ATG4B

Cysteine protease ATG4B is an enzyme that in humans is encoded by the ATG4B gene.

ATG4B
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2CY7, 2D1I, 2Z0D, 2Z0E, 2ZZP
Identifiers
Aliases	ATG4B, APG4B, AUTL1, autophagy related 4B cysteine peptidase, HsAPG4B
External IDs	OMIM: 611338; MGI: 1913865; HomoloGene: 100868; GeneCards: ATG4B; OMA:ATG4B - orthologs
Gene location (Human) Chr. Chromosome 2 (human) Band 2q37.3 Start 241,637,213 bp End 241,673,857 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right hemisphere of cerebellum anterior pituitary right lobe of thyroid gland left testis left lobe of thyroid gland body of uterus canal of the cervix right ovary left ovary mucosa of transverse colon n/a More reference expression data BioGPS n/a
Gene ontology Molecular function peptidase activity cysteine-type peptidase activity endopeptidase activity protein binding hydrolase activity cysteine-type endopeptidase activity Cellular component cytoplasm cytosol Biological process autophagy protein transport autophagy of nucleus C-terminal protein lipidation positive regulation of protein catabolic process autophagy of mitochondrion autophagosome assembly macroautophagy proteolysis protein targeting to membrane protein delipidation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 23192 66615 Ensembl ENSG00000168397 n/a UniProt Q9Y4P1 Q8BGE6 RefSeq (mRNA) NM_013325 NM_178326 NM_174874 NM_001368266 RefSeq (protein) NP_037457 NP_847896 NP_777363 NP_001355195 Location (UCSC) Chr 2: 241.64 – 241.67 Mb n/a PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Function

Autophagy is the process by which endogenous proteins and damaged organelles are destroyed intracellularly. Autophagy is postulated to be essential for cell homeostasis and cell remodeling during differentiation, metamorphosis, non-apoptotic cell death, and aging. Reduced levels of autophagy have been described in some malignant tumors, and a role for autophagy in controlling the unregulated cell growth linked to cancer has been proposed. This gene encodes a member of the autophagin protein family. The encoded protein is also designated as a member of the C-54 family of cysteine proteases. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. One main function of Atg4 is to cleave the pre-protein of Atg8, leading to the non-lipidated soluble (-I) form which can be processed further by Atg3, Atg7, Atg5-12 into the lipidated form (-II) anchored to the autophagic membrane.

Interactions

ATG4B has been shown to interact with GABARAPL2.

External links

• Human ATG4B genome location and ATG4B gene details page in the UCSC Genome Browser.

Further reading

• Kraft LJ, Kenworthy AK (Jan 2012). "Imaging protein complex formation in the autophagy pathway: analysis of the interaction of LC3 and Atg4B(C74A) in live cells using Förster resonance energy transfer and fluorescence recovery after photobleaching". Journal of Biomedical Optics. 17 (1): 011008–011008–13. Bibcode:2012JBO....17a1008K. doi:10.1117/1.JBO.17.1.011008. PMC 3380812. PMID 22352642.
• Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Feb 1999). "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 6 (1): 63–70. doi:10.1093/dnares/6.1.63. PMID 10231032.
• Hartley JL, Temple GF, Brasch MA (Nov 2000). "DNA cloning using in vitro site-specific recombination". Genome Research. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
• Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (Mar 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Research. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
• Kabeya Y, Mizushima N, Yamamoto A, Oshitani-Okamoto S, Ohsumi Y, Yoshimori T (Jun 2004). "LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation". Journal of Cell Science. 117 (Pt 13): 2805–12. doi:10.1242/jcs.01131. PMID 15169837.
• Tanida I, Sou YS, Ezaki J, Minematsu-Ikeguchi N, Ueno T, Kominami E (Aug 2004). "HsAtg4B/HsApg4B/autophagin-1 cleaves the carboxyl termini of three human Atg8 homologues and delipidates microtubule-associated protein light chain 3- and GABAA receptor-associated protein-phospholipid conjugates". The Journal of Biological Chemistry. 279 (35): 36268–76. doi:10.1074/jbc.M401461200. PMID 15187094.
• Tanida I, Ueno T, Kominami E (Nov 2004). "Human light chain 3/MAP1LC3B is cleaved at its carboxyl-terminal Met121 to expose Gly120 for lipidation and targeting to autophagosomal membranes". The Journal of Biological Chemistry. 279 (46): 47704–10. doi:10.1074/jbc.M407016200. PMID 15355958.
• Wiemann S, Arlt D, Huber W, Wellenreuther R, Schleeger S, Mehrle A, Bechtel S, Sauermann M, Korf U, Pepperkok R, Sültmann H, Poustka A (Oct 2004). "From ORFeome to biology: a functional genomics pipeline". Genome Research. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
• Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (Sep 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
• Sugawara K, Suzuki NN, Fujioka Y, Mizushima N, Ohsumi Y, Inagaki F (Dec 2005). "Structural basis for the specificity and catalysis of human Atg4B responsible for mammalian autophagy". The Journal of Biological Chemistry. 280 (48): 40058–65. doi:10.1074/jbc.M509158200. PMID 16183633.
• Kumanomidou T, Mizushima T, Komatsu M, Suzuki A, Tanida I, Sou YS, Ueno T, Kominami E, Tanaka K, Yamane T (Jan 2006). "The crystal structure of human Atg4b, a processing and de-conjugating enzyme for autophagosome-forming modifiers". Journal of Molecular Biology. 355 (4): 612–8. doi:10.1016/j.jmb.2005.11.018. PMID 16325851.
• Mehrle A, Rosenfelder H, Schupp I, del Val C, Arlt D, Hahne F, Bechtel S, Simpson J, Hofmann O, Hide W, Glatting KH, Huber W, Pepperkok R, Poustka A, Wiemann S (Jan 2006). "The LIFEdb database in 2006". Nucleic Acids Research. 34 (Database issue): D415-8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.
• Tanida I, Sou YS, Minematsu-Ikeguchi N, Ueno T, Kominami E (Jun 2006). "Atg8L/Apg8L is the fourth mammalian modifier of mammalian Atg8 conjugation mediated by human Atg4B, Atg7 and Atg3". The FEBS Journal. 273 (11): 2553–62. doi:10.1111/j.1742-4658.2006.05260.x. PMID 16704426. S2CID 11899126.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (Nov 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.
• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.