ATG5_ARATH
ID ATG5_ARATH Reviewed; 337 AA.
AC Q9FFI2;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Autophagy protein 5 {ECO:0000305};
DE AltName: Full=Protein autophagy 5 {ECO:0000305};
DE Short=AtAPG5 {ECO:0000303|PubMed:12114572};
GN Name=ATG5 {ECO:0000303|PubMed:16040659};
GN Synonyms=APG5 {ECO:0000303|PubMed:12114572}; OrderedLocusNames=At5g17290;
GN ORFNames=MKP11_14;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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;
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 NOMENCLATURE, AND GENE FAMILY.
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 [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16040659; DOI=10.1104/pp.105.060673;
RA Thompson A.R., Doelling J.H., Suttangkakul A., Vierstra R.D.;
RT "Autophagic nutrient recycling in Arabidopsis directed by the ATG8 and
RT ATG12 conjugation pathways.";
RL Plant Physiol. 138:2097-2110(2005).
RN [7]
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 [8]
RP FUNCTION.
RX PubMed=23327451; DOI=10.1186/1756-0500-6-17;
RA Lee T.A., Vande Wetering S.W., Brusslan J.A.;
RT "Stromal protein degradation is incomplete in Arabidopsis thaliana
RT autophagy mutants undergoing natural senescence.";
RL BMC Res. Notes 6:17-17(2013).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24463818; DOI=10.1242/jcs.139709;
RA Yoshimoto K., Shibata M., Kondo M., Oikawa K., Sato M., Toyooka K.,
RA Shirasu K., Nishimura M., Ohsumi Y.;
RT "Organ-specific quality control of plant peroxisomes is mediated by
RT autophagy.";
RL J. Cell Sci. 127:1161-1168(2014).
CC -!- FUNCTION: Required for autophagy. Conjugation to ATG12 is essential for
CC plant nutrient recycling (PubMed:16040659). Involved in a negative
CC feedback loop that modulates NPR1-dependent salicylic acid (SA)
CC signaling and limits senescence and immunity-related programmed cell
CC death (PCD) in plants (PubMed:19773385). Involved in complete
CC proteolysis of chloroplast stroma proteins in senescent leaves
CC (PubMed:23327451). Involved in the degradation of damaged peroxisomes
CC (PubMed:24463818). {ECO:0000269|PubMed:16040659,
CC ECO:0000269|PubMed:19773385, ECO:0000269|PubMed:23327451,
CC ECO:0000269|PubMed:24463818}.
CC -!- SUBUNIT: Conjugated to ATG12. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16040659}.
CC -!- PTM: Conjugated to ATG12; which is essential for autophagy. Conjugation
CC with ATG12 involves ATG7 as an E1-like activating enzyme and ATG10 as
CC an E2-like conjugating enzyme (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mutant plants are hypersensitive to nitrogen or
CC carbon starvation (PubMed:16040659). Early senescence phenotype
CC (PubMed:16040659, PubMed:19773385). Hyper accumulation of salicylic
CC acid (SA) (PubMed:19773385). Increased number of peroxisomes and
CC accumulation of peroxisomal proteins (PubMed:24463818).
CC {ECO:0000269|PubMed:16040659, ECO:0000269|PubMed:19773385,
CC ECO:0000269|PubMed:24463818}.
CC -!- SIMILARITY: Belongs to the ATG5 family. {ECO:0000305}.
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DR EMBL; AB005238; BAB10516.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92409.1; -; Genomic_DNA.
DR EMBL; AK117572; BAC42232.1; -; mRNA.
DR EMBL; BT005100; AAO50633.1; -; mRNA.
DR RefSeq; NP_197231.1; NM_121735.5.
DR AlphaFoldDB; Q9FFI2; -.
DR SMR; Q9FFI2; -.
DR BioGRID; 16870; 2.
DR IntAct; Q9FFI2; 1.
DR STRING; 3702.AT5G17290.1; -.
DR TCDB; 9.A.15.3.1; the autophagy-related phagophore-formation transporter (apt) family.
DR PaxDb; Q9FFI2; -.
DR PRIDE; Q9FFI2; -.
DR ProteomicsDB; 246738; -.
DR EnsemblPlants; AT5G17290.1; AT5G17290.1; AT5G17290.
DR GeneID; 831594; -.
DR Gramene; AT5G17290.1; AT5G17290.1; AT5G17290.
DR KEGG; ath:AT5G17290; -.
DR Araport; AT5G17290; -.
DR TAIR; locus:2167195; AT5G17290.
DR eggNOG; KOG2976; Eukaryota.
DR HOGENOM; CLU_051894_0_0_1; -.
DR InParanoid; Q9FFI2; -.
DR OMA; RDDEAGW; -.
DR OrthoDB; 457861at2759; -.
DR PhylomeDB; Q9FFI2; -.
DR PRO; PR:Q9FFI2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFI2; baseline and differential.
DR Genevisible; Q9FFI2; AT.
DR GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IBA:GO_Central.
DR GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IMP:TAIR.
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:0006501; P:C-terminal protein lipidation; IBA:GO_Central.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IEP:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042594; P:response to starvation; IMP:TAIR.
DR Gene3D; 1.10.246.190; -; 1.
DR Gene3D; 3.10.20.620; -; 1.
DR InterPro; IPR007239; Atg5.
DR InterPro; IPR042526; Atg5_HR.
DR InterPro; IPR042527; Atg5_UblA_dom.
DR PANTHER; PTHR13040; PTHR13040; 1.
DR Pfam; PF04106; APG5; 1.
PE 2: Evidence at transcript level;
KW Autophagy; Cytoplasm; Isopeptide bond; Plant defense; Protein transport;
KW Reference proteome; Stress response; Transport; Ubl conjugation.
FT CHAIN 1..337
FT /note="Autophagy protein 5"
FT /id="PRO_0000250585"
FT REGION 271..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 128
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ATG12)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 337 AA; 38477 MW; FF217F03864B4E33 CRC64;
MAKEAVKYVW EGAIPLQIHL HKSDVASHPA PPPALVLAPR IGYLPLLIPL IKPYFKDSLP
PGEDSIWFDY KGFPLKWYIP TGVLFDLLCA EPERPWNLTI HFRGYPCNIL IPCEGEDSVK
WNFVNSLKEA QYIINGNCKN VMNMSQSDQE DLWTSVMNGD LDAYTRLSPK LKMGTVEDEF
SRKTSLSSPQ SQQVVPETEV AGQVKTARIP VRLYVRSLNK DFENLEDVPE IDTWDDISYL
NRPVEFLKEE GKCFTLRDAI KSLLPEFMGD RAQTSGEERS IDDTEEADGS REMGEIKLVR
IQGIEMKLEI PFSWVVNNLM NPEFYLHISV LVKAPQR
