ATG1_BEAB2
ID ATG1_BEAB2 Reviewed; 930 AA.
AC J4W0G2;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Serine/threonine-protein kinase ATG1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P53104};
DE AltName: Full=Autophagy-related protein 1 {ECO:0000303|PubMed:27197558};
GN Name=ATG1 {ECO:0000303|PubMed:27197558}; ORFNames=BBA_07025;
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860;
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.-H., Zheng P., Wang Z.-L., Zhang S., Xie X.-Q., Shang Y.,
RA St Leger R.J., Zhao G.-P., Wang C., Feng M.-G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(2012).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27197558; DOI=10.1038/srep26376;
RA Ying S.H., Liu J., Chu X.L., Xie X.Q., Feng M.G.;
RT "The autophagy-related genes BbATG1 and BbATG8 have different functions in
RT differentiation, stress resistance and virulence of mycopathogen Beauveria
RT bassiana.";
RL Sci. Rep. 6:26376-26376(2016).
RN [3]
RP INDUCTION.
RX PubMed=28557308; DOI=10.1111/1462-2920.13803;
RA Chu Z.J., Sun H.H., Zhu X.G., Ying S.H., Feng M.G.;
RT "Discovery of a new intravacuolar protein required for the autophagy,
RT development and virulence of Beauveria bassiana.";
RL Environ. Microbiol. 19:2806-2818(2017).
CC -!- FUNCTION: Serine/threonine protein kinase involved in the cytoplasm to
CC vacuole transport (Cvt) and found to be essential in autophagy, where
CC it is required for the formation of autophagosomes (PubMed:27197558).
CC Involved in the clearance of protein aggregates which cannot be
CC efficiently cleared by the proteasome (By similarity). Required for
CC selective autophagic degradation of the nucleus (nucleophagy) as well
CC as for mitophagy which contributes to regulate mitochondrial quantity
CC and quality by eliminating the mitochondria to a basal level to fulfill
CC cellular energy requirements and preventing excess ROS production (By
CC similarity). Also involved in endoplasmic reticulum-specific autophagic
CC process, in selective removal of ER-associated degradation (ERAD)
CC substrates (By similarity). Plays a key role in ATG9 and ATG23 cycling
CC through the pre-autophagosomal structure and is necessary to promote
CC ATG18 binding to ATG9 through phosphorylation of ATG9. Catalyzes
CC phosphorylation of ATG4, decreasing the interaction between ATG4 and
CC ATG8 and impairing deconjugation of PE-conjugated forms of ATG8 (By
CC similarity). Contributes to conidiation by regulating the conidial
CC levels of the conidiation-related protein CP15 and mediates fungal
CC oxidation resistance by controlling total superoxide dismutase (SOD)
CC activity (PubMed:27197558). {ECO:0000250|UniProtKB:P53104,
CC ECO:0000269|PubMed:27197558}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:P53104};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P53104};
CC -!- SUBUNIT: Homodimer (By similarity). Dimerization requires the presence
CC of ATG13 (By similarity). Forms a ternary complex with ATG13 and ATG17
CC (By similarity). {ECO:0000250|UniProtKB:P53104}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53104}.
CC Preautophagosomal structure membrane {ECO:0000250|UniProtKB:P53104};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P53104}.
CC -!- INDUCTION: Expression is reduced when the vacuolar protein VLP4 is
CC absent (PubMed:28557308). {ECO:0000269|PubMed:28557308}.
CC -!- DOMAIN: The LIR motif is required for the interaction with ATG8 and for
CC the association of ATG1 with autophagosomes (By similarity).
CC {ECO:0000250|UniProtKB:P53104}.
CC -!- DOMAIN: The C-terminal region of ATG1 responsible for ATG13-binding
CC comprises six alpha-helices which fold into two antiparallel three-
CC helix bundles resembling each other (By similarity).
CC {ECO:0000250|UniProtKB:W0T9X4}.
CC -!- DISRUPTION PHENOTYPE: Blocks autophagy (PubMed:27197558). Leads to
CC reduced conidial germination under starvation (PubMed:27197558).
CC Especially, leads to reduced CP15 levels in conidia (PubMed:27197558).
