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1  structure 1211  species 0  interactions 2421  sequences 48  architectures

Family: ATG14 (PF10186)

Summary: Vacuolar sorting 38 and autophagy-related subunit 14

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Vacuolar sorting 38 and autophagy-related subunit 14 Provide feedback

The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway [1]. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localisation of this complex at the PAS is controlled by Atg14 [2]. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex [3].

Literature references

  1. Kametaka S, Okano T, Ohsumi M, Ohsumi Y; , J Biol Chem 1998;273:22284-22291.: Apg14p and Apg6/Vps30p form a protein complex essential for autophagy in the yeast, Saccharomyces cerevisiae. PUBMED:9712845 EPMC:9712845

  2. Suzuki K, Ohsumi Y;, FEBS Lett. 2007;581:2156-2161.: Molecular machinery of autophagosome formation in yeast, Saccharomyces cerevisiae. PUBMED:17382324 EPMC:17382324

  3. Sun Q, Fan W, Chen K, Ding X, Chen S, Zhong Q;, Proc Natl Acad Sci U S A. 2008;105:19211-19216.: Identification of Barkor as a mammalian autophagy-specific factor for Beclin 1 and class III phosphatidylinositol 3-kinase. PUBMED:19050071 EPMC:19050071

  4. Sun LL, Li M, Suo F, Liu XM, Shen EZ, Yang B, Dong MQ, He WZ, Du LL;, PLoS Genet. 2013;9:e1003715.: Global analysis of fission yeast mating genes reveals new autophagy factors. PUBMED:23950735 EPMC:23950735

  5. Nakatogawa H, Suzuki K, Kamada Y, Ohsumi Y;, Nat Rev Mol Cell Biol. 2009;10:458-467.: Dynamics and diversity in autophagy mechanisms: lessons from yeast. PUBMED:19491929 EPMC:19491929

Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR018791

This entry includes Atg14 (autophagy-related protein 14) from budding yeasts, Vps38 from fission yeasts and their homologues, Atg14L/Bakor (beclin-1-associated autophagy-related key regulator) and UVRAG (UV irradiation resistance-associated gene), from animals.

Atg14 is a hydrophilic protein with a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole [ PUBMED:9712845 ].

Barkor positively regulates autophagy through its interaction with Beclin-1, with decreased levels of autophagosome formation observed when Barkor expression is eliminated [ PUBMED:19050071 ]. UVRAG is also a Beclin 1 binding protein that positively stimulate starvation-induced autophagy [ PUBMED:16799551 ]. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer.

Class III phosphatidylinositol 3-kinase (PI3-kinase) regulates multiple membrane trafficking. In yeast, two distinct PI3-kinase complexes are known: complex I (Vps34, Vps15, Vps30/Atg6, and Atg14) is involved in autophagy, and complex II (Vps34, Vps15, Vps30/Atg6, and Vps38) functions in the vacuolar protein sorting pathway [ PUBMED:11157979 ]. In mammals, complex II is also involved in autophagy [ PUBMED:20643123 ]. The mammalian counterparts of Vps34, Vps15, and Vps30/Atg6 are Vps34, p150, and Beclin 1, respectively, and UV irradiation resistance-associated gene (UVRAG) has been identified as identical to yeast Vps38 [ PUBMED:18843052 ].

Domain organisation

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Pfam Clan

This family is a member of clan BCLiA (CL0551), which has the following description:

This superfamily is characterised by families of proteins that inhibit apoptosis, They are regulated by all BH3-only proteins to promote apoptosis.

The clan contains the following 5 members:

ATG14 Bcl-2 Bcl-2_3 BID VPS38


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Curation and family details

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Seed source: KOGs (KOG4398), Wood V
Previous IDs: DUF2355; Atg14;
Type: Family
Sequence Ontology: SO:0100021
Author: KOGs, Finn RD , Coggill P
Number in seed: 27
Number in full: 2421
Average length of the domain: 292.40 aa
Average identity of full alignment: 18 %
Average coverage of the sequence by the domain: 53.39 %

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HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 33.2 33.2
Trusted cut-off 33.2 33.2
Noise cut-off 33.0 33.1
Model length: 324
Family (HMM) version: 11
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Species distribution

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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the ATG14 domain has been found. There are 1 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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