ATG2_ARATH
ID ATG2_ARATH Reviewed; 1892 AA.
AC F8S296; A0A1I9LTA0; F4JB41; Q9LJK9; Q9LJL0;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Autophagy-related protein 2 {ECO:0000303|PubMed:21645148};
DE Short=AtAPG2 {ECO:0000303|PubMed:12114572};
DE AltName: Full=Protein PEROXISOME UNUSUAL POSITIONING 1 {ECO:0000303|PubMed:24368788};
GN Name=ATG2 {ECO:0000303|PubMed:21645148};
GN Synonyms=APG2 {ECO:0000303|PubMed:12114572},
GN PEUP1 {ECO:0000303|PubMed:24368788};
GN OrderedLocusNames=At3g19190 {ECO:0000312|Araport:AT3G19190};
GN ORFNames=MVI11.10/MVI11.11 {ECO:0000312|EMBL:BAB02960.1,
GN ECO:0000312|EMBL:BAB02961.1};
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 [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21645148; DOI=10.1111/j.1365-313x.2011.04669.x;
RA Wang Y., Nishimura M.T., Zhao T., Tang D.;
RT "ATG2, an autophagy-related protein, negatively affects powdery mildew
RT resistance and mildew-induced cell death in Arabidopsis.";
RL Plant J. 68:74-87(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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 GENE FAMILY, AND NOMENCLATURE.
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19773385; DOI=10.1105/tpc.109.068635;
RA Yoshimoto K., Jikumaru Y., Kamiya Y., Kusano M., Consonni C., Panstruga R.,
RA Ohsumi Y., Shirasu K.;
RT "Autophagy negatively regulates cell death by controlling NPR1-dependent
RT salicylic acid signaling during senescence and the innate immune response
RT in Arabidopsis.";
RL Plant Cell 21:2914-2927(2009).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24368788; DOI=10.1105/tpc.113.116947;
RA Shibata M., Oikawa K., Yoshimoto K., Kondo M., Mano S., Yamada K.,
RA Hayashi M., Sakamoto W., Ohsumi Y., Nishimura M.;
RT "Highly oxidized peroxisomes are selectively degraded via autophagy in
RT Arabidopsis.";
RL Plant Cell 25:4967-4983(2013).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=24285797; DOI=10.1105/tpc.113.117192;
RA Hackenberg T., Juul T., Auzina A., Gwizdz S., Malolepszy A.,
RA Van Der Kelen K., Dam S., Bressendorff S., Lorentzen A., Roepstorff P.,
RA Lehmann Nielsen K., Joergensen J.E., Hofius D., Van Breusegem F.,
RA Petersen M., Andersen S.U.;
RT "Catalase and NO CATALASE ACTIVITY1 promote autophagy-dependent cell death
RT in Arabidopsis.";
RL Plant Cell 25:4616-4626(2013).
CC -!- FUNCTION: Lipid transfer protein involved in autophagosome assembly
CC (PubMed:21645148). Tethers the edge of the isolation membrane (IM) to
CC the endoplasmic reticulum (ER) and mediates direct lipid transfer from
CC ER to IM for IM expansion (By similarity). Binds to the ER exit site
CC (ERES), which is the membrane source for autophagosome formation, and
CC extracts phospholipids from the membrane source to the IM for membrane
CC expansion (By similarity). Plays an essential role in plant nutrient
CC recycling (PubMed:21645148, PubMed:19773385). Involved in the negative
CC regulation of plant defense responses to biotrophic pathogens
CC (PubMed:21645148). Involved in a negative feedback loop that modulates
CC NPR1-dependent salicylic acid (SA) signaling and limits senescence and
CC immunity-related programmed cell death (PCD) in plants
CC (PubMed:19773385). Involved in the degradation of damaged peroxisomes
CC (PubMed:24368788). {ECO:0000250|UniProtKB:Q2TAZ0,
CC ECO:0000269|PubMed:19773385, ECO:0000269|PubMed:21645148,
CC ECO:0000269|PubMed:24368788}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-
CC sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663,
CC ChEBI:CHEBI:57262; Evidence={ECO:0000250|UniProtKB:Q2TAZ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-
CC diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895,
CC ChEBI:CHEBI:64612; Evidence={ECO:0000250|UniProtKB:Q2TAZ0};
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000250|UniProtKB:Q96BY7}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96BY7}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P53855}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P53855}.
