Autophagy-related protein 9A (ATG9A)

The protein contains 839 amino acids for an estimated molecular weight of 94447 Da.

 

Involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Plays a key role in the organization of the preautophagosomal structure/phagophore assembly site (PAS), the nucleating site for formation of the sequestering vesicle. Cycles between a juxta-nuclear trans-Golgi network compartment and late endosomes. Nutrient starvation induces accumulation on autophagosomes. Starvation-dependent trafficking requires ULK1, ATG13 and SUPT20H. (updated: April 1, 2015)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  3. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  4. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  5. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
  6. Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete		TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.
Protein sequence (FASTA)
Protein coevolution profile (FreeContact)
Multiple Sequence Alignment (Muscle)

This protein is predicted to be membranous by TOPCONS.

Topcons

Interpro domains
Total structural coverage: 13%
Model score: 36
MODL_ROSETTA-3.4

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VariantDescription
dbSNP:rs2276635
dbSNP:rs2276634

The reference OMIM entry for this protein is 612204

Autophagy 9, s. cerevisiae, homolog of, a; atg9a
Apg9-like 1; apg9l1

CLONING

Yamada et al. (2005) cloned mouse and human ATG9A, which they called APG9L1. The deduced 839-amino acid human protein has an APG9-like domain and predicted transmembrane domains. Northern blot and RT-PCR analysis detected APG9L1 in all tissues examined. Mouse Apg9l1 was also widely expressed. Time-lapse imaging showed that mouse Apg9l1 colocalized with the autophagosome membrane marker Lc3 (MAP1LC3A; 601242) in transfected COS-7 cells.

GENE FUNCTION

Using small interfering RNA, Yamada et al. (2005) found that knockdown of APG9L1 in HeLa cells reduced starvation-induced autophagosome formation and that mouse Apg9l2 (ATG9B; 612205) complemented the loss of APG9L1. Yamada et al. (2005) concluded that APG9L1 is essential for mammalian autophagy and that APG9L2 is complementary to APG9L1.

MAPPING

Yamada et al. (2005) stated that the ATG9A gene maps to chromosome 2q35.

EVOLUTION

Yamada et al. (2005) found that all lower eukaryotes have a single ATG9 gene, and all vertebrates they examined had 2 genes, ATG9A and ATG9B, suggesting that a duplication of the ATG9 gene occurred before the divergence of fish. ... More on the omim web site

Subscribe to this protein entry history

Dec. 9, 2018: Protein entry updated
Automatic update: model status changed

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 612204 was added.