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0  structures 250  species 0  interactions 520  sequences 16  architectures

Family: Atg14 (PF10186)

Summary: UV radiation resistance protein and autophagy-related subunit 14

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UV radiation resistance protein 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


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR018791

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. In mammals, the counterparts of Vps34, Vps15, and Vps30/Atg6 are Vps34, p150, and Beclin 1, respectively. Mammalian UV irradiation resistance-associated gene (UVRAG) has been identified as identical to yeast Vps38 [PUBMED:18843052].

The Atg14 (autophagy-related protein 14) proteins are hydrophilic proteins 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 [PUBMED:9712845].

This entry represents Atg14 and UVRAG, which bind Beclin 1 to forms two distinct PI3-kinase complexes. This entry also includes Bakor (beclin-1-associated autophagy-related key regulator), also known as autophagy-related protein 14-like protein, which share sequence similarity to the yeast Atg14 protein [PUBMED:19050071]. Barkor positively regulates autophagy through its interaction with Beclin-1, with decreased levels of autophagosome formation observed when Barkor expression is eliminated [PUBMED:19050071]. 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.

Gene Ontology

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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 3 members:

Atg14 Bcl-2 Bcl-2_3

Alignments

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(39)
Full
(520)
Representative proteomes NCBI
(532)
Meta
(2)
RP15
(111)
RP35
(180)
RP55
(293)
RP75
(371)
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  Seed
(39)
Full
(520)
Representative proteomes NCBI
(532)
Meta
(2)
RP15
(111)
RP35
(180)
RP55
(293)
RP75
(371)
Alignment:
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  Seed
(39)
Full
(520)
Representative proteomes NCBI
(532)
Meta
(2)
RP15
(111)
RP35
(180)
RP55
(293)
RP75
(371)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

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Curation and family details

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Curation View help on the curation process

Seed source: KOGs (KOG4398), Wood V
Previous IDs: DUF2355;
Type: Family
Author: KOGs, Finn RD, Coggill PC
Number in seed: 39
Number in full: 520
Average length of the domain: 295.80 aa
Average identity of full alignment: 16 %
Average coverage of the sequence by the domain: 56.42 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 27.1 27.1
Trusted cut-off 27.1 27.2
Noise cut-off 27.0 27.0
Model length: 302
Family (HMM) version: 4
Download: download the raw HMM for this family

Species distribution

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