ID   ATG7_ARATH              Reviewed;         697 AA.
AC   Q94CD5; Q9FJ46;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 139.
DE   RecName: Full=Ubiquitin-like modifier-activating enzyme atg7;
DE   AltName: Full=ATG12-activating enzyme E1 atg7;
DE   AltName: Full=Autophagy-related protein 7;
DE            Short=AtAPG7;
DE   AltName: Full=Protein PEROXISOME UNUSUAL POSITIONING 4 {ECO:0000303|PubMed:24368788};
GN   Name=ATG7; Synonyms=APG7, PEUP4 {ECO:0000303|PubMed:24368788};
GN   OrderedLocusNames=At5g45900; ORFNames=K15I22.10;
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], FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=12070171; DOI=10.1074/jbc.m204630200;
RA   Doelling J.H., Walker J.M., Friedman E.M., Thompson A.R., Vierstra R.D.;
RT   "The APG8/12-activating enzyme APG7 is required for proper nutrient
RT   recycling and senescence in Arabidopsis thaliana.";
RL   J. Biol. Chem. 277:33105-33114(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA   Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT   features of the regions of 1,081,958 bp covered by seventeen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:379-391(1998).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-558.
RX   PubMed=24368788; DOI=10.1105/tpc.113.116947;
RA   Shibata M., Oikawa K., Yoshimoto K., Kondo M., Mano S., Yamada K.,
RA   Hayashi M., Sakamoto W., Ohsumi Y., Nishimura M.;
RT   "Highly oxidized peroxisomes are selectively degraded via autophagy in
RT   Arabidopsis.";
RL   Plant Cell 25:4967-4983(2013).
RN   [7]
RP   FUNCTION.
RX   PubMed=24510943; DOI=10.1093/jxb/eru008;
RA   Sakuraba Y., Lee S.H., Kim Y.S., Park O.K., Hoertensteiner S., Paek N.C.;
RT   "Delayed degradation of chlorophylls and photosynthetic proteins in
RT   Arabidopsis autophagy mutants during stress-induced leaf yellowing.";
RL   J. Exp. Bot. 65:3915-3925(2014).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (3.11 ANGSTROMS) OF 7-325.
RA   Yamaguchi M., Matoba K., Sawada R., Fujioka Y., Nakatogawa H., Yamamoto H.,
RA   Kobashigawa Y., Hoshida H., Akada R., Ohsumi Y., Noda N.N., Inagaki F.;
RT   "Non-canonical recognition and ambiguous Ubl-loading of two distinct E2s by
RT   autophagy-essential E1, Atg7.";
RL   Submitted (SEP-2012) to the PDB data bank.
CC   -!- FUNCTION: E1-like activating enzyme involved in the 2 ubiquitin-like
CC       systems required for cytoplasm to vacuole transport (Cvt) and
CC       autophagy. Activates ATG12 for its conjugation with ATG5 and ATG8 for
CC       its conjugation with phosphatidylethanolamine. Both systems are needed
CC       for the ATG8 association to Cvt vesicles and autophagosomes. Involved
CC       in the senescence process (PubMed:12070171). Involved in the
CC       degradation of damaged peroxisomes (PubMed:24368788). Involved in the
CC       non-selective degradation of chlorophylls and photosynthetic proteins
CC       during stress-induced leaf yellowing (PubMed:24510943).
CC       {ECO:0000269|PubMed:12070171, ECO:0000269|PubMed:24368788,
CC       ECO:0000269|PubMed:24510943}.
CC   -!- SUBUNIT: Homodimer. Interacts with ATG8 through a thioester bond
CC       between Cys-558 and the C-terminal glycine of ATG8 and with ATG12
CC       through a thioester bond between Cys-558 and the C-terminal glycine of
CC       ATG12. Interacts also with ATG3 (By similarity). {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Constitutively expressed (at protein level).
CC       {ECO:0000269|PubMed:12070171}.
CC   -!- DEVELOPMENTAL STAGE: Up-regulated during leaf senescence.
CC       {ECO:0000269|PubMed:12070171}.
CC   -!- DOMAIN: The C-terminal residues are required for homodimerization, as
CC       well as the interactions with ATG3, ATG8 and ATG12. {ECO:0000250}.
CC   -!- DOMAIN: The GxGxxG motif is important for the function, possibly
CC       through binding with ATP.
CC   -!- DISRUPTION PHENOTYPE: Increased number of peroxisomes and accumulation
CC       of peroxisomal proteins. {ECO:0000269|PubMed:24368788}.
CC   -!- SIMILARITY: Belongs to the ATG7 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB09318.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF492761; AAM70190.1; -; mRNA.
DR   EMBL; AB073173; BAB88385.1; -; mRNA.
DR   EMBL; AB016870; BAB09318.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED95313.1; -; Genomic_DNA.
DR   EMBL; AY034945; AAK59451.1; -; mRNA.
DR   EMBL; AY150456; AAN12897.1; -; mRNA.
DR   RefSeq; NP_568652.1; NM_123958.3.
DR   PDB; 3VX8; X-ray; 3.11 A; A/D=7-325.
DR   PDBsum; 3VX8; -.
DR   AlphaFoldDB; Q94CD5; -.
DR   SMR; Q94CD5; -.
DR   BioGRID; 19879; 4.
DR   IntAct; Q94CD5; 3.
DR   MINT; Q94CD5; -.
DR   STRING; 3702.Q94CD5; -.
