ATG8B_ARATH
ID ATG8B_ARATH Reviewed; 122 AA.
AC Q9XEB5;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Autophagy-related protein 8b;
DE AltName: Full=Autophagy-related ubiquitin-like modifier ATG8b;
DE Short=AtAPG8b;
DE Short=Protein autophagy 8b;
DE Flags: Precursor;
GN Name=ATG8B; Synonyms=APG8B; OrderedLocusNames=At4g04620; ORFNames=F4H6.14;
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=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 [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 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 [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).
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). {ECO:0000250|UniProtKB:Q8LEM4,
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 -!- TISSUE SPECIFICITY: Constitutively expressed.
CC {ECO:0000269|PubMed:15494556}.
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}.
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DR EMBL; AB073176; BAB88388.1; -; mRNA.
DR EMBL; AF074021; AAD29776.1; -; Genomic_DNA.
DR EMBL; AL161501; CAB80827.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82404.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82405.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67912.1; -; Genomic_DNA.
DR EMBL; BT006385; AAP21193.1; -; mRNA.
DR EMBL; AK227679; BAE99666.1; -; mRNA.
DR EMBL; AY084859; AAM61423.1; -; mRNA.
DR PIR; C85058; C85058.
DR RefSeq; NP_001329707.1; NM_001340494.1.
DR RefSeq; NP_192371.1; NM_116700.2.
DR RefSeq; NP_849298.1; NM_178967.4.
DR AlphaFoldDB; Q9XEB5; -.
DR SMR; Q9XEB5; -.
DR BioGRID; 11105; 5.
DR IntAct; Q9XEB5; 6.
DR STRING; 3702.AT4G04620.1; -.
DR PaxDb; Q9XEB5; -.
DR PRIDE; Q9XEB5; -.
DR ProteomicsDB; 246550; -.
DR EnsemblPlants; AT4G04620.1; AT4G04620.1; AT4G04620.
DR EnsemblPlants; AT4G04620.2; AT4G04620.2; AT4G04620.
DR EnsemblPlants; AT4G04620.3; AT4G04620.3; AT4G04620.
DR GeneID; 825794; -.
DR Gramene; AT4G04620.1; AT4G04620.1; AT4G04620.
DR Gramene; AT4G04620.2; AT4G04620.2; AT4G04620.
DR Gramene; AT4G04620.3; AT4G04620.3; AT4G04620.
DR KEGG; ath:AT4G04620; -.
DR Araport; AT4G04620; -.
DR TAIR; locus:2125791; AT4G04620.
DR eggNOG; KOG1654; Eukaryota.
DR HOGENOM; CLU_119276_0_1_1; -.
DR InParanoid; Q9XEB5; -.
DR OMA; CTRERRQ; -.
DR OrthoDB; 1508198at2759; -.
DR PhylomeDB; Q9XEB5; -.
DR PRO; PR:Q9XEB5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9XEB5; baseline and differential.
DR Genevisible; Q9XEB5; 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 Autophagy; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Lipoprotein;
KW Membrane; Microtubule; Protein transport; Reference proteome; Transport;
KW Ubl conjugation pathway; Vacuole.
FT CHAIN 1..117
FT /note="Autophagy-related protein 8b"
FT /id="PRO_0000286907"
FT PROPEP 118..122
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q2XPP5"
FT /id="PRO_0000286908"
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; 13880 MW; BAC932F997E760CF CRC64;
MEKNSFKLSN PLEMRMAEST RIRAKYPERV PVIVEKAGQS DVPDIDKKKY LVPADLTIGQ
FVYVVRKRIK LGAEKAIFVF VKNTLPPTAA LMSAIYEEHK DEDGFLYMTY SGENTFGGSF
YC
