ATG8A_ARATH
ID ATG8A_ARATH Reviewed; 122 AA.
AC Q8LEM4; O65447; Q8S928;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Autophagy-related protein 8a;
DE AltName: Full=Autophagy-related ubiquitin-like modifier ATG8a;
DE Short=AtAPG8a;
DE Short=Protein autophagy 8a;
DE Flags: Precursor;
GN Name=ATG8A; Synonyms=APG8A; OrderedLocusNames=At4g21980; ORFNames=F1N20.80;
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].
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 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.
RN [7]
RP INTERACTION WITH ATG4B, AND BINDING TO MICROTUBULES.
RX PubMed=15178341; DOI=10.1016/j.febslet.2004.04.088;
RA Ketelaar T., Voss C., Dimmock S.A., Thumm M., Hussey P.J.;
RT "Arabidopsis homologues of the autophagy protein Atg8 are a novel family of
RT microtubule binding proteins.";
RL FEBS Lett. 567:302-306(2004).
RN [8]
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 [9]
RP INDUCTION.
RX PubMed=16157655; DOI=10.1093/jxb/eri276;
RA Slavikova S., Shy G., Yao Y., Glozman R., Levanony H., Pietrokovski S.,
RA Elazar Z., Galili G.;
RT "The autophagy-associated Atg8 gene family operates both under favourable
RT growth conditions and under starvation stresses in Arabidopsis plants.";
RL J. Exp. Bot. 56:2839-2849(2005).
RN [10]
RP INTERACTION WITH NBR1.
RX PubMed=21606687; DOI=10.4161/auto.7.9.16389;
RA Svenning S., Lamark T., Krause K., Johansen T.;
RT "Plant NBR1 is a selective autophagy substrate and a functional hybrid of
RT the mammalian autophagic adapters NBR1 and p62/SQSTM1.";
RL Autophagy 7:993-1010(2011).
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 ATG4B (PubMed:15178341). Interacts with NBR1
CC (PubMed:21606687). {ECO:0000269|PubMed:15178341,
CC ECO:0000269|PubMed:21606687}.
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:0000269|PubMed:15178341}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8LEM4-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Constitutively expressed.
CC {ECO:0000269|PubMed:15494556}.
CC -!- INDUCTION: Induced by sugar starvation. {ECO:0000269|PubMed:16157655}.
CC -!- PTM: The C-terminal 5 residues are removed by ATG4 to expose Gly-117 at
CC the C-terminus. This Gly-117 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18101.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79153.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF492759; AAM70188.1; -; mRNA.
DR EMBL; AB073175; BAB88387.1; -; mRNA.
DR EMBL; AL022140; CAA18101.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161556; CAB79153.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84537.1; -; Genomic_DNA.
DR EMBL; BT002024; AAN72035.1; -; mRNA.
DR EMBL; BT006522; AAP21330.1; -; mRNA.
DR EMBL; AY085349; AAM62580.1; -; mRNA.
DR PIR; T49105; T49105.
DR RefSeq; NP_567642.1; NM_118319.4. [Q8LEM4-1]
DR AlphaFoldDB; Q8LEM4; -.
DR BMRB; Q8LEM4; -.
DR SMR; Q8LEM4; -.
DR BioGRID; 13576; 5.
DR STRING; 3702.AT4G21980.2; -.
DR PaxDb; Q8LEM4; -.
DR PRIDE; Q8LEM4; -.
DR EnsemblPlants; AT4G21980.1; AT4G21980.1; AT4G21980. [Q8LEM4-1]
DR GeneID; 828287; -.
DR Gramene; AT4G21980.1; AT4G21980.1; AT4G21980. [Q8LEM4-1]
DR KEGG; ath:AT4G21980; -.
DR Araport; AT4G21980; -.
DR eggNOG; KOG1654; Eukaryota.
DR HOGENOM; CLU_119276_0_1_1; -.
DR InParanoid; Q8LEM4; -.
DR PhylomeDB; Q8LEM4; -.
DR PRO; PR:Q8LEM4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8LEM4; baseline and differential.
DR Genevisible; Q8LEM4; AT.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
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 Alternative splicing; Autophagy; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Lipoprotein; Membrane; Microtubule; Protein transport;
KW Reference proteome; Transport; Ubl conjugation pathway; Vacuole.
FT CHAIN 1..117
FT /note="Autophagy-related protein 8a"
FT /id="PRO_0000286905"
FT PROPEP 118..122
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q2XPP5"
FT /id="PRO_0000286906"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 117..118
FT /note="Cleavage; by ATG4"
FT /evidence="ECO:0000250|UniProtKB:Q2XPP5"
FT LIPID 117
FT /note="Phosphatidylethanolamine amidated glycine"
FT /evidence="ECO:0000250|UniProtKB:P38182"
SQ SEQUENCE 122 AA; 13695 MW; 9F04845BD559349B CRC64;
MAKSSFKISN PLEARMSESS RIREKYPDRI PVIVEKAGQS DVPDIDKKKY LVPADLTVGQ
FVYVVRKRIK LGAEKAIFVF VKNTLPPTAA LMSAIYEEHK DEDGFLYMTY SGENTFGSLT
VA
