ID   ATG4C_HUMAN             Reviewed;         458 AA.
AC   Q96DT6; A6NLR8; Q96K04;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   19-JAN-2010, entry version 64.
DE   RecName: Full=Cysteine protease ATG4C;
DE            EC=3.4.22.-;
DE   AltName: Full=Autophagy-related protein 4 homolog C;
DE   AltName: Full=Autophagin-3;
DE   AltName: Full=Autophagy-related cysteine endopeptidase 3;
DE   AltName: Full=AUT-like 3 cysteine endopeptidase;
GN   Name=ATG4C; Synonyms=APG4C, AUTL1, AUTL3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=12446702; DOI=10.1074/jbc.M208247200;
RA   Marino G., Uria J.A., Puente X.S., Quesada V., Bordallo J.,
RA   Lopez-Otin C.;
RT   "Human autophagins, a family of cysteine proteinases potentially
RT   implicated in cell degradation by autophagy.";
RL   J. Biol. Chem. 278:3671-3678(2003).
RN   [2]
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
RT   cysteine endopeptidase involved in autophagy.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [4]
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.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   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.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   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.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
CC   -!- FUNCTION: Cysteine protease required for autophagy, which cleaves
CC       the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP,
CC       allowing the liberation of form I. A subpopulation of form I is
CC       subsequently converted to a smaller form (form II). Form II, with
CC       a revealed C-terminal glycine, is considered to be the
CC       phosphatidylethanolamine (PE)-conjugated form, and has the
CC       capacity for the binding to autophagosomes.
CC   -!- ENZYME REGULATION: Inhibited by N-ethylmaleimide.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle, heart,
CC       liver and testis.
CC   -!- SIMILARITY: Belongs to the peptidase C54 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB55356.1; Type=Frameshift; Positions=420;
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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; BC033024; AAH33024.1; -; mRNA.
DR   IPI; IPI00156979; -.
DR   RefSeq; NP_116241.2; -.
DR   RefSeq; NP_835739.1; -.
DR   UniGene; Hs.7353; -.
DR   SMR; Q96DT6; 38-426.
DR   STRING; Q96DT6; -.
DR   MEROPS; C54.004; -.
DR   PhosphoSite; Q96DT6; -.
DR   Ensembl; ENST00000317868; ENSP00000322159; ENSG00000125703; Homo sapiens.
DR   Ensembl; ENST00000371120; ENSP00000360161; ENSG00000125703; Homo sapiens.
DR   GeneID; 84938; -.
DR   KEGG; hsa:84938; -.
DR   UCSC; uc001dat.1; human.
DR   CTD; 84938; -.
DR   GeneCards; GC01P062962; -.
DR   H-InvDB; HIX0000660; -.
DR   HGNC; HGNC:16040; ATG4C.
DR   HPA; HPA007049; -.
DR   MIM; 611339; gene.
DR   PharmGKB; PA25183; -.
DR   eggNOG; prNOG17368; -.
DR   HOGENOM; HBG445086; -.
DR   HOVERGEN; Q96DT6; -.
DR   InParanoid; Q96DT6; -.
DR   OMA; KMLKISS; -.
DR   OrthoDB; EOG9THZD3; -.
DR   PhylomeDB; Q96DT6; -.
DR   NextBio; 75392; -.
DR   ArrayExpress; Q96DT6; -.
DR   Bgee; Q96DT6; -.
DR   CleanEx; HS_ATG4C; -.
DR   Genevestigator; Q96DT6; -.
DR   GermOnline; ENSG00000125703; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:HPA.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IMP:UniProtKB.
DR   GO; GO:0005515; F:protein binding; ISS:UniProtKB.
DR   GO; GO:0000045; P:autophagic vacuole assembly; IGI:UniProtKB.
DR   GO; GO:0019941; P:modification-dependent protein catabolic pr...; IEA:UniProtKB-KW.
DR   GO; GO:0006612; P:protein targeting to membrane; ISS:UniProtKB.
DR   InterPro; IPR005078; Peptidase_C54.
DR   PANTHER; PTHR22624; Peptidase_C54; 1.
DR   Pfam; PF03416; Peptidase_C54; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Autophagy; Complete proteome; Cytoplasm; Hydrolase;
KW   Protease; Protein transport; Thiol protease; Transport;
KW   Ubl conjugation pathway.
FT   CHAIN         1    458       Cysteine protease ATG4C.
FT                                /FTId=PRO_0000215849.
FT   ACT_SITE    111    111       Nucleophile (By similarity).
FT   ACT_SITE    345    345       Potential.
FT   ACT_SITE    347    347       By similarity.
FT   MOD_RES       1      1       N-acetylmethionine.
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
//