CC -!- DISRUPTION PHENOTYPE: Early senescence phenotype (PubMed:21645148,
CC PubMed:19773385, PubMed:24368788). Defects in autophagosome formation.
CC Enhanced resistance to powdery mildew (Golovinomyces cichoracearum) and
CC mildew-induced cell death. Constitutive expression of defense-related
CC genes (PubMed:21645148). Increased number of peroxisomes and
CC accumulation of peroxisomal proteins (PubMed:24368788). Reduced
CC sensitivity to programmed cell death (PCD) induced by both hydroxyurea
CC and the bacterial avirulent factor avrRpm1 (PubMed:24285797).
CC {ECO:0000269|PubMed:19773385, ECO:0000269|PubMed:21645148,
CC ECO:0000269|PubMed:24285797, ECO:0000269|PubMed:24368788}.
CC -!- SIMILARITY: Belongs to the ATG2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEE76206.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB02960.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes.; Evidence={ECO:0000305};
CC Sequence=BAB02961.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes.; Evidence={ECO:0000305};
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DR EMBL; HQ446214; ADU79134.1; -; mRNA.
DR EMBL; AP000419; BAB02960.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP000419; BAB02961.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76206.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; ANM65807.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65808.1; -; Genomic_DNA.
DR RefSeq; NP_001327751.1; NM_001338385.1.
DR RefSeq; NP_001327752.1; NM_001338386.1.
DR RefSeq; NP_188550.3; NM_112806.3.
DR AlphaFoldDB; F8S296; -.
DR STRING; 3702.AT3G19190.1; -.
DR TCDB; 9.A.15.3.1; the autophagy-related phagophore-formation transporter (apt) family.
DR iPTMnet; F8S296; -.
DR PaxDb; F8S296; -.
DR PRIDE; F8S296; -.
DR ProteomicsDB; 246735; -.
DR EnsemblPlants; AT3G19190.2; AT3G19190.2; AT3G19190.
DR EnsemblPlants; AT3G19190.3; AT3G19190.3; AT3G19190.
DR GeneID; 821453; -.
DR Gramene; AT3G19190.2; AT3G19190.2; AT3G19190.
DR Gramene; AT3G19190.3; AT3G19190.3; AT3G19190.
DR KEGG; ath:AT3G19190; -.
DR Araport; AT3G19190; -.
DR TAIR; locus:2094063; AT3G19190.
DR eggNOG; KOG2993; Eukaryota.
DR OMA; FYLYDRS; -.
DR OrthoDB; 40783at2759; -.
DR PRO; PR:F8S296; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F8S296; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
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:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0030242; P:autophagy of peroxisome; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR GO; GO:0010150; P:leaf senescence; IMP:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
DR InterPro; IPR026849; ATG2.
DR InterPro; IPR026885; ATG2_CAD_motif.
DR InterPro; IPR026886; ATG2_fungi/plants.
DR InterPro; IPR015412; Autophagy-rel_C.
DR InterPro; IPR026854; VPS13-like_N.
DR PANTHER; PTHR13190; PTHR13190; 1.
DR PANTHER; PTHR13190:SF1; PTHR13190:SF1; 1.
DR Pfam; PF13329; ATG2_CAD; 1.
DR Pfam; PF09333; ATG_C; 1.
DR Pfam; PF12624; Chorein_N; 1.
PE 2: Evidence at transcript level;
KW Autophagy; Endoplasmic reticulum; Lipid transport; Membrane; Plant defense;
KW Protein transport; Reference proteome; Stress response; Transport.