CC Impairs growth of the mycelia on host cadavers and considerably weakens
CC virulence (PubMed:27197558). {ECO:0000269|PubMed:27197558}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. APG1/unc-51/ULK1 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH725171; EJP64020.1; -; Genomic_DNA.
DR RefSeq; XP_008600344.1; XM_008602122.1.
DR AlphaFoldDB; J4W0G2; -.
DR SMR; J4W0G2; -.
DR STRING; 655819.J4W0G2; -.
DR EnsemblFungi; EJP64020; EJP64020; BBA_07025.
DR GeneID; 19890037; -.
DR HOGENOM; CLU_006447_0_0_1; -.
DR InParanoid; J4W0G2; -.
DR Proteomes; UP000002762; Unassembled WGS sequence.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IEA:EnsemblFungi.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0097635; C:extrinsic component of autophagosome membrane; IEA:EnsemblFungi.
DR GO; GO:0061908; C:phagophore; IEA:EnsemblFungi.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0120095; C:vacuole-isolation membrane contact site; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000045; P:autophagosome assembly; IEA:EnsemblFungi.
DR GO; GO:0000422; P:autophagy of mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0044805; P:late nucleophagy; IEA:EnsemblFungi.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0061709; P:reticulophagy; IEA:EnsemblFungi.
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 InterPro; IPR022708; Ser/Thr_kinase_C.
DR PANTHER; PTHR24348; PTHR24348; 1.
DR Pfam; PF12063; DUF3543; 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 2: Evidence at transcript level;
KW ATP-binding; Autophagy; Cytoplasm; Kinase; Membrane; Nucleotide-binding;
KW Protein transport; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Transport.
FT CHAIN 1..930
FT /note="Serine/threonine-protein kinase ATG1"
FT /id="PRO_0000443865"
FT DOMAIN 23..326
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 336..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..897
FT /note="ATG13-binding"
FT /evidence="ECO:0000250|UniProtKB:W0T9X4"
FT REGION 853..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 29..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 930 AA; 102313 MW; 91423C1F186ED4FF CRC64;
MTSRQEGASS HGSRRSSRHV GSFIIDREIG KGSFAQVYMG WHKESKAAVA IKSVELERLN
KKLKENLYGE IQILKTLRHP HIVALHDCVE SSTHINLIME YCELGDLSLF IKKRDKLITH
PATHDMARKY PSAPNSGLHE VVIRHFLKQL SSALEFLRAK NYVHRDVKPQ NLLLLPSQAF
REERALPIME ASQDSLIPIS GLASLPMLKL ADFGFARVLP STSLADTLCG SPLYMAPEIL
RYERYDAKAD LWSVGTVLYE MITGRPPFRA RNHVELLRKI EAAEDVIKFP REVSVTPDLK
ALVRSLLKRS PVERLSFENF FAHHVVTGDI LGLVEDDIPK PPKRELETIR QGEALPSSPR
VQMARQLSSD PRDTRSSPKS PRSSPRSSTV NSSADAAPRR QSQNAERRLS ISSHNSGQGL
GIQRPAPPIQ SHTAPNHPRA ADRSGREPQP SSLRVARQPS DVSLTEEEKA AQDVMFERDY
VVVERRHVEV NALADELAAN EKLGQNNSSA KSSPLQRRYT QQGSATSTTG AIPTPASRTA
LVAQGRAGQD RRSSYEKALS ASPGSASSAI SKAIQDASLR LFGYKVNTMR QKGSSPPLYQ
PFPAYPTPTS AGLLSDGKGS QVSDEDAKAA QAIEEFATRS DCVYGFAEVK YKQLLPMAPS
MDYGLGGVSP DKGTSEEDGL TVDATVALSE EALVLYVKSL TLLARAMDIA SLWWSKKTRA
ESSVVSQTLV QRINAVVQWV RQRFNEVLEK SEVVRLKLTE AQKLLPEDHP SNPAHQGEDS
IASSAVGAKQ VYLTPGISAE KLMYDRALEM SRAAAIDEVT NENLPGCEIS YLTAIRMLEA
VLDSDDEATA RNISSGKEIA KDATQEGSDL DTEEAAHVRK MITMITGRLN MVRKKQQMIA
EANNQAKHVS AMRRLSGDVT PRSVPSYGST
