ATG8D_ARATH
ID ATG8D_ARATH Reviewed; 120 AA.
AC Q9SL04; Q8LBA9;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Autophagy-related protein 8d;
DE AltName: Full=Autophagy-related ubiquitin-like modifier ATG8d;
DE Short=AtAPG8d;
DE Short=Protein autophagy 8d;
DE Flags: Precursor;
GN Name=ATG8D; Synonyms=APG8D; OrderedLocusNames=At2g05630; ORFNames=T20G20.2;
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 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.
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 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:0000250|UniProtKB:Q8LEM4}.
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=Q9SL04-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Constitutively expressed.
CC {ECO:0000269|PubMed:15494556}.
CC -!- PTM: The C-terminal 3 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}.
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DR EMBL; AB073178; BAB88390.1; -; mRNA.
DR EMBL; AC006220; AAD24645.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05958.1; -; Genomic_DNA.
DR EMBL; BT003090; AAO23655.1; -; mRNA.
DR EMBL; AK227339; BAE99350.1; -; mRNA.
DR EMBL; AY087320; AAM64870.1; -; mRNA.
DR PIR; H84470; H84470.
DR RefSeq; NP_178631.1; NM_126586.4. [Q9SL04-1]
DR AlphaFoldDB; Q9SL04; -.
DR SMR; Q9SL04; -.
DR BioGRID; 512; 14.
DR IntAct; Q9SL04; 11.
DR PRIDE; Q9SL04; -.
DR ProteomicsDB; 246548; -. [Q9SL04-1]
DR EnsemblPlants; AT2G05630.1; AT2G05630.1; AT2G05630. [Q9SL04-1]
DR GeneID; 815112; -.
DR Gramene; AT2G05630.1; AT2G05630.1; AT2G05630. [Q9SL04-1]
DR KEGG; ath:AT2G05630; -.
DR Araport; AT2G05630; -.
DR HOGENOM; CLU_119276_0_1_1; -.
DR InParanoid; Q9SL04; -.
DR OMA; AHDQDIS; -.
DR PhylomeDB; Q9SL04; -.
DR PRO; PR:Q9SL04; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SL04; baseline and differential.
DR Genevisible; Q9SL04; 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 8d"
FT /id="PRO_0000286911"
FT PROPEP 118..120
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q2XPP5"
FT /id="PRO_0000286912"
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"
FT CONFLICT 47
FT /note="R -> K (in Ref. 6; AAM64870)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 120 AA; 13907 MW; D906A366B1E090F2 CRC64;
MAISSFKHEH PLEKRQAEAA RIREKYPDRI PVIVERAEKS DVPDIDRKKY LVPADLTVGQ
FVYVVRKRIK LSPEKAIFIF VKNILPPTAA IMSAIYEEHK DEDGFLYMSY SGENTFGIFF
