ATG11_ARATH
ID ATG11_ARATH Reviewed; 1148 AA.
AC Q9SUG7;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Autophagy-related protein 11 {ECO:0000303|PubMed:24563201};
GN Name=ATG11 {ECO:0000303|PubMed:24563201};
GN OrderedLocusNames=At4g30790 {ECO:0000312|Araport:AT4G30790};
GN ORFNames=T10C21.140 {ECO:0000312|EMBL:CAB52452.1};
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 [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 [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-851, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [4]
RP FUNCTION, SUBUNIT, INTERACTION WITH ATG8E; ATG13A AND ATG101, SUBCELLULAR
RP LOCATION, AIM MOTIF, AND DISRUPTION PHENOTYPE.
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: Accessory protein involved in autophagy. Acts as scaffold
CC protein of the ATG1-ATG13 complex for faithful delivery of autophagic
CC vesicles to the vacuole. Involved in the stress-induced phosphorylation
CC of ATG1A for turnover of ATG1-ATG13 complex and proper ATG1-ATG13
CC complex assembly or activity. Required for selective mitophagy.
CC Required for senescence-induced breakdown of mitochondria-resident
CC proteins and mitochondrial vesicles. Seems not essential for ATG8-
CC mediated autophagy. {ECO:0000269|PubMed:24563201}.
CC -!- SUBUNIT: Homodimer. Interacts with ATG8E, ATG13A and ATG101. Binds to
CC ATG8E on autophagic vesicles. {ECO:0000269|PubMed:24563201}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome
CC {ECO:0000269|PubMed:24563201}.
CC -!- DISRUPTION PHENOTYPE: Mutant plants are hypersensitive to nitrogen or
CC carbon starvation and show early senescence.
CC {ECO:0000269|PubMed:24563201}.
CC -!- SIMILARITY: Belongs to the ATG11 family. {ECO:0000305}.
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DR EMBL; AL109787; CAB52452.1; -; Genomic_DNA.
DR EMBL; AL161577; CAB79797.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85809.1; -; Genomic_DNA.
DR PIR; D85360; D85360.
DR RefSeq; NP_194808.1; NM_119225.3.
DR AlphaFoldDB; Q9SUG7; -.
DR STRING; 3702.AT4G30790.1; -.
DR iPTMnet; Q9SUG7; -.
DR PaxDb; Q9SUG7; -.
DR PRIDE; Q9SUG7; -.
DR ProteomicsDB; 246828; -.
DR EnsemblPlants; AT4G30790.1; AT4G30790.1; AT4G30790.
DR GeneID; 829202; -.
DR Gramene; AT4G30790.1; AT4G30790.1; AT4G30790.
DR KEGG; ath:AT4G30790; -.
DR Araport; AT4G30790; -.
DR TAIR; locus:2131944; AT4G30790.
DR eggNOG; ENOG502QUG9; Eukaryota.
DR HOGENOM; CLU_007054_0_0_1; -.
DR InParanoid; Q9SUG7; -.
DR OMA; GLRWYLI; -.
DR OrthoDB; 78873at2759; -.
DR PhylomeDB; Q9SUG7; -.
DR PRO; PR:Q9SUG7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SUG7; baseline and differential.
DR Genevisible; Q9SUG7; AT.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IBA:GO_Central.
DR GO; GO:0005776; C:autophagosome; IMP:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IMP:UniProtKB.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:UniProtKB.
DR GO; GO:0030242; P:autophagy of peroxisome; IBA:GO_Central.
DR GO; GO:0010150; P:leaf senescence; IMP:UniProtKB.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
DR InterPro; IPR040040; ATG11.
DR InterPro; IPR019460; Atg11_C.
DR InterPro; IPR045326; ATG17-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR13222; PTHR13222; 1.
DR Pfam; PF10377; ATG11; 1.
DR Pfam; PF04108; ATG17_like; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
PE 1: Evidence at protein level;
KW Autophagy; Coiled coil; Cytoplasmic vesicle; Phosphoprotein;
KW Protein transport; Reference proteome; Stress response; Transport.
FT CHAIN 1..1148
FT /note="Autophagy-related protein 11"
FT /id="PRO_0000434625"
FT REGION 699..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 816..868
FT /evidence="ECO:0000255"
FT COILED 956..996
FT /evidence="ECO:0000255"
FT MOTIF 567..570
FT /note="AIM (Atg8-family-interacting motif)"
FT /evidence="ECO:0000305|PubMed:24563201"
FT MOTIF 1130..1133
FT /note="AIM (Atg8-family-interacting motif)"
FT /evidence="ECO:0000305|PubMed:24563201"
FT MOD_RES 851
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19245862"
SQ SEQUENCE 1148 AA; 129184 MW; 2F343F650DE4B537 CRC64;
MSGSFTESFA DDGKLLLCVA ENGHSFEFQC SETTSVESVM RFVESVSGIA LSDQLLLSLD
MKLEPQKLLS AFGLPASDRE VFVFNKAMLQ SNSHPPSPED VDLQDVADAL PPASLHEHHP
LDDASDPALK ALPLYERQFR YHFHKGRTIY NCTVVKHENC ERLTREQKVQ QRAVEVATRN
LEQYYRVIYQ NFLEFMKRYK HQHRLHSDLL MNFGRDIEKL RSAKIHPYLQ TESRKCLLDF
VKEDNLKKAV ENCASSHRQF ENKIAQFQQM FVEVKRKVEE LFACRASLSM KNLEVTVKDH
ERFIDEEKSI MQSLSKDVNT VKKLVDDCMS SQVSSSLRPH DAVSALGPMY EVHDKNHLPK
MQACYNSISE LLDFCKNKKN EMNNFVHGYM QKITYVTYII KDAKLQFPVF REAMVRQDDL
FADLKLVRGV GPAYRACLAE VVRRKASMKL YMGMAGQLAE KLAMKRETEV RKREEFLKTH
GPFVPRDVLA SMGLYDTPTQ CDVNVAPYDT SLLNIEISDV DRYAPEFLVG LHSKIASLKS
SLTMSGDSSL SAEPEEIGID TFDKDNFDDI LAASELIEIA GTSKMEVENA KLKADLASAI
SRICSLGPQF EYEVLDESEV ENVLKNAADK TAEALQAKDE YEKHLLLMLK EKQMHCDSYE
KRIRELEQRL SDEYLQGQRH NNKDVSGLNL MHEKVSEYKA EASSDVEGNK THVSGSEPMD
EVSCVSNLTS KQPCKAREGM DENMVDSSQV LSQPLDSSML ESQQNNEKGG KDSEAGEMGV
FLSNSSTAES PQKSLDDNVA TGRGLDAKDS GDIILELRNE LMEKSNKLSE MESKLNGAME
EVSNLSRELE TNQKLLEESQ MNCAHLENCL HEAREEAQTH LCAADRRASQ YTALRASAVK
MRGLFERFRS SVCAGSGIAD FADSLRTLAQ ALANSVNENE DDGTTEFRKC IRVLADKVSF
LSKHREELLE KCQNLEATSE QTRKDLEEKK ELVKTLYTKH QLGKQANKEK ISFGRLEVHE
IAAFVLNQAG HYEAINRNCP NYYLSSESEA LFTDHLPSRP TYIVGQIVHI ERQIVKLPSQ
LSASASPEAG KTHHLCSDQG SRTLASSSIS TSTSATTTSN PYGLSSGCEY FIVTIAMLPD
TAIHQQAS
