ID   ATG4C_HUMAN             Reviewed;         458 AA.
AC   Q96DT6; A6NLR8; D3DQ58; Q96K04;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   02-SEP-2026, entry version 164.
DE   RecName: Full=Cysteine protease ATG4C {ECO:0000305};
DE            EC=3.4.22.- {ECO:0000269|PubMed:21177865};
DE   AltName: Full=AUT-like 3 cysteine endopeptidase;
DE   AltName: Full=Autophagy-related cysteine endopeptidase 3 {ECO:0000303|PubMed:12446702};
DE            Short=Autophagin-3 {ECO:0000303|PubMed:12446702};
DE   AltName: Full=Autophagy-related protein 4 homolog C {ECO:0000303|PubMed:21177865};
DE            Short=HsAPG4C {ECO:0000303|PubMed:29458288};
GN   Name=ATG4C {ECO:0000303|PubMed:21177865, ECO:0000312|HGNC:HGNC:16040};
GN   Synonyms=APG4C {ECO:0000303|Ref.3}, AUTL1, AUTL3
GN   {ECO:0000312|HGNC:HGNC:16040};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   RETRACTED PAPER.
RC   TISSUE=Brain;
RX   PubMed=12446702; DOI=10.1074/jbc.m208247200;
RA   Marino G., Uria J.A., Puente X.S., Quesada V., Bordallo J., Lopez-Otin C.;
RT   "Human autophagins, a family of cysteine proteinases potentially implicated
RT   in cell degradation by autophagy.";
RL   J. Biol. Chem. 278:3671-3678(2003).
RN   [2]
RP   RETRACTION NOTICE OF PUBMED:12446702.
RX   PubMed=30808002; DOI=10.1074/jbc.w118.007325;
RA   Marino G., Uria J.A., Puente X.S., Quesada V., Bordallo J., Lopez-Otin C.;
RL   J. Biol. Chem. 294:1431-1431(2019).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RA   Chen J.M., Barrett A.J.;
RT   "Cloning and sequencing of a human homologue of the yeast Apg4 cysteine
RT   endopeptidase involved in autophagy.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [9]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX   PubMed=21177865; DOI=10.1074/jbc.m110.199059;
RA   Li M., Hou Y., Wang J., Chen X., Shao Z.M., Yin X.M.;
RT   "Kinetics comparisons of mammalian Atg4 homologues indicate selective
RT   preferences toward diverse Atg8 substrates.";
RL   J. Biol. Chem. 286:7327-7338(2011).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451 AND THR-452, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [11]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=29458288; DOI=10.1080/15548627.2018.1437341;
RA   Kauffman K.J., Yu S., Jin J., Mugo B., Nguyen N., O'Brien A., Nag S.,
RA   Lystad A.H., Melia T.J.;
RT   "Delipidation of mammalian Atg8-family proteins by each of the four ATG4
RT   proteases.";
RL   Autophagy 14:992-1010(2018).
RN   [12]
RP   FUNCTION.
RX   PubMed=30661429; DOI=10.1080/15548627.2019.1569925;
RA   Agrotis A., Pengo N., Burden J.J., Ketteler R.;
RT   "Redundancy of human ATG4 protease isoforms in autophagy and LC3/GABARAP
RT   processing revealed in cells.";
RL   Autophagy 15:976-997(2019).
RN   [13]
RP   FUNCTION.
RX   PubMed=33773106; DOI=10.1016/j.molcel.2021.03.001;
RA   Nguyen T.N., Padman B.S., Zellner S., Khuu G., Uoselis L., Lam W.K.,
RA   Skulsuppaisarn M., Lindblom R.S.J., Watts E.M., Behrends C., Lazarou M.;
RT   "ATG4 family proteins drive phagophore growth independently of the
RT   LC3/GABARAP lipidation system.";
RL   Mol. Cell 81:2013-2030(2021).
RN   [14]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=33909989; DOI=10.1016/j.molcel.2021.03.020;
RA   Durgan J., Lystad A.H., Sloan K., Carlsson S.R., Wilson M.I., Marcassa E.,
RA   Ulferts R., Webster J., Lopez-Clavijo A.F., Wakelam M.J., Beale R.,
RA   Simonsen A., Oxley D., Florey O.;
RT   "Non-canonical autophagy drives alternative ATG8 conjugation to
RT   phosphatidylserine.";
RL   Mol. Cell 81:2031-2040(2021).
CC   -!- FUNCTION: Cysteine protease that plays a key role in autophagy by
CC       mediating both proteolytic activation and delipidation of ATG8 family
CC       proteins (PubMed:21177865, PubMed:29458288, PubMed:30661429). The
CC       protease activity is required for proteolytic activation of ATG8 family
CC       proteins: cleaves the C-terminal amino acid of ATG8 proteins MAP1LC3
CC       and GABARAPL2, to reveal a C-terminal glycine (PubMed:21177865).
