AT18D_ARATH
ID AT18D_ARATH Reviewed; 391 AA.
AC Q0WPK3; Q9LXZ6;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Autophagy-related protein 18d;
DE Short=AtATG18d;
GN Name=ATG18D; OrderedLocusNames=At3g56440; ORFNames=T5P19_90;
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;
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 [4]
RP GENE FAMILY, INDUCTION, AND TISSUE SPECIFICITY.
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).
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 similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the PI(3,5)P2 regulatory complex at least
CC composed of ATG18, SAC/FIG4, FAB1 and VAC14. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: 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 -!- TISSUE SPECIFICITY: Expressed in roots, stems, flowers and leaves.
CC {ECO:0000269|PubMed:15860012}.
CC -!- INDUCTION: Down-regulated during senescence.
CC {ECO:0000269|PubMed:15860012}.
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 -!- SIMILARITY: Belongs to the WD repeat PROPPIN family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB88047.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL163972; CAB88047.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79522.1; -; Genomic_DNA.
DR EMBL; AK229064; BAF00946.1; -; mRNA.
DR PIR; T49045; T49045.
DR RefSeq; NP_191203.2; NM_115502.4.
DR AlphaFoldDB; Q0WPK3; -.
DR SMR; Q0WPK3; -.
DR STRING; 3702.AT3G56440.1; -.
DR PaxDb; Q0WPK3; -.
DR PRIDE; Q0WPK3; -.
DR ProteomicsDB; 246821; -.
DR DNASU; 824811; -.
DR EnsemblPlants; AT3G56440.1; AT3G56440.1; AT3G56440.
DR GeneID; 824811; -.
DR Gramene; AT3G56440.1; AT3G56440.1; AT3G56440.
DR KEGG; ath:AT3G56440; -.
DR Araport; AT3G56440; -.
DR TAIR; locus:2102614; AT3G56440.
DR eggNOG; KOG2111; Eukaryota.
DR HOGENOM; CLU_025895_2_1_1; -.
DR InParanoid; Q0WPK3; -.
DR OMA; MGTTNYL; -.
DR OrthoDB; 966922at2759; -.
DR PhylomeDB; Q0WPK3; -.
DR PRO; PR:Q0WPK3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q0WPK3; baseline and differential.
DR Genevisible; Q0WPK3; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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: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:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
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 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 SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 2: Evidence at transcript level;
KW Autophagy; Membrane; Protein transport; Reference proteome; Repeat;
KW Transport; Vacuole; WD repeat.
FT CHAIN 1..391
FT /note="Autophagy-related protein 18d"
FT /id="PRO_0000421882"
FT REPEAT 31..69
FT /note="WD 1"
FT REPEAT 74..118
FT /note="WD 2"
FT REPEAT 203..243
FT /note="WD 3"
FT REPEAT 248..287
FT /note="WD 4"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 43888 MW; 9AA833FDE2FE8386 CRC64;
MDPRRNFQPG GYDSRNTFTS GSFGPPDFGE SDEAELVSVS WNQDYSCFAA GTSHGFRIYN
CEPFKETFRR ELKDGGFKIV EMLFRSNILA LVGGGPNSQY PSNKVLIWDD HQGRCISEFT
FRSEIRAVKL RRDRIVVVLE HKIYVYNFMD LRLLHQIENM ANPRGLCCLS HHMNTSVLAC
PGIRRGEVRV EHFGLNMVQI INAHDSNIAC MTLTLDGLLL ATASTKGTLI RIFNTMDGTR
LQEVRRGVDR ADIYSIALSP NVQWLAVSSD KGTVHIFSLR VRVIGEDAYS TEHETSSNSL
QPLVSPASGA NPGSSLSFLR GVLPKYFSSE WSFSQFHVPE VTQYFAAFGA QNTIAIIGLD
GSFYRCNFDP VNGGEMTQLE HFHFLKQDSP R
