AT18F_ARATH
ID AT18F_ARATH Reviewed; 763 AA.
AC Q9FH32;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Autophagy-related protein 18f;
DE Short=AtATG18f;
GN Name=ATG18F; OrderedLocusNames=At5g54730; ORFNames=K5F14.9;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 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, flowers and leaves.
CC {ECO:0000269|PubMed:15860012}.
CC -!- INDUCTION: By sucrose and nitrogen starvation.
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}.
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DR EMBL; AB022214; BAB09939.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96531.1; -; Genomic_DNA.
DR RefSeq; NP_200284.1; NM_124854.4.
DR AlphaFoldDB; Q9FH32; -.
DR STRING; 3702.AT5G54730.1; -.
DR iPTMnet; Q9FH32; -.
DR PaxDb; Q9FH32; -.
DR PRIDE; Q9FH32; -.
DR ProteomicsDB; 246602; -.
DR EnsemblPlants; AT5G54730.1; AT5G54730.1; AT5G54730.
DR GeneID; 835562; -.
DR Gramene; AT5G54730.1; AT5G54730.1; AT5G54730.
DR KEGG; ath:AT5G54730; -.
DR Araport; AT5G54730; -.
DR TAIR; locus:2157523; AT5G54730.
DR eggNOG; KOG2109; Eukaryota.
DR HOGENOM; CLU_003829_2_0_1; -.
DR InParanoid; Q9FH32; -.
DR OMA; FTHAVIQ; -.
DR OrthoDB; 537714at2759; -.
DR PhylomeDB; Q9FH32; -.
DR PRO; PR:Q9FH32; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FH32; baseline and differential.
DR Genevisible; Q9FH32; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042594; P:response to starvation; IEP:TAIR.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR022175; BCAS3.
DR InterPro; IPR045142; BCAS3-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13268; PTHR13268; 1.
DR Pfam; PF12490; BCAS3; 1.
DR SMART; SM00320; WD40; 2.
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..763
FT /note="Autophagy-related protein 18f"
FT /id="PRO_0000421884"
FT REPEAT 345..385
FT /note="WD 1"
FT REPEAT 402..441
FT /note="WD 2"
FT REGION 701..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 763 AA; 82780 MW; 62A0F9F15D60D334 CRC64;
MKKNGDGSSP KSPDGVVSRS ARSSFRALSN CLKVISSGAS TVARSAVSAA SSAVESHHDQ
VLWAGFDNLQ KEDGDTRRVL LLAFKSGFQV WDVEDTENVH VIVSAHDGQA FFMQMLLNPI
NSGVLDDRFY KSRPLLAVCG DYSSKKISSD NPGSETVATP TNVYVYSLKS QSYVHTLKFR
ATIYSVRCCS RIVAVLQAAQ IDCFDAATLE MDYRIVTNSI VCGSLGVGYG PLAVGPRWIA
YSGSRIATSS SAIFTSEIVS LSTSSPSVAQ FARDSSKQLA SGIANLGDKG YRSLTKYCSE
VLPNPYIPGL KGIGVGNEKV ADAESIGMVI VKDITNKSVI TQFKAHKSPI SALCFDQSGL
LLVTASIQGH NINVFRIMPT ISTSRAVKTT TFAHLFRLQR GFTNAVIQDI CFSKDSNLIV
VGSSRGTSHL FEINPEKEGD APVPMSAISR IRSGNSSGWI GTVSGAASAA AGMVAGSVPG
TVTSTFCYCD EKSNNNYYGS VADMCSKTNL LVFAPSGCMT QYALREHQVG VGHETAAMTG
FDSESGLETE GKLAVDPIRR WSMIQNQSRR ETHDPHSDIY GGGTSVDSKS KVFPEVVRKQ
SVEEAWKVSK KGTTRVVDKR HLYIYEAEQQ QTHLPTQLPL WARRKFRFQE LVLNRGEEIS
GGGGREMEIE GIQTRTIEAR TRDLVPVWGY LQSPRSQQVI NESIQSPSTT TQDDKVATLE
GHGTETDLGA VHSEEQTQSE PVDKEGIAEE KNHSEDEDEE QVD