CC       Exposure of the glycine at the C-terminus is essential for ATG8
CC       proteins conjugation to phosphatidylethanolamine (PE) and insertion to
CC       membranes, which is necessary for autophagy (By similarity). In
CC       addition to the protease activity, also mediates delipidation of ATG8
CC       family proteins (PubMed:29458288, PubMed:33909989). Catalyzes
CC       delipidation of PE-conjugated forms of ATG8 proteins during
CC       macroautophagy (PubMed:29458288, PubMed:33909989). Compared to ATG4B,
CC       the major protein for proteolytic activation of ATG8 proteins, shows
CC       weaker ability to cleave the C-terminal amino acid of ATG8 proteins,
CC       while it displays stronger delipidation activity (PubMed:29458288). In
CC       contrast to other members of the family, weakly or not involved in
CC       phagophore growth during mitophagy (PubMed:33773106).
CC       {ECO:0000250|UniProtKB:Q9Y4P1, ECO:0000269|PubMed:21177865,
CC       ECO:0000269|PubMed:29458288, ECO:0000269|PubMed:30661429,
CC       ECO:0000269|PubMed:33773106, ECO:0000269|PubMed:33909989}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-C-terminal L-amino acid-glycyl-
CC         phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-
CC         glycine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine;
CC         Xref=Rhea:RHEA:67548, Rhea:RHEA-COMP:17323, Rhea:RHEA-COMP:17324,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:64612, ChEBI:CHEBI:172940,
CC         ChEBI:CHEBI:172941; Evidence={ECO:0000269|PubMed:29458288,
CC         ECO:0000269|PubMed:33909989};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67549;
CC         Evidence={ECO:0000269|PubMed:29458288, ECO:0000269|PubMed:33909989};
CC   -!- ACTIVITY REGULATION: Inhibited by N-ethylmaleimide.
CC       {ECO:0000269|PubMed:21177865}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=47.5 uM for MAP1LC3B {ECO:0000269|PubMed:21177865};
CC         KM=12.4 uM for GABARAPL2 {ECO:0000269|PubMed:21177865};
CC   -!- INTERACTION:
CC       Q96DT6; P42858: HTT; NbExp=15; IntAct=EBI-3225845, EBI-466029;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8BGE6}.
CC   -!- SIMILARITY: Belongs to the peptidase C54 family. {ECO:0000305}.
CC   -!- CAUTION: A paper describing ATG4C tissue expression and activity has
CC       been retracted, due to concerns of image duplication in some of the
CC       figures. {ECO:0000269|PubMed:12446702, ECO:0000305|PubMed:30808002}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB55356.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AJ312234; CAC85556.1; -; mRNA.
DR   EMBL; AJ320169; CAC43939.1; -; mRNA.
DR   EMBL; AK027773; BAB55356.1; ALT_FRAME; mRNA.
DR   EMBL; AC103923; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471059; EAX06579.1; -; Genomic_DNA.
DR   EMBL; CH471059; EAX06580.1; -; Genomic_DNA.
DR   EMBL; BC033024; AAH33024.1; -; mRNA.
DR   CCDS; CCDS623.1; -.
DR   RefSeq; NP_116241.2; NM_032852.4.
DR   RefSeq; NP_835739.1; NM_178221.3.
DR   AlphaFoldDB; Q96DT6; -.
DR   SMR; Q96DT6; -.
DR   BioGRID; 124372; 40.
DR   FunCoup; Q96DT6; 183.
DR   IntAct; Q96DT6; 43.
DR   NDEx; IQUERY-CP-ATG4C; 1 NDEx IQuery Curated Pathway.
DR   STRING; 9606.ENSP00000322159; -.
DR   MEROPS; C54.004; -.
DR   GlyGen; Q96DT6; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q96DT6; -.
DR   PhosphoSitePlus; Q96DT6; -.
DR   BioMuta; ATG4C; -.
DR   DMDM; 61211867; -.
DR   jPOST; Q96DT6; -.
DR   MassIVE; Q96DT6; -.
DR   PaxDb; 9606-ENSP00000322159; -.
DR   PeptideAtlas; Q96DT6; -.
DR   ProteomicsDB; 76320; -.
DR   Pumba; Q96DT6; -.
DR   Antibodypedia; 1971; 570 antibodies from 40 providers.
DR   DNASU; 84938; -.
DR   Ensembl; ENST00000317868.9; ENSP00000322159.4; ENSG00000125703.16.
DR   Ensembl; ENST00000371120.7; ENSP00000360161.3; ENSG00000125703.16.
DR   Ensembl; ENST00000852834.1; ENSP00000522893.1; ENSG00000125703.16.
DR   Ensembl; ENST00000852837.1; ENSP00000522896.1; ENSG00000125703.16.
DR   Ensembl; ENST00000852839.1; ENSP00000522898.1; ENSG00000125703.16.
DR   Ensembl; ENST00000852840.1; ENSP00000522899.1; ENSG00000125703.16.
DR   Ensembl; ENST00000852842.1; ENSP00000522901.1; ENSG00000125703.16.
DR   Ensembl; ENST00000929148.1; ENSP00000599207.1; ENSG00000125703.16.
