRAMD2) is a protein encoded by the GRAMD2A gene.[5] Like GRAMD2B, the protein consists of a GRAM domain and a transmembrane domain that anchors it to the endoplasmic reticulum.[6][7]
GRAMD2A is a mammalian representative of the yeast lipid transfer proteins anchored at a membrane contact site (LAM) family.[7] It has four paralogs: GRAMD1A, GRAMD1B, GRAMD1C and GRAMD2B. Unlike LAM and its paralogs except GRAMD2B, GRAMD2A lacks a VASt domain.
The protein localizes to sites where membranes from different organelles are in close apposition.[7] There, it tethers the endoplasmic reticulum to the plasma membrane through its GRAM domain binding phosphatidylinositol 4,5-bisphosphate in the plasma membrane at sites enriched for the phospholipid.[7] The protein ensures proper stromal interaction molecule 1 (STIM1) recruitment to these sites of membrane contact as part of the store-operated calcium entry pathway – a component of intracellular calcium homeostasis.[7]
References
- 1 2 3 GRCh38: Ensembl release 89: ENSG00000175318 - Ensembl, May 2017
- 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000074259 - Ensembl, May 2017
- ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ "GRAMD2A GRAM domain containing 2A [ Homo sapiens (human) ]". Retrieved March 7, 2020.
- ↑ "RecName: Full=GRAM domain-containing protein 2A)". Retrieved March 7, 2020.
- 1 2 3 4 5 Besprozvannaya M, Dickson E, Li H, Ginburg KS, Bers DM, Auwerx J, Nunnari J (February 2018). "GRAM domain proteins specialize functionally distinct ER-PM contact sites in human cells". eLife. 22 (7): e31019. doi:10.7554/eLife.31019. PMC 5823543. PMID 29469807.