Q6P4T0 · ATG2A_MOUSE

  • Protein
    Autophagy-related protein 2 homolog A
  • Gene
    Atg2a
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

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

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum membrane
Cellular Componentlipid droplet
Cellular Componentorganelle membrane contact site
Cellular Componentphagophore assembly site membrane
Molecular Functionlipid transfer activity
Biological Processautophagosome assembly
Biological Processpositive regulation of autophagosome assembly

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Autophagy-related protein 2 homolog A

Gene names

    • Name
      Atg2a
    • Synonyms
      Kiaa0404

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • FVB/N
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q6P4T0
  • Secondary accessions
    • Q3U9I1
    • Q6PHN0
    • Q6ZQC4
    • Q8R213

Proteomes

Organism-specific databases

Subcellular Location

Preautophagosomal structure membrane
; Peripheral membrane protein
Lipid droplet
Endoplasmic reticulum membrane
; Peripheral membrane protein
Note: Localizes to endoplasmic reticulum-autophagosome contact sites.

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00003152351-1914
Modified residue764Phosphoserine
Modified residue869Phosphoserine
Modified residue875Phosphoserine
Modified residue877Phosphoserine
Modified residue1246Phosphoserine
Modified residue1282Phosphoserine
Modified residue1290Phosphoserine
Modified residue1381Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Interacts with ATG9A (via C-terminus). Interacts with TMEM41B. Interacts with VMP1.

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain14-112Chorein N-terminal
Region1222-1243Disordered
Region1299-1337Disordered
Region1337-1383WIPI-interacting
Region1427-1452Disordered
Compositional bias1431-1452Polar residues
Region1589-1634Disordered
Compositional bias1601-1634Polar residues
Region1803-1822Disordered
Compositional bias1806-1822Basic and acidic residues

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 status
    Complete
  • Length
    1,914
  • Mass (Da)
    210,939
  • Last updated
    2006-09-19 v2
  • Checksum
    16742111A5534572
MSRWLWPWSNCVKERVCRYLLQHYLGHFFQEHLSLDQLSLDLYKGSVALRDIHLETWSVNEFLRSMESPLELVEGFVSSIEVAVPWAALLTDHCTVCVSGLQLTLQPRQGSGPGAADSQSWASCMTTSLQLAQECLREGLPEPSEPPQPLEGLEMFAQTIETVLRRIKVTFLNTVVRVEHSLGDEDRSVAVEVRVQRLEYCDEAVRDPSQAPPVDVHQPPAFLHKLLQLSGVCLYFEELPSQADPPQPPLQIGSCTGYVELMVRLKQNEAFPGPKLEVSGQLGSLHLLLTPRQLQQLQRLLSAVNLADPAGLADKLNKSRPLGAEDLWLIEQDLNQQLQAGAVAESLSLYPITNPLNLDSTDLFFSMAGLTSSVTSAVSELSVYSVDLGSSVHSNMAFHRPSTPPHSGGKMAPTPLLDTTRPDSLVKMTLGGVSLTLLQTASPSSGPSDLPTHFFAEFDAAKDGPFGSRDFSHLRPRFQRACPCSHVRLTGTAVQLSWELRTGSHSRRTSSTEVHFGQLEVLECLWPRAATEPEYTEILSFPSHSGSEASARPCAHLRHTQTIRRVLKSRSRRSTACHCHSELSLDLADFQSDVELGSLDRLAALFRQVTTPSEPPAGLLTEPPQATELQTVFRLSAPRATLRLRFPIPDLRPDRDPWAGQAVRAEQLRLELSEPQFRSELNSGPGPPAPTRLELTCSDLQGIYEDGEKPPVPCLRVSKALNPRSTEAKYFLPQVVVTLNPQSSGTQWETAYEKGRDLELSTESPCELQQPEPSPFSSKRTMYETEEMVIPGDPEEMRTFQSRTLALSRCTLDVIMPSAHIFLPSKEVYESIYNRINNDLLMWEPADLLPTSSAAARPPGSSGFKMCKSAFKLDSDSDEEDAQFFSMASGVPQTPAPEPSRRQSQSTFSTLVTVLKGRITALCEAKDETGKRLDVTHGELVLDVEQGTIFSVAQYRGQPGLGYFCLEAEKAKLYHRAAIEDYLLPTHLEVPSFAPPAQLAPTIYPSEEGVTERGTLGRKGQGPPMLSAAVRIHLDPHKNVKEFLVTVRLHKATLRHYMAPPEQSWHSQLLDFLDVLDDPVLGYLPPTVITVLHTHLFSCAVDYRPLYLPVRVLVTAETFTLSSNIVMDTSTFLLRFILDDSALYLSDKCEVESLDLRRDYVCVLDIDLLELVIKTWKGSTEGRLSQPLFELRCSNNVVHVHSCADSCALLVNLLQYLTSSGDLHPPPRPPSPTEIAGQKLSESPASLPSCLPVETALINQRDLTDALLDTERRGLQELAQSSGGPLPQASPVSVYLFPGERSGAQAPLPPPGASSHTLGSKAKEHENEEEGDGDTLDSDEFCILDAPGLGIAPRDGEPIVTQLHPGPIIVHDGHFSQPLGSTDLLRAPAHFPVPSSRVVLREVSFIWHLYGGRDFGLHPTYRARVGLTGPRVSPSRSSGPNRPQNSWRTQGGIGRQHQVLMEIQLSKVSFQHEVYPEESAIAGGLGQELDERPLSRQVLIVQELEIRDRLATSKINKFLHLHTSERLPRRTHSNMLTIKALHVAPTSSVGGPECCLRVSMMPLRLNVDQDALFFLKDFFTSLAASINPMVPGDTSEAPRETHSRPGSPQEGQSEDTETASNPPEAPGSSHSSSDQQPIYFREFRFTSEVPICLDYHGKHVTVDQVGTFMGLLIGLAQLNCSELKLKRLCCRHGLLGVDKVLCYALNEWLQDIRKNQLPGLLGGVGPMHSVVQLFQGFRDLLWLPIEQYRKDGRLIRGLQRGAASFGSSTASAALELSNRLVQAIQATAETVYDILSPASPVSRSLQDKRSSRKLRRGQQPADLREGMAKAYDAVREGILDTAQTICDVASRGHEQKGLTGAVGGVIRQLPPTVVKPIIVATEATSNVLGGMRNQILPDAHKDHALKWRLEEAQD

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
F6V3Y9F6V3Y9_MOUSEAtg2a1718

Sequence caution

The sequence BAC97942.1 differs from that shown. Reason: Erroneous initiation
The sequence BAE30685.1 differs from that shown. Reason: Frameshift

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict285in Ref. 1; BAC97942
Compositional bias1431-1452Polar residues
Compositional bias1601-1634Polar residues
Sequence conflict1738in Ref. 3; BAE30685
Compositional bias1806-1822Basic and acidic residues
Sequence conflict1865in Ref. 3; BAE30685

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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