[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Brain; DOI=10.1074/jbc.M208247200; PubMed=12446702 [NCBI, ExPASy, EBI, Israel, Japan] Marino G., Uria J.A., Puente X.S., Quesada V., Bordallo J., Lopez-Otin C.; "Human autophagins, a family of cysteine proteinases potentially implicated in cell degradation by autophagy."; J. Biol. Chem. 278:3671-3678(2003).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=C57BL/6; TISSUE=Brain; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

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 (By similarity).
ENZYME REGULATION: Inhibited by N-ethylmaleimide (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (Probable).
SIMILARITY: Belongs to the peptidase C54 family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AJ312233; CAC85555.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC058981; AAH58981.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00177235; -.

XP_001471904.1; -.

3D structure databases

ModBase

Q811C2.

Protein family/group databases

MEROPS

C54.004; -.

PTM databases

PhosphoSite

Q811C2; -.

Organism-specific databases

MGI

MGI:2651854; Atg4c.

Gene expression databases

Q811C2; -.

Q811C2; -.

MM_ATG4C; -.

ENSMUSG00000028550; Mus musculus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from sequence or structural similarity from UniProtKB).
GO:0005875;	Cellular component: microtubule associated complex (inferred from sequence or structural similarity from UniProtKB).
GO:0004197;	Molecular function: cysteine-type endopeptidase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0008017;	Molecular function: microtubule binding (inferred from sequence or structural similarity from UniProtKB).
GO:0006914;	Biological process: autophagy (inferred from sequence or structural similarity from UniProtKB).
GO:0019941;	Biological process: modification-dependent protein catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0006623;	Biological process: protein targeting to vacuole (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR005078; Peptidase_C54.
Graphical view of domain structure.

PANTHER

PTHR22624; Peptidase_C54; 1.

Pfam

PF03416; Peptidase_C54; 1.
Pfam graphical view of domain structure.

Proteomic databases

PRIDE

Q811C2; -.

Genome annotation databases

Ensembl

ENSMUSG00000028550; Mus musculus. [Contig view]

GeneID

100044217; -.

KEGG

mmu:100044217; -.
mmu:242557; -.

Phylogenomic databases

HOGENOM

Q811C2; -.

HOVERGEN

Q811C2; -.

Other

457721; -.

Atg4c; Mus musculus.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Autophagy; Cytoplasm; Hydrolase; Protease; Protein transport; Thiol protease; Transport; Ubl conjugation pathway.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 458`	`458`	`Cysteine protease ATG4C.`	`PRO_0000215850`
`ACT_SITE`	`111 111`		`Nucleophile (By similarity).`
`ACT_SITE`	`345 345`		`Potential.`
`ACT_SITE`	`347 347`		`By similarity.`
`CONFLICT`	`87 87`		`I -> L (in Ref. 2; AAH58981).`
`CONFLICT`	`190 190`		`T -> A (in Ref. 2; AAH58981).`

Sequence information

Length: 458 AA [This is the length of the unprocessed precursor]

Molecular weight: 52086 Da [This is the MW of the unprocessed precursor]

CRC64: E6A134A6939A0C78 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEASGTDEVD KLKTKFISAW NNMKYSWVLK TKTYFSRNSP VLLLGKCYHF KYEDESKMLP 

        70         80         90        100        110        120 
ARSGCAIEDH VIAGNVEEFR KDFISRIWLT YREEFPQIEA SALTTDCGWG CTLRTGQMLL 

       130        140        150        160        170        180 
AQGLILHFLG RAWTWPDALH IENADSDSWT SNTVKKFTAS FEASLSGDRE LRTPAVSLKE 

       190        200        210        220        230        240 
TSGKCPDDHT VRNEAYHRKI ISWFGDSPVA VFGLHRLIEF GKKSGKKAGD WYGPAVVAHI 

       250        260        270        280        290        300 
LRKAVEEARH PDLQGLTIYV AQDCTVYNSD VIDKQTDSVT AGDARDKAVI ILVPVRLGGE 

       310        320        330        340        350        360 
RTNTDYLEFV KGVLSLEYCV GIIGGKPKQS YYFAGFQDDS LIYMDPHYCQ SFVDVSIKDF 

       370        380        390        400        410        420 
PLETFHCPSP KKMSFRKMDP SCTIGFYCRN VQDFERASEE ITKMLKISSK EKYPLFTFVN 

       430        440        450 
GHSKDFDFTS TAASEEDLFS EDERKNFKRF STEEFVLL

Q811C2 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools