ATG1_ASPOR
ID ATG1_ASPOR Reviewed; 934 AA.
AC Q2UGZ7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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:23136971};
GN ORFNames=AO090023000647 {ECO:0000303|PubMed:16372010};
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [2]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=23136971; DOI=10.1111/1574-6968.12047;
RA Yanagisawa S., Kikuma T., Kitamoto K.;
RT "Functional analysis of Aoatg1 and detection of the Cvt pathway in
RT Aspergillus oryzae.";
RL FEMS Microbiol. Lett. 338:168-176(2013).
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 (By similarity). Required for conidiation and development of
CC aerial hyphae (PubMed:23136971). {ECO:0000250|UniProtKB:P53104,
CC ECO:0000269|PubMed:23136971}.
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. Forms a ternary complex with ATG13 and ATG17.
CC {ECO:0000250|UniProtKB:P53104}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23136971}.
CC Preautophagosomal structure membrane {ECO:0000269|PubMed:23136971};
CC Peripheral membrane protein {ECO:0000269|PubMed:23136971}.
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; AP007157; BAE59168.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2UGZ7; -.
DR SMR; Q2UGZ7; -.
DR STRING; 510516.Q2UGZ7; -.
DR PRIDE; Q2UGZ7; -.
DR EnsemblFungi; BAE59168; BAE59168; AO090023000647.
DR HOGENOM; CLU_006447_0_0_1; -.
DR OMA; INNVVQW; -.
DR Proteomes; UP000006564; Chromosome 3.
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:0000329; C:fungal-type vacuole 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 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..934
FT /note="Serine/threonine-protein kinase atg1"
FT /id="PRO_0000317789"
FT DOMAIN 22..328
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 335..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..580
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 934 AA; 102377 MW; D45CD6ED9C4400F3 CRC64;
MSSSHHRRSR ETSHAEMPIG RYTRLDEIGR GSFATVYQGV HTKSRTYVAI KSVNLSKLNK
KLKENLSSEI HILKGLYHPH IVALIDCHET TSHIHLVMEY CALGDLSLFI KRRDTLGDHR
YTQDMIAKYP NPRGGALNEV VVRHFLKQLA SALKFLRDRN LIHRDIKPQN LLLCPSPSSY
RSGVAQVVPF KGCDESFSPA TGLESLPMLK IADFGFARSL PSTSLAETLC GSPLYMAPEI
LRYEKYDAKA DLWSVGTVLY EMVVGKPPFR ATNHVELLRK IEKGEDRIKF PEENPASEQI
KSLIRMLLKR NPVERMNFSD FFDCDTITGP IPGLIADDAP STSRRSSVAV NTSGSTSRPQ
SRTGSRTPTG MKREKDASYP GKKDDQVSYP AAHRPPTQRS DTPPASSPMR RMGSGDRATT
SKETVTTTPR RPSVVSLATA PGRQELVDRN ATAAVMERQR SRNTYAGVPQ TEKQAEKTKE
ESERAAQEIA FERDYVLVEK RAVEVNAFAD ELAHSPRIQG GFPRNAYALS RRPGTQGSST
ATATSPLATT GKAMQVASGR ARADSTHTRQ GSYERRYGQS PTSAISKALH MASGRLFGMG
FSPPMTITKG GRSPPLGYNP FPAYPAAQGS LMVVGDGART NVTLDEDAKT VQVIEECATR
SDVVYGFAEV KYKQLIPLAP SVQTDPSGRA NVPGGERDST DLTDGGLTVD AVVTLSEEAL
VLYVKALSLL AKSMDIAGAW WSRKNRGEAF GESAMGRTDA TSTLVSNRIN NVVQWVRNRF
NEVLEKAEFV RLKLIEGQKR LPPDHPSHPS NHSVGPSVGS GASTDVVVSS GVTAEKLMYD
RALEMSRAAA INELTGEELS GCEIAYVTAI RMLEAVLEEE EVSRSEPGSG TDRGDARRDG
DKAMLDGVRM EDRQVVIKSS IFIVTRKQSS FVLP
