ATG9_ARATH
ID ATG9_ARATH Reviewed; 866 AA.
AC Q8RUS5; Q9SJX0;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Autophagy-related protein 9 {ECO:0000303|PubMed:12114572};
DE Short=AtAPG9 {ECO:0000303|PubMed:12114572};
GN Name=ATG9 {ECO:0000303|PubMed:24805779};
GN Synonyms=APG9 {ECO:0000303|PubMed:12114572};
GN OrderedLocusNames=At2g31260 {ECO:0000312|Araport:AT2G31260};
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, GENE FAMILY,
RP NOMENCLATURE, AND DISRUPTION PHENOTYPE.
RX PubMed=12114572; DOI=10.1104/pp.011024;
RA Hanaoka H., Noda T., Shirano Y., Kato T., Hayashi H., Shibata D.,
RA Tabata S., Ohsumi Y.;
RT "Leaf senescence and starvation-induced chlorosis are accelerated by the
RT disruption of an Arabidopsis autophagy gene.";
RL Plant Physiol. 129:1181-1193(2002).
RN [2]
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 [3]
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 [4]
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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=24249832; DOI=10.1105/tpc.113.118307;
RA Zhuang X., Wang H., Lam S.K., Gao C., Wang X., Cai Y., Jiang L.;
RT "A BAR-domain protein SH3P2, which binds to phosphatidylinositol 3-
RT phosphate and ATG8, regulates autophagosome formation in Arabidopsis.";
RL Plant Cell 25:4596-4615(2013).
RN [6]
RP FUNCTION.
RX PubMed=24805779; DOI=10.14348/molcells.2014.0042;
RA Shin K.D., Lee H.N., Chung T.;
RT "A revised assay for monitoring autophagic flux in Arabidopsis thaliana
RT reveals involvement of AUTOPHAGY-RELATED9 in autophagy.";
RL Mol. Cells 37:399-405(2014).
RN [7]
RP STRUCTURE BY ELECTRON MICROSCOPY (7.8 ANGSTROMS), AND SUBUNIT.
RX PubMed=31276439; DOI=10.1080/15548627.2019.1639300;
RA Lai L.T.F., Yu C., Wong J.S.K., Lo H.S., Benlekbir S., Jiang L.,
RA Lau W.C.Y.;
RT "Subnanometer resolution cryo-EM structure of Arabidopsis thaliana ATG9.";
RL Autophagy 16:575-583(2020).
CC -!- FUNCTION: Phospholipid scramblase involved in autophagy by mediating
CC autophagosomal membrane expansion (PubMed:12114572, PubMed:24805779).
CC Cycles between the preautophagosomal structure/phagophore assembly site
CC (PAS) and the cytoplasmic vesicle pool and supplies membrane for the
CC growing autophagosome. Lipid scramblase activity plays a key role in
CC preautophagosomal structure/phagophore assembly by distributing the
CC phospholipids that arrive through ATG2 from the cytoplasmic to the
CC luminal leaflet of the bilayer, thereby driving autophagosomal membrane
CC expansion (By similarity). In addition to autophagy, also plays a role
CC in necrotic cell death (By similarity). Plays an essential role in
CC plant nutrient recycling (PubMed:12114572).
CC {ECO:0000250|UniProtKB:Q68FE2, ECO:0000250|UniProtKB:Q7Z3C6,
CC ECO:0000269|PubMed:12114572, ECO:0000269|PubMed:24805779}.
CC -!- SUBUNIT: Homotrimer; forms a homotrimer with a central pore that forms
CC a path between the two membrane leaflets.
CC {ECO:0000269|PubMed:31276439}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000269|PubMed:24249832}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flowers.
CC {ECO:0000269|PubMed:12114572}.
CC -!- DOMAIN: Forms a homotrimer with a solvated central pore, which is
CC connected laterally to the cytosol through the cavity within each
CC protomer. Acts as a lipid scramblase that uses its central pore to
CC function: the central pore opens laterally to accommodate lipid
CC headgroups, thereby enabling lipid flipping and redistribution of
CC lipids added to the outer leaflet of ATG9-containing vesicles, thereby
CC enabling growth into autophagosomes. {ECO:0000250|UniProtKB:Q7Z3C6}.
CC -!- DISRUPTION PHENOTYPE: Mutant plants are hypersensitive to nitrogen or
CC carbon starvation and show early bolting senescence.
CC {ECO:0000269|PubMed:12114572}.
CC -!- SIMILARITY: Belongs to the ATG9 family. {ECO:0000305}.
CC -!- CAUTION: Low resolution structures by electron microscopy suggested the
CC presence of six transmembrane regions (PubMed:31276439). However, high
CC resolution structures in human and S.pombe showed that it is composed
CC of four transmembrane and two intramembrane regions (By similarity).
