ATG3_ARATH
ID ATG3_ARATH Reviewed; 313 AA.
AC Q0WWQ1; Q8L982; Q8S930; Q9FKG9;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Autophagy-related protein 3;
DE AltName: Full=Autophagy-related E2-like conjugation enzyme ATG3;
DE Short=AtAPG3;
DE Short=Protein autophagy 3;
GN Name=ATG3; Synonyms=APG3; OrderedLocusNames=At5g61500; ORFNames=K11J9.3;
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], 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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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 Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E2 conjugating enzyme responsible for the E2-like covalent
CC binding of phosphatidylethanolamine to the C-terminal Gly of ATG8. This
CC step is required for the membrane association of ATG8. The formation of
CC the ATG8-phosphatidylethanolamine conjugate is essential for autophagy
CC and for the cytoplasm to vacuole transport (Cvt).
CC -!- SUBUNIT: Interacts with ATG8 through an intermediate thioester bond
CC between Cys-258 and the C-terminal Gly of ATG8. Also interacts with the
CC C-terminal region of the E1-like ATG7 enzyme (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q0WWQ1; Q9LVK3: ATG12B; NbExp=2; IntAct=EBI-8276607, EBI-8276588;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATG3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08995.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB073170; BAB88382.1; -; mRNA.
DR EMBL; AB012239; BAB08995.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97476.1; -; Genomic_DNA.
DR EMBL; BT024713; ABD59051.1; -; mRNA.
DR EMBL; AK226290; BAE98447.1; -; mRNA.
DR EMBL; AY088587; AAM66117.1; -; mRNA.
DR RefSeq; NP_568934.1; NM_125543.5.
DR PDB; 3VX8; X-ray; 3.11 A; B/C=26-313.
DR PDB; 7EU4; X-ray; 3.20 A; O/P/Q/R=152-162.
DR PDBsum; 3VX8; -.
DR PDBsum; 7EU4; -.
DR AlphaFoldDB; Q0WWQ1; -.
DR SMR; Q0WWQ1; -.
DR BioGRID; 21515; 3.
DR IntAct; Q0WWQ1; 1.
DR MINT; Q0WWQ1; -.
DR STRING; 3702.AT5G61500.1; -.
DR TCDB; 9.A.15.3.1; the autophagy-related phagophore-formation transporter (apt) family.
DR PaxDb; Q0WWQ1; -.
DR PRIDE; Q0WWQ1; -.
DR ProteomicsDB; 246736; -.
DR DNASU; 836271; -.
DR EnsemblPlants; AT5G61500.1; AT5G61500.1; AT5G61500.
DR GeneID; 836271; -.
DR Gramene; AT5G61500.1; AT5G61500.1; AT5G61500.
DR KEGG; ath:AT5G61500; -.
DR Araport; AT5G61500; -.
DR TAIR; locus:2151566; AT5G61500.
DR eggNOG; KOG2981; Eukaryota.
DR HOGENOM; CLU_027518_0_0_1; -.
DR OMA; YDKYYQV; -.
DR OrthoDB; 1432328at2759; -.
DR PhylomeDB; Q0WWQ1; -.
DR PRO; PR:Q0WWQ1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q0WWQ1; baseline and differential.
DR Genevisible; Q0WWQ1; AT.
DR GO; GO:0000153; C:cytoplasmic ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0019776; F:Atg8 ligase activity; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR007135; Atg3/Atg10.
DR PANTHER; PTHR12866; PTHR12866; 1.
DR Pfam; PF03987; Autophagy_act_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Cytoplasm; Protein transport; Reference proteome;
KW Transport; Ubl conjugation pathway.
FT CHAIN 1..313
FT /note="Autophagy-related protein 3"
FT /id="PRO_0000286937"
FT REGION 103..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 258
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255"
FT CONFLICT 203
FT /note="K -> E (in Ref. 5; BAE98447)"
FT /evidence="ECO:0000305"
FT HELIX 26..30
FT /evidence="ECO:0007829|PDB:3VX8"
FT HELIX 35..48
FT /evidence="ECO:0007829|PDB:3VX8"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:3VX8"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:3VX8"
FT STRAND 71..80
FT /evidence="ECO:0007829|PDB:3VX8"
FT STRAND 193..202
FT /evidence="ECO:0007829|PDB:3VX8"
FT TURN 203..206
FT /evidence="ECO:0007829|PDB:3VX8"
FT STRAND 207..215
FT /evidence="ECO:0007829|PDB:3VX8"
FT HELIX 224..229
FT /evidence="ECO:0007829|PDB:3VX8"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:3VX8"
FT STRAND 246..255
FT /evidence="ECO:0007829|PDB:3VX8"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3VX8"
FT HELIX 260..274
FT /evidence="ECO:0007829|PDB:3VX8"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:3VX8"
FT HELIX 283..291
FT /evidence="ECO:0007829|PDB:3VX8"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:3VX8"
SQ SEQUENCE 313 AA; 35332 MW; D6357AE8646FEC2E CRC64;
MVLSQKLHEA FKGTVERITG PRTISAFKEK GVLSVSEFVL AGDNLVSKCP TWSWESGDAS
KRKPYLPSDK QFLITRNVPC LRRAASVAED YEAAGGEVLV DDEDNDGWLA THGKPKDKGK
EEDNLPSMDA LDINEKNTIQ SIPTYFGGEE DDDIPDMEEF DEADNVVEND PATLQSTYLV
AHEPDDDNIL RTRTYDLSIT YDKYYQTPRV WLTGYDESRM LLQPELVMED VSQDHARKTV
TIEDHPHLPG KHASVHPCRH GAVMKKIIDV LMSRGVEPEV DKYLFLFLKF MASVIPTIEY
DYTMDFDLGS SST
