ATG8F_ARATH
ID ATG8F_ARATH Reviewed; 121 AA.
AC Q8VYK7; O23496;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Autophagy-related protein 8f;
DE AltName: Full=Autophagy-related ubiquitin-like modifier ATG8f;
DE Short=AtAPG8f;
DE Short=Protein autophagy 8f;
DE Flags: Precursor;
GN Name=ATG8F; Synonyms=APG8F; OrderedLocusNames=At4g16520;
GN ORFNames=dl4285c, FCAALL.383;
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
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 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 [7]
RP SUBCELLULAR LOCATION.
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 [8]
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).
RN [9]
RP INTERACTION WITH ATI1 AND ATI2.
RX PubMed=22253227; DOI=10.1105/tpc.111.093112;
RA Honig A., Avin-Wittenberg T., Ufaz S., Galili G.;
RT "A new type of compartment, defined by plant-specific Atg8-interacting
RT proteins, is induced upon exposure of Arabidopsis plants to carbon
RT starvation.";
RL Plant Cell 24:288-303(2012).
RN [10]
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).
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 NBR1
CC (PubMed:21606687). Interacts with ATI1 and ATI2 (PubMed:22253227).
CC Interacts with SH3P2 (PubMed:24249832). {ECO:0000250|UniProtKB:Q9SL04,
CC ECO:0000269|PubMed:21606687, ECO:0000269|PubMed:22253227,
CC ECO:0000269|PubMed:24249832}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000269|PubMed:16157655}; Lipid-anchor
CC {ECO:0000269|PubMed:16157655}. Vacuole membrane
CC {ECO:0000269|PubMed:16157655}; Lipid-anchor
CC {ECO:0000269|PubMed:16157655}. 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-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=CAB10428.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78694.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB073180; BAB88392.1; -; mRNA.
DR EMBL; Z97341; CAB10428.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161544; CAB78694.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83764.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83765.1; -; Genomic_DNA.
DR EMBL; AY070464; AAL49930.1; -; mRNA.
DR EMBL; AY091667; AAM10266.1; -; mRNA.
DR PIR; B71432; B71432.
DR RefSeq; NP_567504.1; NM_117751.4.
DR RefSeq; NP_849395.1; NM_179064.2.
DR PDB; 7DHT; NMR; -; A=1-121.
DR PDBsum; 7DHT; -.
DR AlphaFoldDB; Q8VYK7; -.
DR SMR; Q8VYK7; -.
DR BioGRID; 12644; 12.
DR IntAct; Q8VYK7; 9.
DR STRING; 3702.AT4G16520.2; -.
DR PaxDb; Q8VYK7; -.
DR PRIDE; Q8VYK7; -.
DR ProteomicsDB; 246621; -.
DR EnsemblPlants; AT4G16520.1; AT4G16520.1; AT4G16520.
DR EnsemblPlants; AT4G16520.2; AT4G16520.2; AT4G16520.
DR GeneID; 827351; -.
DR Gramene; AT4G16520.1; AT4G16520.1; AT4G16520.
DR Gramene; AT4G16520.2; AT4G16520.2; AT4G16520.
DR KEGG; ath:AT4G16520; -.
DR Araport; AT4G16520; -.
DR TAIR; locus:2130759; AT4G16520.
DR eggNOG; KOG1654; Eukaryota.
DR HOGENOM; CLU_119276_0_1_1; -.
DR InParanoid; Q8VYK7; -.
DR OMA; AKMKWMF; -.
DR OrthoDB; 1508198at2759; -.
DR PhylomeDB; Q8VYK7; -.
DR PRO; PR:Q8VYK7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8VYK7; baseline and differential.
DR Genevisible; Q8VYK7; AT.
DR GO; GO:0005776; C:autophagosome; IDA:TAIR.
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 3D-structure; Autophagy; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Lipoprotein; Membrane; Microtubule; Protein transport; Reference proteome;
KW Transport; Ubl conjugation pathway; Vacuole.
FT CHAIN 1..117
FT /note="Autophagy-related protein 8f"
FT /id="PRO_0000286915"
FT PROPEP 118..121
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q2XPP5"
FT /id="PRO_0000286916"
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 TURN 6..8
FT /evidence="ECO:0007829|PDB:7DHT"
FT HELIX 12..25
FT /evidence="ECO:0007829|PDB:7DHT"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:7DHT"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:7DHT"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:7DHT"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:7DHT"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:7DHT"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:7DHT"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:7DHT"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:7DHT"
SQ SEQUENCE 121 AA; 13762 MW; CBC5FD9D4A201DEC CRC64;
MAKSSFKQEH DLEKRRAEAA RIREKYPDRI PVIVEKAEKS DIPTIDKKKY LVPADLTVGQ
FVYVIRKRIK LSAEKAIFIF VDNVLPPAGA LMSSVYEEKK DDDGFLYVTY SGENTFGFGS
P
