ATG8E_ARATH
ID ATG8E_ARATH Reviewed; 122 AA.
AC Q8S926; Q945K6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Autophagy-related protein 8e;
DE AltName: Full=Autophagy-related ubiquitin-like modifier ATG8e;
DE Short=AtAPG8e;
DE Short=Protein autophagy 8e;
DE Flags: Precursor;
GN Name=ATG8E; Synonyms=APG8E; OrderedLocusNames=At2g45170;
GN ORFNames=F4L23, T14P1.2;
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=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;
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 [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).
RN [6]
RP INTERACTION WITH SH3P2.
RX PubMed=24249832; DOI=10.1105/tpc.113.118307;
RA Zhuang X., Wang H., Lam S.K., Gao C., Wang X., Cai Y., Jiang L.;
RT "A BAR-domain protein SH3P2, which binds to phosphatidylinositol 3-
RT phosphate and ATG8, regulates autophagosome formation in Arabidopsis.";
RL Plant Cell 25:4596-4615(2013).
RN [7]
RP INTERACTION WITH ATG1A AND ATG11.
RX PubMed=24563201; DOI=10.1105/tpc.113.120014;
RA Li F., Chung T., Vierstra R.D.;
RT "AUTOPHAGY-RELATED11 plays a critical role in general autophagy- and
RT senescence-induced mitophagy in Arabidopsis.";
RL Plant Cell 26:788-807(2014).
CC -!- FUNCTION: Ubiquitin-like modifier involved in autophagosomes formation.
CC May mediate the delivery of the autophagosomes to the vacuole via the
CC microtubule cytoskeleton. {ECO:0000250|UniProtKB:P38182}.
CC -!- SUBUNIT: Interacts with ATG4 (By similarity). Interacts with SH3P2
CC (PubMed:24249832). Interacts with ATG1A and ATG11. Binds to ATG1A and
CC ATG11 on autophagic vesicles (PubMed:24563201).
CC {ECO:0000250|UniProtKB:Q9SL04, ECO:0000269|PubMed:24249832,
CC ECO:0000269|PubMed:24563201}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000250|UniProtKB:P38182}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P38182}. Vacuole membrane
CC {ECO:0000250|UniProtKB:P38182}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P38182}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q8LEM4}.
CC -!- TISSUE SPECIFICITY: Constitutively expressed.
CC {ECO:0000269|PubMed:15494556}.
CC -!- PTM: The C-terminal 4 residues are removed by ATG4 to expose Gly-118 at
CC the C-terminus. This Gly-118 forms then a thioester bond with the 'Cys-
CC 558' of ATG7 (E1-like activating enzyme) before being transferred to
CC the 'Cys-258' of ATG3 (the specific E2 conjugating enzyme), in order to
CC be finally amidated with phosphatidylethanolamine. This lipid
CC modification anchors ATG8 to autophagosomes.
CC {ECO:0000250|UniProtKB:P38182}.
CC -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
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DR EMBL; AB073179; BAB88391.1; -; mRNA.
DR EMBL; AC002387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002685; AEC10520.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10521.1; -; Genomic_DNA.
DR EMBL; AF412106; AAL06559.1; -; mRNA.
DR EMBL; AY074388; AAL67084.1; -; mRNA.
DR PIR; C84887; C84887.
DR RefSeq; NP_182042.2; NM_130080.6.
DR RefSeq; NP_850431.2; NM_180100.7.
DR AlphaFoldDB; Q8S926; -.
DR SMR; Q8S926; -.
DR BioGRID; 4461; 4.
DR STRING; 3702.AT2G45170.2; -.
DR PaxDb; Q8S926; -.
DR PRIDE; Q8S926; -.
DR ProteomicsDB; 246620; -.
DR EnsemblPlants; AT2G45170.1; AT2G45170.1; AT2G45170.
DR EnsemblPlants; AT2G45170.2; AT2G45170.2; AT2G45170.
DR GeneID; 819125; -.
DR Gramene; AT2G45170.1; AT2G45170.1; AT2G45170.
DR Gramene; AT2G45170.2; AT2G45170.2; AT2G45170.
DR KEGG; ath:AT2G45170; -.
DR Araport; AT2G45170; -.
DR TAIR; locus:2055537; AT2G45170.
DR eggNOG; KOG1654; Eukaryota.
DR HOGENOM; CLU_119276_0_1_1; -.
DR OMA; FKMDNDF; -.
DR OrthoDB; 1508198at2759; -.
DR PRO; PR:Q8S926; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8S926; baseline and differential.
DR Genevisible; Q8S926; AT.
DR GO; GO:0005776; C:autophagosome; IDA:TAIR.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; IEP:TAIR.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0045471; P:response to ethanol; IDA:TAIR.
DR InterPro; IPR004241; Atg8-like.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10969; PTHR10969; 1.
DR Pfam; PF02991; ATG8; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
PE 1: Evidence at protein level;
KW Autophagy; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Lipoprotein;
KW Membrane; Microtubule; Protein transport; Reference proteome; Transport;
KW Ubl conjugation pathway; Vacuole.
FT CHAIN 1..118
FT /note="Autophagy-related protein 8e"
FT /id="PRO_0000286913"
FT PROPEP 119..122
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q2XPP5"
FT /id="PRO_0000286914"
FT SITE 118..119
FT /note="Cleavage; by ATG4"
FT /evidence="ECO:0000250|UniProtKB:Q2XPP5"
FT LIPID 118
FT /note="Phosphatidylethanolamine amidated glycine"
FT /evidence="ECO:0000250|UniProtKB:P38182"
FT CONFLICT 11
FT /note="N -> D (in Ref. 1; BAB88391)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 122 AA; 13947 MW; AA504855340CE173 CRC64;
MNKGSIFKMD NDFEKRKAEA GRIREKYPDR IPVIVEKAEK SEVPNIDKKK YLVPSDLTVG
QFVYVIRKRI KLSAEKAIFI FVDNVLPPTG ELMSSVYEDK KDEDGFLYIT YSGENTFGAS
SI
