ATG7_ARATH
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 25-MAY-2022, entry version 133.
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.AT5G45900.1; -.
DR TCDB; 9.A.15.3.1; the autophagy-related phagophore-formation transporter (apt) family.
DR PaxDb; Q94CD5; -.
DR PRIDE; Q94CD5; -.
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; locus:2152375; AT5G45900.
DR eggNOG; KOG2337; Eukaryota.
DR HOGENOM; CLU_012998_2_1_1; -.
DR InParanoid; Q94CD5; -.
DR OMA; VQTWRYS; -.
DR OrthoDB; 549762at2759; -.
DR PhylomeDB; Q94CD5; -.
DR PRO; PR:Q94CD5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94CD5; baseline and differential.
DR Genevisible; Q94CD5; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0019778; F:Atg12 activating enzyme activity; IBA:GO_Central.
DR GO; GO:0019779; F:Atg8 activating enzyme activity; ISS:TAIR.
DR GO; GO:0007568; P:aging; IMP:TAIR.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; ISS:TAIR.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0006501; P:C-terminal protein lipidation; IBA:GO_Central.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IEP:TAIR.
DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR GO; GO:0006497; P:protein lipidation; ISS:TAIR.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.140.100; -; 1.
DR Gene3D; 3.40.140.70; -; 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 PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF16420; ATG7_N; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
DR TIGRFAMs; TIGR01381; E1_like_apg7; 1.
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
