AT18A_ARATH
ID AT18A_ARATH Reviewed; 425 AA.
AC Q93VB2; Q3EAF7; Q9LZI8;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Autophagy-related protein 18a;
DE Short=AtATG18a;
DE AltName: Full=Protein PEROXISOME UNUSUAL POSITIONING 2 {ECO:0000305};
GN Name=ATG18A; Synonyms=PEUP2 {ECO:0000305}; OrderedLocusNames=At3g62770;
GN ORFNames=F26K9_200;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 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 [4]
RP GENE FAMILY, INDUCTION, FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15860012; DOI=10.1111/j.1365-313x.2005.02397.x;
RA Xiong Y., Contento A.L., Bassham D.C.;
RT "AtATG18a is required for the formation of autophagosomes during nutrient
RT stress and senescence in Arabidopsis thaliana.";
RL Plant J. 42:535-546(2005).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY METHYL VIOLOGEN.
RX PubMed=17098847; DOI=10.1104/pp.106.092106;
RA Xiong Y., Contento A.L., Nguyen P.Q., Bassham D.C.;
RT "Degradation of oxidized proteins by autophagy during oxidative stress in
RT Arabidopsis.";
RL Plant Physiol. 143:291-299(2007).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY SALT AND BY OSMOTIC
RP STRESS.
RX PubMed=19587533; DOI=10.4161/auto.5.7.9290;
RA Liu Y., Xiong Y., Bassham D.C.;
RT "Autophagy is required for tolerance of drought and salt stress in
RT plants.";
RL Autophagy 5:954-963(2009).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21332848; DOI=10.1111/j.1365-313x.2011.04546.x;
RA Lenz H.D., Haller E., Melzer E., Kober K., Wurster K., Stahl M.,
RA Bassham D.C., Vierstra R.D., Parker J.E., Bautor J., Molina A.,
RA Escudero V., Shindo T., van der Hoorn R.A., Gust A.A., Nuernberger T.;
RT "Autophagy differentially controls plant basal immunity to biotrophic and
RT necrotrophic pathogens.";
RL Plant J. 66:818-830(2011).
RN [8]
RP INTERACTION WITH WRKY33, SUBCELLULAR LOCATION, INDUCTION BY BOTRYTIS
RP CINEREA, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21395886; DOI=10.1111/j.1365-313x.2011.04553.x;
RA Lai Z., Wang F., Zheng Z., Fan B., Chen Z.;
RT "A critical role of autophagy in plant resistance to necrotrophic fungal
RT pathogens.";
RL Plant J. 66:953-968(2011).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21847024; DOI=10.4161/psb.6.9.16967;
RA Wang Y., Wu Y., Tang D.;
RT "The autophagy gene, ATG18a, plays a negative role in powdery mildew
RT resistance and mildew-induced cell death in Arabidopsis.";
RL Plant Signal. Behav. 6:1408-1410(2011).
RN [10]
RP INDUCTION BY WATER STRESS, AND FUNCTION.
RX PubMed=22532286; DOI=10.1007/s00425-012-1655-5;
RA Nakayama M., Kaneko Y., Miyazawa Y., Fujii N., Higashitani N., Wada S.,
RA Ishida H., Yoshimoto K., Shirasu K., Yamada K., Nishimura M., Takahashi H.;
RT "A possible involvement of autophagy in amyloplast degradation in columella
RT cells during hydrotropic response of Arabidopsis roots.";
RL Planta 236:999-1012(2012).
CC -!- FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis
CC and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
CC Required for autophagy by autophagosome formation during nutrient
CC deprivation, senescence and under abiotic stresses, including
CC oxidative, high salt and osmotic stress conditions. Cooperates with
CC jasmonate- and WRKY33-mediated signaling pathways in the regulation of
CC plant defense responses to necrotrophic pathogens.
CC {ECO:0000269|PubMed:15860012, ECO:0000269|PubMed:17098847,
CC ECO:0000269|PubMed:19587533, ECO:0000269|PubMed:21332848,
CC ECO:0000269|PubMed:21395886, ECO:0000269|PubMed:21847024,
CC ECO:0000269|PubMed:22532286}.
CC -!- SUBUNIT: Component of the PI(3,5)P2 regulatory complex at least
CC composed of ATG18, SAC/FIG4, FAB1 and VAC14 (By similarity). Interacts
CC with WRKY33. {ECO:0000250, ECO:0000269|PubMed:21395886}.
CC -!- INTERACTION:
CC Q93VB2; Q8S8P5: WRKY33; NbExp=3; IntAct=EBI-6510711, EBI-1392374;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21395886}. Nucleus
CC {ECO:0000269|PubMed:21395886}. Preautophagosomal structure membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Vacuole
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Note=Peripheral membrane protein of pre-autophagosomal structure (PAS)
CC and vacuole. {ECO:0000250}.
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=Q93VB2-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, flowers and leaves.
CC {ECO:0000269|PubMed:15860012}.
