ATG4A_ARATH
ID ATG4A_ARATH Reviewed; 467 AA.
AC Q8S929; O80583; Q3EBG5;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Cysteine protease ATG4a {ECO:0000305};
DE EC=3.4.22.- {ECO:0000250|UniProtKB:Q9Y4P1};
DE AltName: Full=Autophagy-related protein 4 homolog a {ECO:0000303|PubMed:12114572};
DE Short=AtAPG4a {ECO:0000303|PubMed:12114572};
DE Short=Protein autophagy 4a {ECO:0000303|PubMed:12114572};
GN Name=ATG4A {ECO:0000303|PubMed:12114572};
GN Synonyms=APG4A {ECO:0000303|PubMed:12114572}; OrderedLocusNames=At2g44140;
GN ORFNames=F6E13.27;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NOMENCLATURE, AND GENE FAMILY.
RX PubMed=12114572; DOI=10.1104/pp.011024;
RA Hanaoka H., Noda T., Shirano Y., Kato T., Hayashi H., Shibata D.,
RA Tabata S., Ohsumi Y.;
RT "Leaf senescence and starvation-induced chlorosis are accelerated by the
RT disruption of an Arabidopsis autophagy gene.";
RL Plant Physiol. 129:1181-1193(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=15494556; DOI=10.1105/tpc.104.025395;
RA Yoshimoto K., Hanaoka H., Sato S., Kato T., Tabata S., Noda T., Ohsumi Y.;
RT "Processing of ATG8s, ubiquitin-like proteins, and their deconjugation by
RT ATG4s are essential for plant autophagy.";
RL Plant Cell 16:2967-2983(2004).
CC -!- FUNCTION: Cysteine protease that plays a key role in autophagy by
CC mediating both proteolytic activation and delipidation of ATG8 family
CC proteins. The protease activity is required for proteolytic activation
CC of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8
CC proteins to reveal a C-terminal glycine (By similarity). Exposure of
CC the glycine at the C-terminus is essential for ATG8 proteins
CC conjugation to phosphatidylethanolamine (PE) and insertion to
CC membranes, which is necessary for autophagy. In addition to the
CC protease activity, also mediates delipidation of PE-conjugated ATG8
CC proteins (By similarity). {ECO:0000250|UniProtKB:Q2XPP4,
CC ECO:0000250|UniProtKB:Q9Y4P1}.
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:0000250|UniProtKB:Q9Y4P1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67549;
CC Evidence={ECO:0000250|UniProtKB:Q9Y4P1};
CC -!- SUBUNIT: Interacts with ATG8. {ECO:0000250|UniProtKB:Q9Y4P1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8BGE6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8S929-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8S929-2; Sequence=VSP_025232;
CC -!- TISSUE SPECIFICITY: Constitutively expressed.
CC {ECO:0000269|PubMed:15494556}.
CC -!- SIMILARITY: Belongs to the peptidase C54 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC23418.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB073171; BAB88383.1; -; mRNA.
DR EMBL; AC004005; AAC23418.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10380.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10381.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62619.1; -; Genomic_DNA.
DR EMBL; AK227012; BAE99076.1; -; mRNA.
DR PIR; T00694; T00694.
DR RefSeq; NP_001318423.1; NM_001337075.1. [Q8S929-2]
DR RefSeq; NP_001324765.1; NM_001337076.1. [Q8S929-1]
DR RefSeq; NP_850412.1; NM_180081.4. [Q8S929-1]
DR AlphaFoldDB; Q8S929; -.
DR SMR; Q8S929; -.
DR STRING; 3702.AT2G44140.1; -.
DR MEROPS; C54.011; -.
DR PaxDb; Q8S929; -.
DR PRIDE; Q8S929; -.
DR EnsemblPlants; AT2G44140.1; AT2G44140.1; AT2G44140. [Q8S929-1]
DR EnsemblPlants; AT2G44140.2; AT2G44140.2; AT2G44140. [Q8S929-2]
DR EnsemblPlants; AT2G44140.3; AT2G44140.3; AT2G44140. [Q8S929-1]
DR GeneID; 819020; -.
DR Gramene; AT2G44140.1; AT2G44140.1; AT2G44140. [Q8S929-1]
DR Gramene; AT2G44140.2; AT2G44140.2; AT2G44140. [Q8S929-2]
DR Gramene; AT2G44140.3; AT2G44140.3; AT2G44140. [Q8S929-1]
DR KEGG; ath:AT2G44140; -.
DR Araport; AT2G44140; -.
DR TAIR; locus:2051754; AT2G44140.
DR eggNOG; KOG2674; Eukaryota.
DR InParanoid; Q8S929; -.
DR PhylomeDB; Q8S929; -.
DR PRO; PR:Q8S929; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8S929; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004175; F:endopeptidase activity; IDA:TAIR.
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 PANTHER; PTHR22624; PTHR22624; 1.
DR Pfam; PF03416; Peptidase_C54; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Autophagy; Cytoplasm; Hydrolase; Protease;
KW Protein transport; Reference proteome; Thiol protease; Transport;
KW Ubl conjugation pathway.
FT CHAIN 1..467
FT /note="Cysteine protease ATG4a"
FT /id="PRO_0000286898"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..467
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 170
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT ACT_SITE 364
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT ACT_SITE 366
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT VAR_SEQ 1..57
FT /note="MKALCDRFVPQQCSSSSKSDTHDKSPLVSDSGPSDNKSKFTLWSNVFTSSSS
FT VSQPY -> MRRTRCSWCFMS (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_025232"
SQ SEQUENCE 467 AA; 51529 MW; 3A6394E0B2A2BEE3 CRC64;
MKALCDRFVP QQCSSSSKSD THDKSPLVSD SGPSDNKSKF TLWSNVFTSS SSVSQPYRES
STSGHKQVCT TRNGWTAFVK RVSMASGAIR RFQERVLGPN RTGLPSTTSD VWLLGVCYKI
SADENSGETD TGTVLAALQL DFSSKILMTY RKGFEPFRDT TYTSDVNWGC MIRSSQMLFA
QALLFHRLGR AWTKKSELPE QEYLETLEPF GDSEPSAFSI HNLIIAGASY GLAAGSWVGP
YAICRAWESL ACKKRKQTDS KNQTLPMAVH IVSGSEDGER GGAPILCIED ATKSCLEFSK
GQSEWTPIIL LVPLVLGLDS VNPRYIPSLV ATFTFPQSVG ILGGKPGAST YIVGVQEDKG
FYLDPHEVQQ VVTVNKETPD VDTSSYHCNV LRYVPLESLD PSLALGFYCR DKDDFDDFCL
RALKLAEESN GAPLFTVTQT HTAINQSNYG FADDDSEDER EDDWQML
