AT13A_ARATH
ID AT13A_ARATH Reviewed; 603 AA.
AC Q9SCK0;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Autophagy-related protein 13a {ECO:0000303|PubMed:12114572};
DE Short=AtAPG13a {ECO:0000303|PubMed:12114572};
GN Name=ATG13A {ECO:0000303|PubMed:21984698};
GN OrderedLocusNames=At3g49590 {ECO:0000312|Araport:AT3G49590};
GN ORFNames=T9C5.180 {ECO:0000312|EMBL:CAB62463.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [8]
RP FUNCTION, INTERACTION WITH ATG1A, SUBCELLULAR LOCATION, PHOSPHORYLATION,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=21984698; DOI=10.1105/tpc.111.090993;
RA Suttangkakul A., Li F., Chung T., Vierstra R.D.;
RT "The ATG1/ATG13 protein kinase complex is both a regulator and a target of
RT autophagic recycling in Arabidopsis.";
RL Plant Cell 23:3761-3779(2011).
RN [9]
RP INTERACTION WITH ATG11 AND ATG101.
RX PubMed=24563201; DOI=10.1105/tpc.113.120014;
RA Li F., Chung T., Vierstra R.D.;
RT "AUTOPHAGY-RELATED11 plays a critical role in general autophagy- and
RT senescence-induced mitophagy in Arabidopsis.";
RL Plant Cell 26:788-807(2014).
CC -!- FUNCTION: Involved in autophagy in a nutritional condition dependent
CC manner. The ATG1-ATG13 protein kinase complex regulates downstream
CC events required for autophagosome enclosure and/or vacuolar delivery.
CC Becomes a target of autophagy under nutrient starvation. Connects
CC autophagy to plant nutritional status. {ECO:0000269|PubMed:21984698}.
CC -!- SUBUNIT: Interacts with ATG1A (PubMed:21984698). Interacts with ATG11
CC and ATG101 (PubMed:24563201). {ECO:0000269|PubMed:21984698,
CC ECO:0000269|PubMed:24563201}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome
CC {ECO:0000269|PubMed:21984698}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q9SCK0-1; Sequence=Displayed;
CC -!- PTM: Phosphorylated during nutrient starvation. Dephosphorylated in
CC nutrient-rich conditions. {ECO:0000269|PubMed:21984698}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. The double mutant plants atg13a-1 and atg13b-2, or atg13a-2
CC and atg13b-2 are hypersensitive to nitrogen or carbon starvation and
CC show early senescence. {ECO:0000269|PubMed:21984698}.
CC -!- SIMILARITY: Belongs to the ATG13 family. Plant subfamily.
CC {ECO:0000305}.
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DR EMBL; AL132964; CAB62463.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78561.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78562.1; -; Genomic_DNA.
DR EMBL; AK316744; BAH19467.1; -; mRNA.
DR EMBL; AK227226; BAE99263.1; -; mRNA.
DR PIR; T46236; T46236.
DR RefSeq; NP_190528.1; NM_114819.3. [Q9SCK0-1]
DR RefSeq; NP_850673.1; NM_180342.1. [Q9SCK0-1]
DR AlphaFoldDB; Q9SCK0; -.
DR SMR; Q9SCK0; -.
DR IntAct; Q9SCK0; 1.
DR STRING; 3702.AT3G49590.3; -.
DR TCDB; 9.A.15.3.1; the autophagy-related phagophore-formation transporter (apt) family.
DR iPTMnet; Q9SCK0; -.
DR PaxDb; Q9SCK0; -.
DR PRIDE; Q9SCK0; -.
DR EnsemblPlants; AT3G49590.1; AT3G49590.1; AT3G49590. [Q9SCK0-1]
DR EnsemblPlants; AT3G49590.2; AT3G49590.2; AT3G49590. [Q9SCK0-1]
DR GeneID; 824121; -.
DR Gramene; AT3G49590.1; AT3G49590.1; AT3G49590. [Q9SCK0-1]
DR Gramene; AT3G49590.2; AT3G49590.2; AT3G49590. [Q9SCK0-1]
DR KEGG; ath:AT3G49590; -.
DR Araport; AT3G49590; -.
DR eggNOG; KOG4573; Eukaryota.
DR HOGENOM; CLU_030687_1_0_1; -.
DR OMA; EAGMQES; -.
DR PhylomeDB; Q9SCK0; -.
DR PRO; PR:Q9SCK0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SCK0; baseline and differential.
DR Genevisible; Q9SCK0; AT.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IBA:GO_Central.
DR GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0006914; P:autophagy; IDA:UniProtKB.
DR GO; GO:0000423; P:mitophagy; IBA:GO_Central.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; 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; 3.30.900.10; -; 1.
DR InterPro; IPR040182; ATG13.
DR InterPro; IPR018731; Atg13_N.
DR InterPro; IPR036570; HORMA_dom_sf.
DR PANTHER; PTHR13430; PTHR13430; 1.
DR Pfam; PF10033; ATG13; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Cytoplasmic vesicle; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..603
FT /note="Autophagy-related protein 13a"
FT /id="PRO_0000434626"
FT REGION 258..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
SQ SEQUENCE 603 AA; 66564 MW; 03844D5B0341200B CRC64;
MDFPENLPSD IGRLEQIVSH FFPKALHIVL NSRIPSLQSR GRTRERLSGL NVRKSDKWFN
LVMGDRPAAL EKLHSWHRNI LDSMIIDIIL VHPISNDNLD DDDDHSDSVV RSAETVIERW
VVQYENPLIM SPQSSDSATR YQKVYKKSII LLRSLYAQTR LLPAYRVSRQ LSSSLASSGY
DLIYKVSSFS DIFSGPVTET MKEFRFAPVE VPPGRLCASV TYRSDLSDFN LGAHITLPPR
IITDYVGSPA TDPMRFFPSP GRSVEGHSFT GRAGRPPLTG SSAERPHSWT SGFHRPPAQF
ATPNQSFSPA QSHQLSPGLH DFHWSRTDAF GDNHQLSPPF SPSGSPSTPR YISGGNSPRI
NVRPGTAPVT IPSSATLNRY VSSNFSEPGR NPLPPFSPKS TRRSPSSQDS LPGIALYRSS
RSGESPSGLM NQYPTQKLSK DSKYDSGRFS GVLSSSDSPR FAFSRSPSRL SSQDDLDDPD
CSCPFDFDDV DESGLQYSHS LDRRKTSSSI SQSLPLGRRS SQDAAVGVLV HMLKTAPPLR
QDSSTYMASM SGVQREGSVS GTESEFSMAR STSDALEELR NYKQLKDLLL SKSKSGSGPT
RVH