CC -!- INDUCTION: By sucrose and nitrogen starvation and during senescence. By
CC methyl viologen. By salt and osmotic stress. By necrotrophic fungal
CC pathogen B.cinerea. Up-regulated in response to both water stress and
CC hydrotropic stimulation. {ECO:0000269|PubMed:15860012,
CC ECO:0000269|PubMed:17098847, ECO:0000269|PubMed:19587533,
CC ECO:0000269|PubMed:21395886, ECO:0000269|PubMed:22532286}.
CC -!- DOMAIN: The first protein part may form a beta-propeller domain
CC involved in specific binding to phosphatidylinositol 3,5-bisphosphate
CC (PIP2), leading to the association of the protein to the membrane.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mutant is more sensitive to nutrient deprivation
CC conditions and exhibits an early senescence phenotype. Prevents
CC autophagosome formation during starvation. More sensitive to methyl
CC viologen (oxidative stress) treatment and accumulates a higher level of
CC oxidized proteins compared to wild type. High sensitivity to salt and
CC osmotic/drought stresses. Displays an enhanced resistance to the
CC powdery mildew pathogen G.cichoracearum with mildew-induced cell death
CC and an enhanced resistance to P.syringae DC3000 but shows an enhanced
CC susceptibility to infection with necrotrophic A.brassicicola and
CC B.cinerea pathogens. {ECO:0000269|PubMed:15860012,
CC ECO:0000269|PubMed:17098847, ECO:0000269|PubMed:19587533,
CC ECO:0000269|PubMed:21332848, ECO:0000269|PubMed:21395886,
CC ECO:0000269|PubMed:21847024}.
CC -!- SIMILARITY: Belongs to the WD repeat PROPPIN family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB83127.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL162651; CAB83127.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80389.1; -; Genomic_DNA.
DR EMBL; AY039545; AAK62600.1; -; mRNA.
DR EMBL; AY059169; AAL15394.1; -; mRNA.
DR PIR; T48066; T48066.
DR RefSeq; NP_567132.4; NM_116142.6. [Q93VB2-1]
DR AlphaFoldDB; Q93VB2; -.
DR SMR; Q93VB2; -.
DR IntAct; Q93VB2; 1.
DR STRING; 3702.AT3G62770.1; -.
DR TCDB; 9.A.15.3.1; the autophagy-related phagophore-formation transporter (apt) family.
DR iPTMnet; Q93VB2; -.
DR PaxDb; Q93VB2; -.
DR PRIDE; Q93VB2; -.
DR ProteomicsDB; 240975; -. [Q93VB2-1]
DR EnsemblPlants; AT3G62770.1; AT3G62770.1; AT3G62770. [Q93VB2-1]
DR GeneID; 825452; -.
DR Gramene; AT3G62770.1; AT3G62770.1; AT3G62770. [Q93VB2-1]
DR KEGG; ath:AT3G62770; -.
DR Araport; AT3G62770; -.
DR TAIR; locus:2081705; AT3G62770.
DR eggNOG; KOG2111; Eukaryota.
DR InParanoid; Q93VB2; -.
DR OMA; EWSVAKY; -.
DR PhylomeDB; Q93VB2; -.
DR PRO; PR:Q93VB2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q93VB2; baseline and differential.
DR Genevisible; Q93VB2; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IMP:UniProtKB.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IEP:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:TAIR.
DR GO; GO:0006497; P:protein lipidation; IBA:GO_Central.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006970; P:response to osmotic stress; IEP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR GO; GO:0042594; P:response to starvation; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Cytoplasm; Membrane; Nucleus;
KW Protein transport; Reference proteome; Repeat; Transport; Vacuole;
KW WD repeat.
FT CHAIN 1..425
FT /note="Autophagy-related protein 18a"
FT /id="PRO_0000421879"
FT REPEAT 73..111
FT /note="WD 1"
FT REPEAT 117..161
FT /note="WD 2"
FT REPEAT 246..286
FT /note="WD 3"
FT REPEAT 291..330
FT /note="WD 4"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 46800 MW; D99D2E757C22189C CRC64;
MATVSSSSWP NPNPNPDSTS ASDSDSTFPS HRDRVDEPDS LDSFSSMSLN SDEPNQTSNQ
SPLSPPTPNL PVMPPPSVLH LSFNQDHACF AVGTDRGFRI LNCDPFREIF RRDFDRGGGV
AVVEMLFRCN ILALVGGGPD PQYPPNKVMI WDDHQGRCIG ELSFRSDVRS VRLRRDRIIV
VLEQKIFVYN FSDLKLMHQI ETIANPKGLC AVSQGVGSMV LVCPGLQKGQ VRIEHYASKR
TKFVMAHDSR IACFALTQDG HLLATASSKG TLVRIFNTVD GTLRQEVRRG ADRAEIYSLA
FSSNAQWLAV SSDKGTVHVF GLKVNSGSQV KDSSRIAPDA TPSSPSSSLS LFKGVLPRYF
SSEWSVAQFR LVEGTQYIAA FGHQKNTVVI LGMDGSFYRC QFDPVNGGEM SQLEYHNCLK
PPSVF
