Reviewed, UniProtKB/Swiss-Prot Q8BGE6 (ATG4B_MOUSE)

Names and origin

Protein names

Recommended name:
    Cysteine protease ATG4B
    EC=3.4.22.-
Alternative name(s):
    Autophagy-related protein 4 homolog B
    Autophagin-1
    Autophagy-related cysteine endopeptidase 1
    AUT-like 1 cysteine endopeptidase

Gene names

Name:	Atg4b
Synonyms:	Apg4b, Autl1, Kiaa0943

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Cysteine protease required for autophagy, which cleaves the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP, allowing the liberation of form I. A subpopulation of form I is subsequently converted to a smaller form (form II). Form II, with a revealed C-terminal glycine, is considered to be the phosphatidylethanolamine (PE)-conjugated form, and has the capacity for the binding to autophagosomes.
Enzyme regulation	Inhibited by N-ethylmaleimide By similarity.
Subcellular location	CytoplasmProbable.
Sequence similarities	Belongs to the peptidase C54 family.

Ontologies

Keywords
Biological process	Autophagy Protein transport Transport Ubl conjugation pathway
Cellular component	Cytoplasm
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	autophagosome formation Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB protein targeting to membrane Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB protein targeting to vacuole Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB microtubule associated complex Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	cysteine-type endopeptidase activity Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB microtubule binding Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 393	393	Cysteine protease ATG4B		PRO_0000215845
Sites
	Active site	74	1	Nucleophile By similarity
	Active site	278	1	Potential
	Active site	280	1	By similarity
Amino acid modifications
	Modified residue	34	1	Phosphoserine
	Modified residue	316	1	Phosphoserine By similarity
	Modified residue	383	1	Phosphoserine
	Modified residue	392	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	128 – 153	26	IAQMG…AQVLK → NCLNCHCCGVMLMLYKAHGS VLAFCR Ref.3
	Sequence conflict	190	1	A → V in CAD43220. Ref.1
	Sequence conflict	190	1	A → V in BAC26079, BAC27455 and BAC35965. Ref.2
	Sequence conflict	325	1	T → K in BAC40587. Ref.2
	Sequence conflict	325	1	T → K Ref.3 Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q8BGE6-1 [UniParc]. Last modified March 15, 2005. Version 2. Checksum: EB9BF54B06F79135	FASTA	393	44,375
	10 20 30 40 50 60 MDAATLTYDT LRFAEFEDFP ETSEPVWILG RKYSIFTEKD EILSDVASRL WFTYRRNFPA 70 80 90 100 110 120 IGGTGPTSDT GWGCMLRCGQ MIFAQALVCR HLGRDWRWTQ RKRQPDSYFN VLNAFLDRKD 130 140 150 160 170 180 SYYSIHQIAQ MGVGEGKSIG QWYGPNTVAQ VLKKLAVFDT WSSLAVHIAM DNTVVMEEIR 190 200 210 220 230 240 RLCRANLPCA GAAALPTDSE RHCNGFPAGA EVTNRPSAWR PLVLLIPLRL GLTDINEAYV 250 260 270 280 290 300 ETLKHCFMMP QSLGVIGGKP NSAHYFIGYV GEELIYLDPH TTQPAVELTD SCFIPDESFH 310 320 330 340 350 360 CQHPPSRMGI GELDPSIAVG FFCKTEEDFN DWCQQVKKLS QLGGALPMFE LVEQQPSHLA 370 380 390 CQDVLNLSLD SSDVERLERF FDSEDEDFEI LSL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human autophagins, a family of cysteine proteinases potentially implicated in cell degradation by autophagy." Marino G., Uria J.A., Puente X.S., Quesada V., Bordallo J., Lopez-Otin C. J. Biol. Chem. 278:3671-3678(2003) [PubMed: 12446702] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Pancreas, Skin and Testis.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Kidney.
[4]	"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H. DNA Res. 10:167-180(2003) [PubMed: 14621295] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 128-393. Tissue: Brain.
[5]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, MASS SPECTROMETRY. Tissue: Liver.
[6]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ504653 mRNA. Translation: CAD43220.1. AK028712 mRNA. Translation: BAC26079.1. AK031570 mRNA. Translation: BAC27455.1. AK075796 mRNA. Translation: BAC35965.1. AK088811 mRNA. Translation: BAC40587.1. BC027184 mRNA. Translation: AAH27184.1. AK129242 mRNA. Translation: BAC98052.1.
UniGene	Mm.29087
3D structure databases
SMR	Q8BGE6. Positions 10-373.
ModBase	Search...
Protein family/group databases
MEROPS	C54.003.
PTM databases
PhosphoSite	Q8BGE6.
Genome annotation databases
Ensembl	ENSMUSG00000026280. Mus musculus. [Contig view]
Organism-specific databases
MGI	MGI:1913865. Atg4b.
Rouge	Search...
Phylogenomic databases
HOGENOM	Q8BGE6.
HOVERGEN	Q8BGE6.
Gene expression databases
ArrayExpress	Q8BGE6.
CleanEx	MM_ATG4B.
GermOnline	ENSMUSG00000026280. Mus musculus.
Family and domain databases
InterPro	IPR005078. Peptidase_C54. [Graphical view]
PANTHER	PTHR22624. Peptidase_C54. 1 hit.
Pfam	PF03416. Peptidase_C54. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

ATG4B_MOUSE

Accession

Primary (citable) accession number: Q8BGE6
Secondary accession number(s): Q6ZQ22, Q8R098

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	November 25, 2008
This is version 45 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)