Q6P4T0 · ATG2A_MOUSE
- ProteinAutophagy-related protein 2 homolog A
- GeneAtg2a
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1914 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Lipid transfer protein involved in autophagosome assembly. Tethers the edge of the isolation membrane (IM) to the endoplasmic reticulum (ER) and mediates direct lipid transfer from ER to IM for IM expansion. Binds to the ER exit site (ERES), which is the membrane source for autophagosome formation, and extracts phospholipids from the membrane source and transfers them to ATG9 (ATG9A or ATG9B) to the IM for membrane expansion. Lipid transfer activity is enhanced by WIPI1 and WDR45/WIPI4, which promote ATG2A-association with phosphatidylinositol 3-monophosphate (PI3P)-containing membranes. Also regulates lipid droplets morphology and distribution within the cell.
(Microbial infection) Mediates the intracellular lifestyle of Cryptococcus neoformans by supporting infection.
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out)
- a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out)
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | lipid droplet | |
Cellular Component | organelle membrane contact site | |
Cellular Component | phagophore assembly site membrane | |
Molecular Function | lipid transfer activity | |
Biological Process | autophagosome assembly | |
Biological Process | positive regulation of autophagosome assembly |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameAutophagy-related protein 2 homolog A
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ6P4T0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Preautophagosomal structure membrane ; Peripheral membrane protein
Endoplasmic reticulum membrane ; Peripheral membrane protein
Note: Localizes to endoplasmic reticulum-autophagosome contact sites.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000315235 | 1-1914 | Autophagy-related protein 2 homolog A | |||
Sequence: MSRWLWPWSNCVKERVCRYLLQHYLGHFFQEHLSLDQLSLDLYKGSVALRDIHLETWSVNEFLRSMESPLELVEGFVSSIEVAVPWAALLTDHCTVCVSGLQLTLQPRQGSGPGAADSQSWASCMTTSLQLAQECLREGLPEPSEPPQPLEGLEMFAQTIETVLRRIKVTFLNTVVRVEHSLGDEDRSVAVEVRVQRLEYCDEAVRDPSQAPPVDVHQPPAFLHKLLQLSGVCLYFEELPSQADPPQPPLQIGSCTGYVELMVRLKQNEAFPGPKLEVSGQLGSLHLLLTPRQLQQLQRLLSAVNLADPAGLADKLNKSRPLGAEDLWLIEQDLNQQLQAGAVAESLSLYPITNPLNLDSTDLFFSMAGLTSSVTSAVSELSVYSVDLGSSVHSNMAFHRPSTPPHSGGKMAPTPLLDTTRPDSLVKMTLGGVSLTLLQTASPSSGPSDLPTHFFAEFDAAKDGPFGSRDFSHLRPRFQRACPCSHVRLTGTAVQLSWELRTGSHSRRTSSTEVHFGQLEVLECLWPRAATEPEYTEILSFPSHSGSEASARPCAHLRHTQTIRRVLKSRSRRSTACHCHSELSLDLADFQSDVELGSLDRLAALFRQVTTPSEPPAGLLTEPPQATELQTVFRLSAPRATLRLRFPIPDLRPDRDPWAGQAVRAEQLRLELSEPQFRSELNSGPGPPAPTRLELTCSDLQGIYEDGEKPPVPCLRVSKALNPRSTEAKYFLPQVVVTLNPQSSGTQWETAYEKGRDLELSTESPCELQQPEPSPFSSKRTMYETEEMVIPGDPEEMRTFQSRTLALSRCTLDVIMPSAHIFLPSKEVYESIYNRINNDLLMWEPADLLPTSSAAARPPGSSGFKMCKSAFKLDSDSDEEDAQFFSMASGVPQTPAPEPSRRQSQSTFSTLVTVLKGRITALCEAKDETGKRLDVTHGELVLDVEQGTIFSVAQYRGQPGLGYFCLEAEKAKLYHRAAIEDYLLPTHLEVPSFAPPAQLAPTIYPSEEGVTERGTLGRKGQGPPMLSAAVRIHLDPHKNVKEFLVTVRLHKATLRHYMAPPEQSWHSQLLDFLDVLDDPVLGYLPPTVITVLHTHLFSCAVDYRPLYLPVRVLVTAETFTLSSNIVMDTSTFLLRFILDDSALYLSDKCEVESLDLRRDYVCVLDIDLLELVIKTWKGSTEGRLSQPLFELRCSNNVVHVHSCADSCALLVNLLQYLTSSGDLHPPPRPPSPTEIAGQKLSESPASLPSCLPVETALINQRDLTDALLDTERRGLQELAQSSGGPLPQASPVSVYLFPGERSGAQAPLPPPGASSHTLGSKAKEHENEEEGDGDTLDSDEFCILDAPGLGIAPRDGEPIVTQLHPGPIIVHDGHFSQPLGSTDLLRAPAHFPVPSSRVVLREVSFIWHLYGGRDFGLHPTYRARVGLTGPRVSPSRSSGPNRPQNSWRTQGGIGRQHQVLMEIQLSKVSFQHEVYPEESAIAGGLGQELDERPLSRQVLIVQELEIRDRLATSKINKFLHLHTSERLPRRTHSNMLTIKALHVAPTSSVGGPECCLRVSMMPLRLNVDQDALFFLKDFFTSLAASINPMVPGDTSEAPRETHSRPGSPQEGQSEDTETASNPPEAPGSSHSSSDQQPIYFREFRFTSEVPICLDYHGKHVTVDQVGTFMGLLIGLAQLNCSELKLKRLCCRHGLLGVDKVLCYALNEWLQDIRKNQLPGLLGGVGPMHSVVQLFQGFRDLLWLPIEQYRKDGRLIRGLQRGAASFGSSTASAALELSNRLVQAIQATAETVYDILSPASPVSRSLQDKRSSRKLRRGQQPADLREGMAKAYDAVREGILDTAQTICDVASRGHEQKGLTGAVGGVIRQLPPTVVKPIIVATEATSNVLGGMRNQILPDAHKDHALKWRLEEAQD | ||||||
Modified residue | 764 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 869 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 875 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 877 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1246 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1282 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1290 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1381 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 14-112 | Chorein N-terminal | ||||
Sequence: ERVCRYLLQHYLGHFFQEHLSLDQLSLDLYKGSVALRDIHLETWSVNEFLRSMESPLELVEGFVSSIEVAVPWAALLTDHCTVCVSGLQLTLQPRQGSG | ||||||
Region | 1222-1243 | Disordered | ||||
Sequence: DLHPPPRPPSPTEIAGQKLSES | ||||||
Region | 1299-1337 | Disordered | ||||
Sequence: GERSGAQAPLPPPGASSHTLGSKAKEHENEEEGDGDTLD | ||||||
Region | 1337-1383 | WIPI-interacting | ||||
Sequence: DSDEFCILDAPGLGIAPRDGEPIVTQLHPGPIIVHDGHFSQPLGSTD | ||||||
Region | 1427-1452 | Disordered | ||||
Sequence: LTGPRVSPSRSSGPNRPQNSWRTQGG | ||||||
Compositional bias | 1431-1452 | Polar residues | ||||
Sequence: RVSPSRSSGPNRPQNSWRTQGG | ||||||
Region | 1589-1634 | Disordered | ||||
Sequence: MVPGDTSEAPRETHSRPGSPQEGQSEDTETASNPPEAPGSSHSSSD | ||||||
Compositional bias | 1601-1634 | Polar residues | ||||
Sequence: THSRPGSPQEGQSEDTETASNPPEAPGSSHSSSD | ||||||
Region | 1803-1822 | Disordered | ||||
Sequence: RSLQDKRSSRKLRRGQQPAD | ||||||
Compositional bias | 1806-1822 | Basic and acidic residues | ||||
Sequence: QDKRSSRKLRRGQQPAD |
Domain
The chorein N-terminal domain mediates lipid transfer activity.
Sequence similarities
Belongs to the ATG2 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,914
- Mass (Da)210,939
- Last updated2006-09-19 v2
- Checksum16742111A5534572
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F6V3Y9 | F6V3Y9_MOUSE | Atg2a | 1718 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 285 | in Ref. 1; BAC97942 | ||||
Sequence: L → M | ||||||
Compositional bias | 1431-1452 | Polar residues | ||||
Sequence: RVSPSRSSGPNRPQNSWRTQGG | ||||||
Compositional bias | 1601-1634 | Polar residues | ||||
Sequence: THSRPGSPQEGQSEDTETASNPPEAPGSSHSSSD | ||||||
Sequence conflict | 1738 | in Ref. 3; BAE30685 | ||||
Sequence: R → G | ||||||
Compositional bias | 1806-1822 | Basic and acidic residues | ||||
Sequence: QDKRSSRKLRRGQQPAD | ||||||
Sequence conflict | 1865 | in Ref. 3; BAE30685 | ||||
Sequence: V → M |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK129132 EMBL· GenBank· DDBJ | BAC97942.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC022657 EMBL· GenBank· DDBJ | AAH22657.1 EMBL· GenBank· DDBJ | mRNA | ||
BC056482 EMBL· GenBank· DDBJ | AAH56482.2 EMBL· GenBank· DDBJ | mRNA | ||
BC063264 EMBL· GenBank· DDBJ | AAH63264.2 EMBL· GenBank· DDBJ | mRNA | ||
AK151782 EMBL· GenBank· DDBJ | BAE30685.1 EMBL· GenBank· DDBJ | mRNA | Frameshift |