DR   Ensembl; ENST00000945357.1; ENSP00000615416.1; ENSG00000125703.16.
DR   Ensembl; ENST00000945359.1; ENSP00000615418.1; ENSG00000125703.16.
DR   Ensembl; ENST00000945360.1; ENSP00000615419.1; ENSG00000125703.16.
DR   GeneID; 84938; -.
DR   KEGG; hsa:84938; -.
DR   MANE-Select; ENST00000317868.9; ENSP00000322159.4; NM_032852.4; NP_116241.2.
DR   UCSC; uc001dat.5; human.
DR   AGR; HGNC:16040; -.
DR   ClinPGx; PA25183; -.
DR   CTD; 84938; -.
DR   DisGeNET; 84938; -.
DR   GeneCards; ATG4C; -.
DR   HGNC; HGNC:16040; ATG4C.
DR   HPA; ENSG00000125703; Low tissue specificity.
DR   MIM; 611339; gene.
DR   OpenTargets; ENSG00000125703; -.
DR   VEuPathDB; HostDB:ENSG00000125703; -.
DR   eggNOG; KOG2674; Eukaryota.
DR   GeneTree; ENSGT00530000063000; -.
DR   HOGENOM; CLU_021259_3_2_1; -.
DR   InParanoid; Q96DT6; -.
DR   OMA; KMAGDWY; -.
DR   OrthoDB; 2960936at2759; -.
DR   PAN-GO; Q96DT6; 8 GO annotations based on evolutionary models.
DR   PhylomeDB; Q96DT6; -.
DR   PathwayCommons; Q96DT6; -.
DR   Reactome; R-HSA-1632852; Macroautophagy.
DR   SABIO-RK; Q96DT6; -.
DR   SignaLink; Q96DT6; -.
DR   Agora; ENSG00000125703; -.
DR   BioGRID-ORCS; 84938; 16 hits in 1151 CRISPR screens.
DR   ChiTaRS; ATG4C; human.
DR   GenomeRNAi; 84938; -.
DR   Pharos; Q96DT6; Tbio.
DR   PRO; PR:Q96DT6; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q96DT6; protein.
DR   Bgee; ENSG00000125703; Expressed in corpus callosum and 175 other cell types or tissues.
DR   ExpressionAtlas; Q96DT6; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProt.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IDA:UniProtKB.
DR   GO; GO:0019786; F:protein-phosphatidylethanolamide deconjugating activity; IBA:GO_Central.
DR   GO; GO:0035973; P:aggrephagy; IBA:GO_Central.
DR   GO; GO:0000045; P:autophagosome assembly; IDA:UniProt.
DR   GO; GO:0006914; P:autophagy; IDA:UniProtKB.
DR   GO; GO:0000423; P:mitophagy; IBA:GO_Central.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR   GO; GO:0051697; P:protein delipidation; IDA:UniProtKB.
DR   GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR   InterPro; IPR046793; ATG4_LIR.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR005078; Peptidase_C54.
DR   InterPro; IPR046792; Peptidase_C54_cat.
DR   PANTHER; PTHR22624; CYSTEINE PROTEASE ATG4; 1.
DR   PANTHER; PTHR22624:SF38; CYSTEINE PROTEASE ATG4C; 1.
DR   Pfam; PF20166; ATG4_LIR; 1.
DR   Pfam; PF03416; Peptidase_C54; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Autophagy; Cytoplasm; Hydrolase; Phosphoprotein; Protease;
KW   Protein transport; Proteomics identification; Reference proteome;
KW   Thiol protease; Transport; Ubl conjugation pathway.
FT   CHAIN           1..458
FT                   /note="Cysteine protease ATG4C"
FT                   /id="PRO_0000215849"
FT   ACT_SITE        111
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT   ACT_SITE        345
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT   ACT_SITE        347
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   MOD_RES         451
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         452
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
SQ   SEQUENCE   458 AA;  52497 MW;  6A23A05E7F20AF27 CRC64;
     MEATGTDEVD KLKTKFISAW NNMKYSWVLK TKTYFSRNSP VLLLGKCYHF KYEDEDKTLP
     AESGCTIEDH VIAGNVEEFR KDFISRIWLT YREEFPQIEG SALTTDCGWG CTLRTGQMLL
     AQGLILHFLG RAWTWPDALN IENSDSESWT SHTVKKFTAS FEASLSGERE FKTPTISLKE
     TIGKYSDDHE MRNEVYHRKI ISWFGDSPLA LFGLHQLIEY GKKSGKKAGD WYGPAVVAHI
     LRKAVEEARH PDLQGITIYV AQDCTVYNSD VIDKQSASMT SDNADDKAVI ILVPVRLGGE
     RTNTDYLEFV KGILSLEYCV GIIGGKPKQS YYFAGFQDDS LIYMDPHYCQ SFVDVSIKDF
     PLETFHCPSP KKMSFRKMDP SCTIGFYCRN VQDFKRASEE ITKMLKFSSK EKYPLFTFVN
     GHSRDYDFTS TTTNEEDLFS EDEKKQLKRF STEEFVLL
//