Detail Information of Protein
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Basic Information:
| Symbol | VAPA |
| Synonyms | VAP33 |
| Protein Name | Vesicle-associated membrane protein-associated protein A (VAMP-A) (VAMP-associated protein A) (VAP-A) (33 kDa VAMP-associated protein) (VAP-33) |
| Species | Human |
| Entrez ID | 9218 |
| Uniprot ID | Q9P0L0 |
| Membrane Contact Site |
ER-Endosome; Endosome-ER
|
| Location (from literature) | ER |
| Cell line/Tissue | HeLa cells; MelJuSo cells; HEK293 cells; HEK293T cells; COS-7 cells |
| Experimental Method | Low throughput experimental methods |
| Protein Sequence | |
| More related results |
Complex Information:
| Complex ID | Subunit of complex | Subcellular location | Species | More |
| CMCS00004 | VAPA; OSBPL1A; sterol; PI(4)P; NPC1 | ER-Endosome; Endosome-ER | Human | more | CMCS00008 | VAPA; VAPB; SNX2 | ER-Endosome; Endosome-ER | Human | more | CMCS00009 | VAPA; VAPB; OSBP; PI(4)P | ER-Endosome; Endosome-ER | Human | more | CMCS00011 | VAPA; VAPB; OSBPL1A | ER-Endosome; Endosome-ER | Human | more | CMCS00023 | VAPA; VAPB; STARD3 | ER-Endosome; Endosome-ER | Human | more | CMCS00024 | VAPA; VAPB; STARD3NL | ER-Endosome; Endosome-ER | Human | more | CMCS00026 | VAPB; VAPA; VPS13C | ER-Endosome; Endosome-ER | Human | more | CMCS00027 | VAPB; VAPA; OSBPL1A; RAB7A; RILP | ER-Endosome; Endosome-ER | Human | more | CMCS00167 | OSBPL10; OSBPL9; VAPA; VAPB; PI(4)P | ER-Endosome; Endosome-ER | Human | more | CMCS00071 | VAPA; VAPB; CERT1 | ER-Endosome; Endosome-ER | Human | more |
Expression Overview of VAPA:
Homology Information of VAPA:
| Uniprot ID | Q9P0L0 |
| EggNOG | / |
| HOGENOM | CLU_032848_0_1_1 |
| OrthoDB | 122649at2759 |
| TreeFam | TF317024 |
| GeneTree | ENSGT00940000154799 |
References:
| Pubmed ID | 24105263 |
| DOI | 10.1242/jcs.139295 |
| Description | FUNDC1 binds directly to DRP2 and their role in mediating Mitochondrionl fission. |
| Description of experimental evidence | The protein was validated by immunoprecipitation, electron microscopy, immunofluorescence, in situ proximity ligation assay, mSDS-PAGE and western blot analysis in HeLa cells. |
| More related results |
| Pubmed ID | 19564404 |
| DOI | 10.1083/jcb.200811005 |
| Description | We show that cholesterol in LEs is sensed by ORP1L, which transmits this information to the Rab7–RILP–p150Glued complex through the formation of ER–LE membrane contact sites (MCSs). At these sites, the ER protein VAP enters the Rab7–RILP complex to control p150Glued binding and positioning of LEs. |
| Description of experimental evidence | The protein was validated by microscopy, FLIM, Immuno-EM and filipin stainings in MelJuSo cells, and these data explain how the ER and cholesterol control the association of LEs with motor proteins and their positioning in cells. |
| More related results |
| Pubmed ID | 27419871 |
| DOI | 10.1016/j.cell.2016.06.037 |
| Description | Endosome-ER Contacts Control Actin Nucleation and Retromer Function through VAP-Dependent Regulation of PI4P. |
| Description of experimental evidence | The protein was validated by TALENs, fluorescence microscopy, western blotting and phosphoinositide analysis in HeLa cells, COS-7 cells, and these results reveal a role of PI5P in retromer-/WASH-dependent budding from endosomes. |
| More related results |
| Pubmed ID | 28564600 |
| DOI | 10.1016/j.celrep.2017.05.028 |
| Description | Cholesterol delivery to the ER required the sterol-, phosphatidylinositol 4-phosphate-, and vesicle-associated membrane protein-associated protein (VAP)-binding activities of ORP1L, as well as NPC1 expression. |
| Description of experimental evidence | The protein was validated by PCR analysis, immunoblotting, immunoprecipitation, fluorescence and electron microscopy in HeLa cells and HEK293 cells. |
| More related results |
| Pubmed ID | 28377464 |
| DOI | 10.15252/embj.201695917 |
| Description | Corroborating this, in vitro reconstitution assays indicated that STARD3 and its ER-anchored partner, Vesicle-associated membrane protein-associated protein (VAP), assemble into a machine that allows a highly efficient transport of cholesterol within membrane contacts. |
| Description of experimental evidence | The protein was validated by immunofluorescence, colocalization analysis, filipin staining, GFP-D4, filipin co-staining, flotation experiments, electron microscopy and stereology in Hela cells, and the complex allows a highly efficient transport of cholesterol within membrane contacts. |
| More related results |
| Pubmed ID | 27270042 |
| DOI | 10.1016/j.devcel.2016.05.005 |
| Description | This sterol traffic depends on interaction between ER-localized VAP and endosomal oxysterol-binding protein ORP1L, and is required for the formation of ILVs within the MVB and thus for the spatial regulation of EGFR signaling. |
| Description of experimental evidence | The protein was validated by electron microscopy, florescence Imaging, western blotting, immunoprecipitation, and quantitative RT-PCR in HeLa cells, which has important role in the sterol traffic. |
| More related results |
| Pubmed ID | 34817532 |
| DOI | 10.1083/jcb.202103141 |
| Description | ORP10, together with ORP9 and VAP, formed ER–endosome MCSs in a phosphatidylinositol 4-phosphate (PI4P)-dependent manner. |
| Description of experimental evidence | The protein was validated by immunofluorescence microscopy, live-cell imaging, image analysis, coimmunoprecipitation and LC-MS/MS in HeLa cells, HEK293T cells and COS-7 cells. |
| More related results |
| Pubmed ID | 30093493 |
| DOI | 10.1083/jcb.201807019 |
| Description | An FFAT motif, a short amino acid sequence known to interact with the ER VAMP-associated protein (VAP), is present in the Vps13α region of both proteins as previously noted.; These findings not only confirm the role of the FFAT motif in anchoring these proteins to the ER but also indicate that binding sites for mitochondria (in VPS13A), late endosomes/lysosomes (in VPS13C), and lipid droplets (both proteins) are localized in the C-terminal regions of the two proteins. |
| Description of experimental evidence | The protein was validated by bioinformatic analysis, mass spectrometry, FRET assays, correlative fluorescence, EM microscopy, Image processing, analysis and statistics in HeLa cells and COS-7 cells which has the lipid transport roles. |
| More related results |
| Pubmed ID | 33124732 |
| DOI | 10.15252/embj.2019104369 |
| Description | The endoplasmic reticulum possesses three major receptors, VAP‐A, VAP‐B, and MOSPD2, which interact with proteins at the surface of other organelles to build contacts; onventional FFATs (illustrated here with STARD11/CERT) which allow the formation of a stable complex between VAPs/MOSPD2 and thus the formation of MCSs. |
| Description of experimental evidence | The protein was validated by pull‐down assays, immunoprecipitation,SDS–PAGE, western blot, CIP treatment, coomassie blue staining, mass spectrometry analysis, immunofluorescence and colocalization analysis in HeLa cells. |
| More related results |