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AT18C_ARATH
ID   AT18C_ARATH             Reviewed;         393 AA.
AC   Q8GYD7; O22195;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Autophagy-related protein 18c;
DE            Short=AtATG18c;
GN   Name=ATG18C; OrderedLocusNames=At2g40810; ORFNames=T20B5.1;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT   "Arabidopsis ORF Clones.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   GENE FAMILY, 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   -!- 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=AAB86441.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC002409; AAB86441.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002685; AEC09882.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09883.1; -; Genomic_DNA.
DR   EMBL; AK117701; BAC42353.1; -; mRNA.
DR   EMBL; BT028913; ABI49460.1; -; mRNA.
DR   PIR; T00745; T00745.
DR   RefSeq; NP_181613.2; NM_129644.4.
DR   RefSeq; NP_973650.1; NM_201921.2.
DR   AlphaFoldDB; Q8GYD7; -.
DR   SMR; Q8GYD7; -.
DR   STRING; 3702.AT2G40810.1; -.
DR   PaxDb; Q8GYD7; -.
DR   PRIDE; Q8GYD7; -.
DR   ProteomicsDB; 246523; -.
DR   EnsemblPlants; AT2G40810.1; AT2G40810.1; AT2G40810.
DR   EnsemblPlants; AT2G40810.2; AT2G40810.2; AT2G40810.
DR   GeneID; 818678; -.
DR   Gramene; AT2G40810.1; AT2G40810.1; AT2G40810.
DR   Gramene; AT2G40810.2; AT2G40810.2; AT2G40810.
DR   KEGG; ath:AT2G40810; -.
DR   Araport; AT2G40810; -.
DR   TAIR; locus:2058450; AT2G40810.
DR   eggNOG; KOG2111; Eukaryota.
DR   HOGENOM; CLU_025895_2_1_1; -.
DR   InParanoid; Q8GYD7; -.
DR   OMA; WSFCKFQ; -.
DR   OrthoDB; 966922at2759; -.
DR   PhylomeDB; Q8GYD7; -.
DR   PRO; PR:Q8GYD7; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q8GYD7; baseline and differential.
DR   Genevisible; Q8GYD7; 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; -; 2.
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   2: Evidence at transcript level;
KW   Autophagy; Membrane; Protein transport; Reference proteome; Repeat;
KW   Transport; Vacuole; WD repeat.
FT   CHAIN           1..393
FT                   /note="Autophagy-related protein 18c"
FT                   /id="PRO_0000421881"
FT   REPEAT          27..65
FT                   /note="WD 1"
FT   REPEAT          70..114
FT                   /note="WD 2"
FT   REPEAT          199..239
FT                   /note="WD 3"
FT   REPEAT          244..283
FT                   /note="WD 4"
SQ   SEQUENCE   393 AA;  43832 MW;  C43E25B24535C444 CRC64;
     MSSTVSNPQG ILQPGSFLLP ESESMKKEEA ELVSVCWNQD SSCFAAGTSH GFRIYNCEPF
     KETFRRELKD GGFKIVEMLF RSNILALVGG GPNSQYPSSK VLIWDDHQSR CISEFAFRSE
     IRAVKLRRDR IVVVLEHKIY VYNFMDLRLL HQIETQANPR GLCCLSHHSN TSVLACPGLN
     RGEIRVEHFG LNMVQIINAH DSSIACMTLT LDGLLLATAS TKGTLIRIFN TMDGTRLQEV
     RRGVDRADIY SIALSPNVQW LAVSSDKGTV HIFSLRVRVV GEDSYSTENG ALLTQQNYSN
     SLQGLVSPTI GTNPGSSLSF MRGVLPKYFS SEWSYAQFHV SEVTQFFAAF GSNNTVAIIG
     MDGSFYRCSF DPVNGGEMGQ LEYIHFMKMD NRP
 
 
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