ATG1A_ARATH
ID ATG1A_ARATH Reviewed; 626 AA.
AC Q94C95; Q9M269;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Serine/threonine-protein kinase ATG1a {ECO:0000305};
DE EC=2.7.11.-;
DE AltName: Full=Autophagy-related protein 1a {ECO:0000303|PubMed:12114572};
DE Short=AtAPG1a {ECO:0000303|PubMed:12114572};
GN Name=ATG1A {ECO:0000303|PubMed:17204848};
GN OrderedLocusNames=At3g61960 {ECO:0000312|Araport:AT3G61960};
GN ORFNames=F21F14.130 {ECO:0000312|EMBL:CAB71903.1};
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=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 [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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17204848; DOI=10.4161/auto.3595;
RA Meijer W.H., van der Klei I.J., Veenhuis M., Kiel J.A.K.W.;
RT "ATG genes involved in non-selective autophagy are conserved from yeast to
RT man, but the selective Cvt and pexophagy pathways also require organism-
RT specific genes.";
RL Autophagy 3:106-116(2007).
RN [6]
RP FUNCTION, INTERACTION WITH ATG13A, 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 [7]
RP INTERACTION WITH ATG8E, SUBCELLULAR LOCATION, AIM MOTIF, AND MUTAGENESIS OF
RP TYR-360 AND VAL-363.
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: Serine/threonine protein kinase involved in autophagy in a
CC nutritional condition-dependent manner. The ATG1-ATG13 protein kinase
CC complex regulates downstream events required for autophagosome
CC enclosure and/or vacuolar delivery. Becomes a target of autophagy under
CC nutrient starvation. Connects autophagy to plant nutritional status.
CC {ECO:0000269|PubMed:21984698}.
CC -!- SUBUNIT: Interacts with ATG13A (PubMed:21984698). Interacts with ATG8E.
CC Binds to ATG8E on autophagic vesicles (PubMed:24563201).
CC {ECO:0000269|PubMed:21984698, ECO:0000269|PubMed:24563201}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome
CC {ECO:0000269|PubMed:21984698, ECO:0000269|PubMed:24563201}.
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=Q94C95-1; 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. {ECO:0000269|PubMed:21984698}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB71903.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL138642; CAB71903.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80285.1; -; Genomic_DNA.
DR EMBL; AY035049; AAK59554.1; -; mRNA.
DR PIR; T47988; T47988.
DR RefSeq; NP_567122.1; NM_116061.3. [Q94C95-1]
DR AlphaFoldDB; Q94C95; -.
DR SMR; Q94C95; -.
DR STRING; 3702.AT3G61960.1; -.
DR TCDB; 9.A.15.3.1; the autophagy-related phagophore-formation transporter (apt) family.
DR iPTMnet; Q94C95; -.
DR PaxDb; Q94C95; -.
DR PRIDE; Q94C95; -.
DR ProteomicsDB; 241040; -. [Q94C95-1]
DR EnsemblPlants; AT3G61960.1; AT3G61960.1; AT3G61960. [Q94C95-1]
DR GeneID; 825369; -.
DR Gramene; AT3G61960.1; AT3G61960.1; AT3G61960. [Q94C95-1]
DR KEGG; ath:AT3G61960; -.
DR Araport; AT3G61960; -.
DR TAIR; locus:2079527; AT3G61960.
DR eggNOG; KOG0595; Eukaryota.
DR InParanoid; Q94C95; -.
DR OrthoDB; 312774at2759; -.
DR PhylomeDB; Q94C95; -.
DR PRO; PR:Q94C95; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q94C95; baseline and differential.
DR Genevisible; Q94C95; AT.
DR GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IDA:UniProtKB.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
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:0042594; P:response to starvation; IBA:GO_Central.
DR GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
DR InterPro; IPR045269; Atg1-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24348; PTHR24348; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Autophagy; Cytoplasmic vesicle; Kinase;
KW Nucleotide-binding; Phosphoprotein; Protein transport; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Transport.
FT CHAIN 1..626
FT /note="Serine/threonine-protein kinase ATG1a"
FT /id="PRO_0000434619"
FT DOMAIN 10..268
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 288..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 360..363
FT /note="AIM (Atg8-family-interacting motif)"
FT /evidence="ECO:0000269|PubMed:24563201"
FT COMPBIAS 288..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 132
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 16..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 360
FT /note="Y->A: Loss of binding to ATG8E; when associated with
FT A-363."
FT /evidence="ECO:0000269|PubMed:24563201"
FT MUTAGEN 363
FT /note="V->A: Loss of binding to ATG8E; when associated with
FT A-360."
FT /evidence="ECO:0000269|PubMed:24563201"
SQ SEQUENCE 626 AA; 69602 MW; 1C1DDE548EB5E0B0 CRC64;
MESARLVGDY ALGPRIGSGS FAVVWLAKHR SSGLEVAVKE IDKKLLSPKV RDNLLKEISI
LSTIDHPNII RFYEAIETGD RIFLVLEYCS GGDLAGYINR HGKVPEAVAK HFMRQLALGL
QVLQEKHFIH RDLKPQNLLL SSKEVTPLLK IGDFGFARSL TPESMAETFC GSPLYMAPEI
IRNQKYDAKA DLWSAGAILF QLVTGKPPFD GNNHIQLFHN IVRDTELKFP EDTRNEIHPD
CVDLCRSLLR RNPIERLTFR EFFNHMFLRE PRQIPDVEHS GFSTCTGKSL LPSAQPSTST
NRFKSSAENV HKHGSSSSAS NSQISMPHTS FEKTRKDTEG QCSSNQSGVV DSLELIEREY
VLVNRPSASL EGSSDCFDTS LQDSGFPNIL PRNEKVSSSS LEAQKPLSDV SGPRPASVSY
LLTEVQRLTI VHPPTKLQLL HQYAQALTEL ASEMGNTGQV KESFAVTLVV LAVWRKALEI
CDSWMMSVGE NEVNPDPTTA PETSIPDLNS PAPAKTWVTQ EFVTALNQAE NLSTQLNETS
AATHMPDAME TIYERALAYG KSGGAEEYLS NKESAATLYK KAILLLSFII EEAVTLSLNP
SFSLTPDDKK RILYYISNLQ HRRSHL