FT CHAIN 1..1892
FT /note="Autophagy-related protein 2"
FT /id="PRO_0000434623"
FT DOMAIN 21..129
FT /note="Chorein N-terminal"
FT /evidence="ECO:0000255"
FT REGION 1357..1376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1866..1892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1892 AA; 209228 MW; 5B8C9B4EC838201B CRC64;
MVFPWNIAKS AEEAFSRWAV KRVVKFLLKK KLGKLILGDI DLDQLDIQLR DGTIQLSDLA
INVDYLNDKF DAPLVIKEGS IGSLLVKMPW KTNGCQVEVD ELELVLAPRL ESNKSSSNEA
STSASTREDL HNIRLEIGKH ENEMLMNAAK SASIDVHEGV KTVAKIVKWF LTSFHVKIKN
LIIAFDPDFG KKQSEAGPRP TLVLRMTEIE CGISEEQVSA NEVSPDNFLG INRLANCVKF
QGAVVELLNM DDDDDGDKTC DKKTSNDVTL IMTGVGGGFS GSLNFSIPWK NGSLDIRKVD
ADISIDPVEV RFQPSTIRWF LQLWKTFTSF GSDCFPSVSH SDFLTDSPTI PTNVMVTPPA
TLSLSGGQEL EHDTTPNLQF IPDWFPSSFS KKEEDGEVDI GASVDQFFEC FDAMRSYQSA
SGSQGMWNWT SSVFTAINAA SSLASGSLLL PSEQQHVETS CKVSFAGVSV VLFFQDEVNW
KGVSTRIHYL GAELRDISVS FQVCLHDLRL EGEVNSMEIA DYCQGGNVVD TANAESQTCL
IKDLQAKVQT SLPPFASSDM HSDSERLSEI VSDGFLFRNK GFAVKTLLVI AAGGSGFQFT
VNFQSSKASH RGSNSFSLSL PPTTFWLNLH SVEMLVNLFN DVSESIPITS HERNQVASSS
KSESLRGSVS ICNARVILWF PFESISERFC NSLGQQFIVV DLSSSPPSDK ERAKERSPGE
MHFPSATRSI CFSVGDASIY LVTSDLKDSE TNSYHRQVEF SAYNILHTNN KTRHQLSTIG
MFWQDRPTVS PWLVERAKML ATQEESIQTD KSGGRGLEFA AVATPKDQDD IYSRSRKEII
LASSFCLYVH LLPLAIHLDS WQYSKLCNLI EEAKNWLSRM AANTAEQTEE SVVCQTSLVV
DCDSIDILVR PEPRMGIKKQ LQTELPGSWI QFNLRVQKLN LMSVPNLGSV SGADFFWLAH
GEGTLLGSVT GLPDQELLLL SCNNSAIKRG NGGGSNALSS RFAGLDFLHL QEPGICNDYL
AVSARGCTIS AVGGRLDWIE VATSFFSFED EKKTQEINSS SSSGSSFILN FVDVGLSYEP
HHENTDHLRQ ASDPWVACLV AASSFSLSKK SLVDSIRNDY RIRIQDLGLL LSVDFDLSKL
GGTYSSEHLH ESGYVKVAND SLIEAILRTN SENGLLWELE CSKSHLVIET CSDTTSGLIR
LATQLQQLLA PDLEESAVHL QTRWDSIQQA NARNDLDISD RLSSSDSSGE MKYLRLESEN
ETGVIGLMDE INEDAFQFDV NPTYQSDSVE CQNNYMSPHG ISHGQAYNWV PATEKLPSNQ
SICGSSSRIN SESSQVFLER ESLPEIFENY CLSEFRPSSE VPQEGDSSGR ELFPETDLRR
GNSGWYDDAS LRIVEDHVSE ATEEDHEEHI LDGECSSFGQ TSYSAVAANG RILLKNIDLK
WRIYSGSDWH DSRKKGENFK HTKGRDTTSC LELELSGVQF LYETFPIGEI CTSKLSLMVQ
DFYLYDRSDN APWTLVLGYY NSKDHPRDSS SYAFKLELKA VRPDPETPLE ENRLRVALLP
ILLHLHQSQL DFLISFFGAN SLEKPVVSMG DSGGSTMSVS VQGHNIIEEA LLPYFQKFDI
WPVNVRVDYS PHHVDIAALT GGKYAELVNL VPWKGIELQL KHVHAAGIYG WGNVCETILG
EWLEDVSQNQ IHQLLKGIPT VRSLSALYAA ALKLVSSPVE SYRKDRRLVK GVQRGTVAFL
RSISLEAVGL GVHLAAGAHD ILLRAEYIFA SSPSLPQPQG RTKTNVRHNQ PRNAKQGMLK
ACESIGDGIG KTASALVRTP LKKYQRGDGA GSAFATVVQG VPTAAIAPAS ACARAVHSAL
VGIRNSLDPE HKKESMEKYL GPDKQRKQDQ HR
