1  structure 109  species 0  interactions 242  sequences 6  architectures

Family: Autophagy_act_C (PF03987)

Summary

Autophagocytosis associated protein, active-site domain Add an annotation

Autophagocytosis is a starvation-induced process responsible for transport of cytoplasmic proteins to the vacuole. The cysteine residue within the HPC motif is the putative active-site residue for recognition of the Apg5 subunit of the autophagosome complex [2].


Literature references

  1. Schlumpberger M, Schaeffeler E, Straub M, Bredschneider M, Wolf DH, Thumm M; , J Bacteriol 1997;179:1068-1076.: AUT1, a gene essential for autophagocytosis in the yeast Saccharomyces cerevisiae. PUBMED:9023185

  2. Mizushima N, Yoshimori T, Ohsumi Y; , FEBS Lett. 2002;532:450-454.: Mouse Apg10 as an Apg12-conjugating enzyme: analysis by the conjugation-mediated yeast two-hybrid method. PUBMED:12482611

  3. Yamaguti M, Suzuki NN, Fujioka Y, Ohsumi Y, Inagaki F; , Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007;63:443-445.: Crystallization and preliminary X-ray analysis of Atg10. PUBMED:17565192


InterPro entry IPR007135

Proteins in this entry belong to the Atg3 group of proteins and the Atg3 conjugation enzymes.

Autophagy is a degradative transport pathway that delivers cytosolic proteins to the lysosome (vacuole) PUBMED:11058089 and is induced by starvation PUBMED:9190802. Cytosolic proteins appear inside the vacuole enclosed in autophagic vesicles. Autophagy significantly differs from other transport pathways by using double membrane layered transport intermediates, called autophagosomes PUBMED:11675007, PUBMED:18472412. The breakdown of vesicular transport intermediates is a unique feature of autophagy PUBMED:11058089. Autophagy can also function in the elimination of invading bacteria and antigens PUBMED:18472412.

Atg3 is the E2 enzyme for the LC3 lipidation process PUBMED:18321988. It is essential for autophagocytosis. The super protein complex, the Atg16L complex, consists of multiple Atg12-Atg5 conjugates. Atg16L has an E3-like role in the LC3 lipidation reaction. The activated intermediate, LC3-Atg3 (E2), is recruited to the site where the lipidation takes place PUBMED:18398292.

Atg3 catalyses the conjugation of Atg8 and phosphatidylethanolamine (PE). Atg3 has an alpha/beta-fold, and its core region is topologically similar to canonical E2 enzymes. Atg3 has two regions inserted in the core region and another with a long alpha-helical structure that protrudes from the core region as far as 30 A PUBMED:17227760. It interacts with atg8 through an intermediate thioester bond between Cys-288 and the C-terminal Gly of atg8. It also interacts with the C-terminal region of the E1-like atg7 enzyme.

Autophagocytosis is a starvation-induced process responsible for transport of cytoplasmic proteins to the vacuole. The cysteine residue within the HPC motif is the putative active-site residue for recognition of the Apg5 subunit of the autophagosome complex PUBMED:12482611.

External database links

Domain organisation

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Alignments

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Trees

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Curation and family details

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Curation View help on the curation process

Seed source: Pfam-B_10019 (release 7.3)
Previous IDs: Autophagy_C;
Type: Domain
Author: Finn RD, Wood V, Coggill PC
Number in seed: 59
Number in full: 242
Average length of the domain: 65.00 aa
Average identity of full alignment: 36 %
Average coverage of the sequence by the domain: 23.02 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.3 21.3
Trusted cut-off 22.0 21.3
Noise cut-off 20.9 20.8
Model length: 65
Family (HMM) version: 8
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Species distribution

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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD 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 Autophagy_act_C domain has been found.

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