ATG1_YEAS7
ID ATG1_YEAS7 Reviewed; 897 AA.
AC A6ZU07;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Serine/threonine-protein kinase ATG1 {ECO:0000250|UniProtKB:P53104};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P53104};
DE AltName: Full=Autophagy-related protein 1 {ECO:0000250|UniProtKB:P53104};
GN Name=ATG1 {ECO:0000250|UniProtKB:P53104};
GN ORFNames=SCY_1890 {ECO:0000303|PubMed:17652520};
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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. Involved in the
CC clearance of protein aggregates which cannot be efficiently cleared by
CC the proteasome. Required for selective autophagic degradation of the
CC nucleus (nucleophagy) as well as for mitophagy which contributes to
CC regulate mitochondrial quantity and quality by eliminating the
CC mitochondria to a basal level to fulfill cellular energy requirements
CC and preventing excess ROS production. Also involved in endoplasmic
CC reticulum-specific autophagic process, in selective removal of ER-
CC associated degradation (ERAD) substrates. Plays a key role in ATG9 and
CC ATG23 cycling through the pre-autophagosomal structure and is necessary
CC to promote ATG18 binding to ATG9 through phosphorylation of ATG9.
CC Catalyzes phosphorylation of ATG4, decreasing the interaction between
CC ATG4 and ATG8 and impairing deconjugation of PE-conjugated forms of
CC ATG8. Finally, ATG1 is also required for the maintenance of cell
CC viability under starvation and for glycogen storage during stationary
CC phase. Plays a role in genome stability through suppression of abnormal
CC mitosis under starvation, and in regulation of filamentous growth.
CC {ECO:0000250|UniProtKB:P53104}.
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 -!- ACTIVITY REGULATION: Activated by hypophosphorylated form of ATG13
CC (present in nitrogen starvation conditions). Also activated by
CC autophopsphorylation of Thr-226 and inhibited by phosphorylation of
CC Ser-34 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Dimerization requires the presence of ATG13. Forms
CC a ternary complex with ATG13 and ATG17. Interacts also with ATG11.
CC {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}. Note=Formes
CC punctate structures in starvation conditions only when ATG13 and ATG17
CC were both present. Localizes to both the isolation membrane (IM) and
CC the vacuole-isolation membrane contact site (VICS) during IM expansion.
CC The IM is a membrane sac generated from the pre-autophagosomal
CC structure that ultimately expands to become a mature autophagosome.
CC {ECO:0000250|UniProtKB:P53104}.
CC -!- DOMAIN: The LIR motif is required for the interaction with ATG8 and for
CC the association of ATG1 with autophagosomes.
CC {ECO:0000250|UniProtKB:P53104}.
CC -!- PTM: Autophosphorylated at Thr-226 and Ser-390. The phosphorylation
CC state may play a role in the induction of protein degradation upon
CC starvation. Phosphorylation at Thr-226 within the activation loop is
CC required for protein kinase activity whereas phosphorylation at Ser-34
CC leads to inhibition of kinase activity. Phosphorylation of Ser-508 and
CC Ser-515 by PKA is required to induce autophagy but not for kinase
CC activity. {ECO:0000250|UniProtKB:P53104}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. APG1/unc-51/ULK1 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; AAFW02000099; EDN61945.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZU07; -.
DR SMR; A6ZU07; -.
DR PRIDE; A6ZU07; -.
DR EnsemblFungi; EDN61945; EDN61945; SCY_1890.
DR HOGENOM; CLU_006447_0_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
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:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW ATP-binding; Autophagy; Cytoplasm; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Protein transport; Serine/threonine-protein kinase;
KW Transferase; Transport.
FT CHAIN 1..897
FT /note="Serine/threonine-protein kinase ATG1"
FT /id="PRO_0000317800"
FT DOMAIN 24..325
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 490..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..886
FT /note="Required for Cvt trafficking"
FT /evidence="ECO:0000250"
FT MOTIF 429..432
FT /note="LIR"
FT /evidence="ECO:0000250"
FT COMPBIAS 490..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 30..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53104"
FT MOD_RES 129
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P53104"
FT MOD_RES 226
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P53104"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53104"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53104"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53104"
FT MOD_RES 508
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P53104"
FT MOD_RES 515
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P53104"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53104"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53104"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53104"
FT MOD_RES 590
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P53104"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53104"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53104"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53104"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53104"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53104"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53104"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53104"
FT MOD_RES 769
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53104"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53104"
SQ SEQUENCE 897 AA; 101717 MW; 7F4C785AA3A7CC46 CRC64;
MGDIKNKDHT TSVNHNLMAS AGNYTAEKEI GKGSFATVYR GHLTSDKSQH VAIKEVSRAK
LKNKKLLENL EIEIAILKKI KHPHIVGLID CERTSTDFYL IMEYCALGDL TFLLKRRKEL
MENHPLLRTV FEKYPPPSEN HNGLHRAFVL SYLQQLASAL KFLRSKNLVH RDIKPQNLLL
STPLIGYHDS KSFHELGFVG IYNLPILKIA DFGFARFLPN TSLAETLCGS PLYMAPEILN
YQKYNAKADL WSVGTVVFEM CCGTPPFRAS NHLELFKKIK RANDVITFPS YCNIEPELKE
LICSLLTFDP AQRIGFEEFF ANKVVNEDLS SYELEDDLPE LESKSKGIVE SNMFVSEYLS
KQPKSPNSNL AGHQSMADNP AELSDALKNS NILTAPAVKT DHTQAVDKKA SNNKYHNSLV
SDRSFEREYV VVEKKSVEVN SLADEVAQAG FNPNPIKHPT STQNQNVLLN EQFSPNNQQY
FQNQGENPRL LRATSSSSGG SDGSRRPSLV DRRLSISSLN PSNALSRALG IASTRLFGGA
NQQQQQQQIT SSPPYSQTLL NSQLFHELTE NIILRIDHLQ HPETLKLDNT NIVSILESLA
AKAFVVYSYA EVKFSQIVPL STTLKGMANF ENRRSMDSNA IAEEQDSDDA EEEDETLKKY
KEDCLSTKTF GKGRTLSATS QLSATFNKLP RSEMILLCNE AIVLYMKALS ILSKSMQVTS
NWWYESQEKS CSLRVNVLVQ WLREKFNECL EKADFLRLKI NDLRFKHASE VAENQTLEEK
GSSEEPVYLE KLLYDRALEI SKMAAHMELK GENLYNCELA YATSLWMLET SLDDDDFTNA
YGDYPFKTNI HLKSNDVEDK EKYHSVLDEN DRIIIRKYID SIANRLKILR QKMNHQN
