ID   ATG1_PENRW              Reviewed;         960 AA.
AC   A7KAL2; B6HBB5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   02-SEP-2026, entry version 94.
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:0000303|PubMed:17204848};
GN   ORFNames=Pc18g03490 {ECO:0000303|PubMed:18820685};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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:17204848).
CC       Involved in the clearance of protein aggregates which cannot be
CC       efficiently cleared by the proteasome. Required for selective
CC       autophagic degradation of the nucleus (nucleophagy) as well as for
CC       mitophagy which contributes to regulate mitochondrial quantity and
CC       quality by eliminating the mitochondria to a basal level to fulfill
CC       cellular energy requirements and preventing excess ROS production. Also
CC       involved in endoplasmic reticulum-specific autophagic process, in
CC       selective removal of ER-associated degradation (ERAD) substrates. Plays
CC       a key role in ATG9 and ATG23 cycling through the pre-autophagosomal
CC       structure and is necessary to promote ATG18 binding to ATG9 through
CC       phosphorylation of ATG9. Catalyzes phosphorylation of ATG4, decreasing
CC       the interaction between ATG4 and ATG8 and impairing deconjugation of
CC       PE-conjugated forms of ATG8 (By similarity).
CC       {ECO:0000250|UniProtKB:P53104, ECO:0000269|PubMed:17204848}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000250|UniProtKB:P53104};
CC   -!- SUBUNIT: Homodimer. Forms a ternary complex with ATG13 and ATG17.
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}.
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; EF107734; ABO31072.1; -; Genomic_DNA.
DR   EMBL; AM920433; CAP94573.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7KAL2; -.
DR   SMR; A7KAL2; -.
DR   STRING; 500485.A7KAL2; -.
DR   VEuPathDB; FungiDB:PCH_Pc18g03490; -.
DR   eggNOG; KOG0595; Eukaryota.
DR   HOGENOM; CLU_006447_0_0_1; -.
DR   OMA; INNVVQW; -.
DR   OrthoDB; 346907at2759; -.
DR   BioCyc; PCHR:PC18G03490-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c18.
DR   GO; GO:0005776; C:autophagosome; IEA:TreeGrafter.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0034045; C:phagophore assembly site membrane; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0106310; F:protein serine kinase activity; ISS:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000045; P:autophagosome assembly; IEA:TreeGrafter.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IEA:TreeGrafter.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:TreeGrafter.
DR   GO; GO:0010506; P:regulation of autophagy; IEA:TreeGrafter.
DR   GO; GO:0042594; P:response to starvation; IEA:TreeGrafter.
DR   GO; GO:0061709; P:reticulophagy; IEA:TreeGrafter.
DR   CDD; cd14009; STKc_ATG1_ULK_like; 1.
DR   FunFam; 1.10.510.10:FF:000817; Serine/threonine-protein kinase ATG1; 1.
DR   FunFam; 3.30.200.20:FF:000399; Serine/threonine-protein kinase atg1; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR045269; Atg1-like.
DR   InterPro; IPR048941; ATG1-like_MIT2.
DR   InterPro; IPR022708; Atg1-like_tMIT.
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:SF22; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR   PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 1.
DR   Pfam; PF12063; ATG1-like_MIT1; 1.
DR   Pfam; PF21127; ATG1-like_MIT2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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   Protein transport; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase; Transport.
FT   CHAIN           1..960
FT                   /note="Serine/threonine-protein kinase atg1"
FT                   /id="PRO_0000317795"
FT   DOMAIN          22..327
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          333..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          503..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          550..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          673..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          789..815
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          926..960
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        520..536
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..566
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        789..800
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        801..815
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        930..951
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        165
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         28..36
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   960 AA;  104745 MW;  D54DFC78DA5C4B30 CRC64;
     MASQHSRRSR EAPRPEMSIG RYTRLDEIGR GSFATVYQGV HTKSKTYVAI KSVNLSKLNK
     KLKENLSSEI DILKGLHHPH IVALIDCHES TSHIHLVMEY CALGDLSLFI KRRDTLGSHK
     YTRDMIAKYP NPPGGSLNEV VTRHFLKQLS SALKFLRDRN LIHRDIKPQN LLLCPSPSSY
     RSGHAQVMPY KGSDDSYEPT TGLESLPMLK IADFGFARSL PATSLAETLC GSPLYMAPEI
     LRYEKYDAKA DLWSVGTVLY EMVVGRPPFR ATNHVELLRK IEKGEDRIRF PEDNPASDDI
     KKLIRGLLKR NPVERLNFPE FFSNNVINDP IPGLLADDAP GPPQSPRPRQ LVGKAEESPY
     DTGPEDKLAY PPGQRPVTTH PKSGTPPTAT DMRRMGSADR PAPAISKEQQ PGGTPPQRPG
     PVSLATAPGR QELIDRNATT AAMDRQRHRN TYAGAPKASD STIRAQEARD RAAQEVAFER
     DYVVVEKRAV EVNAFADELA HSPRLQGGLS RPGQTGAGSR RTTTQGLPTV SPSSPHANAA
     KAMQVVSGRA RADSTHQRQH SYERRYGQSP TSATSAISKA LNMASGRLFG MGFSPPLAIT
     KGGRSPPLAY NPFPAYPPVH ASLLITGDGS KPNATGDEDC KAVQEIEECA TRSDVVFGFA
     EVKYKQLIPL APSASTDPSA RPMDTNVEPD SADSDDGLTV DAIVTLSEEA LVLYVKALSL
     LAKSMDIAGA WWSRKNREEV YGESPTKDSM SAVAGTRINY VVQWVRSRFN EVIEKAEFVR
     LKLIEGQRRL PPDHPSHPDN HSISSTAGSS STADVVVSPG VTAERLMYDR ALEMSRAAAI
     NELTGEDLAN CEITYVTAIR MLEAVLEDDG MRSMPGSNIE RQSSSQGGEK VVLDELQVED
     RQVVVKLVSS MRGRLASVRK KVAVLAKRSS APTPTAGSAG KTPTSNISPV TYATGVTPPR
//