ID   H7BYM2_HUMAN            Unreviewed;       312 AA.
AC   H7BYM2;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Cysteine protease {ECO:0000256|RuleBase:RU363115};
DE            EC=3.4.22.- {ECO:0000256|RuleBase:RU363115};
DE   Flags: Fragment;
GN   Name=ATG4A {ECO:0000313|Ensembl:ENSP00000378354.2};
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 {ECO:0000313|Ensembl:ENSP00000378354.2, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000378354.2, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [2] {ECO:0000313|Ensembl:ENSP00000378354.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Cysteine protease that plays a key role in autophagy by
CC       mediating both proteolytic activation and delipidation of ATG8 family
CC       proteins. {ECO:0000256|RuleBase:RU363115}.
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:0000256|ARBA:ARBA00029362};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67549;
CC         Evidence={ECO:0000256|ARBA:ARBA00029362};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU363115}.
CC   -!- SIMILARITY: Belongs to the peptidase C54 family.
CC       {ECO:0000256|ARBA:ARBA00010958, ECO:0000256|RuleBase:RU363115}.
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DR   EMBL; AL031177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   MEROPS; C54.002; -.
DR   MassIVE; H7BYM2; -.
DR   MaxQB; H7BYM2; -.
DR   PeptideAtlas; H7BYM2; -.
DR   ProteomicsDB; 43666; -.
DR   Antibodypedia; 29398; 574 antibodies from 37 providers.
DR   Ensembl; ENST00000394892.2; ENSP00000378354.2; ENSG00000101844.18.
DR   UCSC; uc065aqc.1; human.
DR   HGNC; HGNC:16489; ATG4A.
DR   VEuPathDB; HostDB:ENSG00000101844; -.
DR   GeneTree; ENSGT00530000063000; -.
DR   HOGENOM; CLU_021259_3_3_1; -.
DR   ChiTaRS; ATG4A; human.
DR   Proteomes; UP000005640; Chromosome X.
DR   Bgee; ENSG00000101844; Expressed in body of pancreas and 190 other cell types or tissues.
DR   ExpressionAtlas; H7BYM2; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019786; F:protein-phosphatidylethanolamide deconjugating activity; IEA:InterPro.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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:SF35; CYSTEINE PROTEASE ATG4A; 1.
DR   Pfam; PF03416; Peptidase_C54; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
PE   1: Evidence at protein level;
KW   Autophagy {ECO:0000256|ARBA:ARBA00023006, ECO:0000256|RuleBase:RU363115};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU363115};
KW   Hydrolase {ECO:0000256|RuleBase:RU363115};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Protease {ECO:0000256|RuleBase:RU363115};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW   ECO:0000256|RuleBase:RU363115};
KW   Proteomics identification {ECO:0007829|EPD:H7BYM2,
KW   ECO:0007829|MaxQB:H7BYM2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          22..308
FT                   /note="Peptidase C54 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03416"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|Ensembl:ENSP00000378354.2"
FT   NON_TER         312
FT                   /evidence="ECO:0000313|Ensembl:ENSP00000378354.2"
SQ   SEQUENCE   312 AA;  35252 MW;  9193B66B429C7E60 CRC64;
     XLSKYEDQIT IFTDYLEEYP DTDELVWILG KQHLLKTGGT GPSSDAGWGC MLRCGQMMLA
     QALICRHLGR DWSWEKQKEQ PKEYQRILQC FLDRKDCCYS IHQMAQMGVG EGKSIGEWFG
     PNTVAQVLKK LALFDEWNSL AVYVSMDNTV VIEDIKKMCR VLPLSADTAG DRPPDSLTAS
     NQSKGTSAYC SAWKPLLLIV PLRLGINQIN PVYVDAFKEC FKMPQSLGAL GGKPNNAYYF
     IGFLGDELIF LDPHTTQTFV DTEENGTVND QTFHCLQSPQ RMNILNLDPS VALGFFCKEE
     KDFDNWCSLV QK
//