DR   TCDB; 9.A.15.3.1; the autophagy-related phagophore-formation transporter (apt) family.
DR   PaxDb; 3702-AT5G45900-1; -.
DR   ProteomicsDB; 246623; -.
DR   EnsemblPlants; AT5G45900.1; AT5G45900.1; AT5G45900.
DR   GeneID; 834630; -.
DR   Gramene; AT5G45900.1; AT5G45900.1; AT5G45900.
DR   KEGG; ath:AT5G45900; -.
DR   Araport; AT5G45900; -.
DR   TAIR; AT5G45900; APG7.
DR   eggNOG; KOG2337; Eukaryota.
DR   HOGENOM; CLU_012998_2_1_1; -.
DR   InParanoid; Q94CD5; -.
DR   OMA; RQIWDAI; -.
DR   OrthoDB; 1128973at2759; -.
DR   PhylomeDB; Q94CD5; -.
DR   PRO; PR:Q94CD5; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q94CD5; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0019779; F:Atg8 activating enzyme activity; ISS:TAIR.
DR   GO; GO:0006914; P:autophagy; ISS:TAIR.
DR   GO; GO:0050832; P:defense response to fungus; IEP:TAIR.
DR   GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR   GO; GO:0006497; P:protein lipidation; ISS:TAIR.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd01486; Apg7; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.140.100; Ubiquitin-like modifier-activating enzyme ATG7 C-terminal domain; 1.
DR   Gene3D; 3.40.140.70; Ubiquitin-like modifier-activating enzyme ATG7 N-terminal domain; 1.
DR   InterPro; IPR006285; Atg7.
DR   InterPro; IPR032197; Atg7_N.
DR   InterPro; IPR042522; Atg7_N_1.
DR   InterPro; IPR042523; Atg7_N_2.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   NCBIfam; TIGR01381; E1_like_apg7; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   PANTHER; PTHR10953:SF3; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME ATG7; 1.
DR   Pfam; PF16420; ATG7_N; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR   Genevisible; Q94CD5; AT.
PE   1: Evidence at protein level;
KW   3D-structure; Autophagy; Protein transport; Reference proteome;
KW   Stress response; Transport; Ubl conjugation pathway.
FT   CHAIN           1..697
FT                   /note="Ubiquitin-like modifier-activating enzyme atg7"
FT                   /id="PRO_0000286939"
FT   REGION          656..697
FT                   /note="Homodimerization"
FT                   /evidence="ECO:0000250"
FT   MOTIF           364..369
FT                   /note="GXGXXG motif"
FT   ACT_SITE        558
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         558
FT                   /note="C->Y: In peup4; loss of function."
FT                   /evidence="ECO:0000269|PubMed:24368788"
FT   STRAND          18..20
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   HELIX           22..34
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   TURN            35..38
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   STRAND          43..49
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   HELIX           65..67
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   STRAND          86..98
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   HELIX           99..104
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   HELIX           108..123
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   HELIX           126..129
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   HELIX           131..133
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   STRAND          137..144
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   TURN            145..148
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   STRAND          149..159
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   STRAND          166..172
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   HELIX           173..176
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   HELIX           179..194
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   STRAND          203..209
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   STRAND          214..217
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   HELIX           219..221
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   HELIX           222..225
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   STRAND          230..237
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   HELIX           250..261
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   STRAND          264..271
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   TURN            280..282
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   STRAND          284..289
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   STRAND          304..307
FT                   /evidence="ECO:0007829|PDB:3VX8"
FT   STRAND          317..320
FT                   /evidence="ECO:0007829|PDB:3VX8"
SQ   SEQUENCE   697 AA;  76522 MW;  F9855AED0F9007FB CRC64;
     MAEKETPAII LQFAPLNSSV DEGFWHSFSS LKLDKLGIDD SPISITGFYG PCGHPQVSNH
     LTLLSESLPL DEQSLIASTS HGNRNKCPVP GILYNTNTVE SFNKLDKQSL LKAEANKIWE
     DIQSGKALED PSVLPRFLVI SFADLKKWSF RYWFAFPAFV LDPPVSLIEL KPASEYFSSE
     EAESVSAACN DWRDSDLTTD VPFFLVSVSS DSKASIRHLK DLEACQGDHQ KLLFGFYDPC
     HLPSNPGWPL RNYLALIRSR WNLETVWFFC YRESRGFADL NLSLVGQASI TLSSGESAET
     VPNSVGWELN KGKRVPRSIS LANSMDPTRL AVSAVDLNLK LMRWRALPSL NLNVLSSVKC
     LLLGAGTLGC QVARTLMGWG IRNITFVDYG KVAMSNPVRQ SLYNFEDCLG RGEFKAVAAV
     KSLKQIFPAM ETSGVVMAIP MPGHPISSQE EDSVLGDCKR LSELIESHDA VFLLTDTRES
     RWLPSLLCAN ANKIAINAAL GFDSYMVMRH GAGPTSLSDD MQNLDINKTN TQRLGCYFCN
     DVVAPQDSMT DRTLDQQCTV TRPGLAPIAG ALAVELLVGV LQHPLGINAK GDNSSLSNTG
     NNDDSPLGIL PHQIRGSVSQ FSQITLLGQA SNSCTACSET VISEYRERGN SFILEAINHP
     TYLEDLTGLT ELKKAANSFN LDWEDDDTDD DDVAVDL
//