CC {ECO:0000250|UniProtKB:O74312, ECO:0000250|UniProtKB:Q7Z3C6,
CC ECO:0000269|PubMed:31276439}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD20671.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB073174; BAB88386.1; -; mRNA.
DR EMBL; AC006593; AAD20671.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC08515.1; -; Genomic_DNA.
DR EMBL; AY075619; AAL91630.1; -; mRNA.
DR EMBL; AY099644; AAM20495.1; -; mRNA.
DR EMBL; BT000243; AAN15562.1; -; mRNA.
DR EMBL; BT000816; AAN33191.1; -; mRNA.
DR PIR; E84718; E84718.
DR RefSeq; NP_850164.1; NM_179833.2.
DR AlphaFoldDB; Q8RUS5; -.
DR SMR; Q8RUS5; -.
DR IntAct; Q8RUS5; 3.
DR STRING; 3702.AT2G31260.1; -.
DR TCDB; 9.A.15.3.1; the autophagy-related phagophore-formation transporter (apt) family.
DR PaxDb; Q8RUS5; -.
DR PRIDE; Q8RUS5; -.
DR ProteomicsDB; 246549; -.
DR EnsemblPlants; AT2G31260.1; AT2G31260.1; AT2G31260.
DR GeneID; 817683; -.
DR Gramene; AT2G31260.1; AT2G31260.1; AT2G31260.
DR KEGG; ath:AT2G31260; -.
DR Araport; AT2G31260; -.
DR TAIR; locus:2042531; AT2G31260.
DR eggNOG; KOG2173; Eukaryota.
DR HOGENOM; CLU_330511_0_0_1; -.
DR InParanoid; Q8RUS5; -.
DR OMA; MAHFETE; -.
DR OrthoDB; 712239at2759; -.
DR PhylomeDB; Q8RUS5; -.
DR PRO; PR:Q8RUS5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8RUS5; baseline and differential.
DR Genevisible; Q8RUS5; AT.
DR GO; GO:0005776; C:autophagosome; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006914; P:autophagy; IMP:TAIR.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IEP:UniProtKB.
DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
DR InterPro; IPR007241; Autophagy-rel_prot_9.
DR PANTHER; PTHR13038; PTHR13038; 2.
DR Pfam; PF04109; ATG9; 1.
PE 1: Evidence at protein level;
KW Autophagy; Lipid transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..866
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000434624"
FT TOPO_DOM 1..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..153
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 320..340
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT TOPO_DOM 341..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..433
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 455..507
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 508..528
FT /evidence="ECO:0000250|UniProtKB:Q7Z3C6"
FT TOPO_DOM 529..866
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 744..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 866 AA; 99467 MW; 8951A9F39911D340 CRC64;
MMSSGHKGPN VRNFFKWQRG ESSSSLTTGL LHNESHEIEL SNYGGIPSPG SESPSGLLNG
ESLNVQPIAD LDLFVERLYS YYRDKGLWCI IVKWAVELLS LGFIICFSGF FLLYVDWNGL
QNAKCGMDAV ESGTKPCDLV KEAIHPHPLS PFTLTTAIIV GYLALFSVYW LFCFLRFFAQ
LKDTLDFRHF YYNNLHVTDN EILTMPWATV LEKVVQLQSS QCLCVVKDLS AHDMVMRLMR
KENYLIGMLN KGLLSFPISH WIPGAGPAVK SAPDGTQYHL VLTKTLEWTL NWCILQSMFD
CNFRVRRDFV SNPTTLKKRL FVVGLAMLLL SPFLVIFMLV YLFLRHAEQF YNHPSTASSR
RWSNLSKWLF REFNEVDHLF KHRINSSVVH ASEYLKQFPS PIISIIAKFV SFVSGGFAAV
LIIIAFLEES LLEGHIFGRN LFWYAAVFGT ITAISRAAIS DELLVLDPVG TMSLVVQNTH
YMPKRWRGKE NKDDVRLELE TLFQYTGMML LEEIASIFIT PFLLMFVVPK RVDDILQFIK
DFTVDIEGVG HVCSFSAFYF ENHGNIKYGS PHNATRREQR SSQGKMEKSF LSFQSSYPSW
ESDSLGKQFL SNLRTFRDRK LHEINTRHSS PSRAWRESTN TPALYRDIPR NPLASGNHTD
SMWLIDPDQR NHPYLLDWYY TSQAHNRTDH PIERANEILT ANQNATDCWP PDLGIRGEDS
RDLLNMEAST SGQFFRESIL RHDQPEGEDS YGSQHPLDGR NQWWGRGNHS QISTAHPATT
NSFIEPPDFI NRYTAGNLLD NSWSRRSIEE EDEEEEELDW EENARRNLSR TTFMDDNDIE
AGIDLHFDDV YSSRPQETST SSTTLR
