ID ATG1_ASPTN Reviewed; 964 AA.
AC Q0CLX3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 77.
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=ATEG_05311 {ECO:0000303|Ref.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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. {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 -!- 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; CH476600; EAU34380.1; -; Genomic_DNA.
DR RefSeq; XP_001214489.1; XM_001214489.1.
DR AlphaFoldDB; Q0CLX3; -.
DR SMR; Q0CLX3; -.
DR STRING; 341663.Q0CLX3; -.
DR EnsemblFungi; EAU34380; EAU34380; ATEG_05311.
DR GeneID; 4320695; -.
DR VEuPathDB; FungiDB:ATEG_05311; -.
DR eggNOG; KOG0595; Eukaryota.
DR HOGENOM; CLU_006447_0_0_1; -.
DR OMA; INNVVQW; -.
DR OrthoDB; 2786057at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IEA:EnsemblFungi.
DR GO; GO:0000421; C:autophagosome membrane; IEA:EnsemblFungi.
DR GO; GO:0005829; C:cytosol; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR GO; GO:0061709; P:reticulophagy; IEA:EnsemblFungi.
DR CDD; cd14009; STKc_ATG1_ULK_like; 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..964
FT /note="Serine/threonine-protein kinase atg1"
FT /id="PRO_0000317790"
FT DOMAIN 26..331
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 32..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 964 AA; 105333 MW; E5834643C699499C CRC64;
MASAHHSRRP RETSQTSQSE MSVGRYTRLG QIGKGSFATV YQGVHTKSRT YVAIKSVNLS
QLNKKLKENL FSEIHILKGL YHPHIVALID CHETTSHIHL VMEYCALGDL SQFIRHRNTL
GEHRYTRDMI AKYPNPRGGA LNEVVVRHFL KQLASALKFL RDRNLIHRDI KPQNLLLCPS
PTSYRAGVAQ IVPFKGSEDS FSPATGLDSL PMLKIADFGF ARSLPATSLA ETLCGSPLYM
APEILRYEKY DAKADLWSVG TVLYEMVVGK PPFRASNHVE LLRRIERGED NIKFPPENPA
SDDIKALIRM LLKRNPVERM NFADFFESNV ITSPIPGLIP DDTGTLRRPS ADLDPLGQNS
PAEPQPSPGA AAGSRREKDV SREDQITYPQ RTTAQTPRSG TPPSSVPMRR GGSADKAPST
PKDTATTYPQ RPSTVSHATA PGRQELLDRN ATTAAMERQR NRHTFGPSQH ERPVDKAKEE
QERAAQDVAF ERDYVVVEKR AVEVNAFADE LAHSPRIQGG FTRNAQTGAI SRRATVQGPQ
TTATSPLASN TKAMQVFPGR SRADSTHARQ SSYERRYGQS PTSATSAISK ALNMASGRLF
GMGFSPPMAI TKGGRSPPLA YNPFPAYPAA QPTLLPIGDG SKTNATLDED AKTVQVIEEC
ATRSDVVYGF AEVKYKQLIP LAPSVPTDPS GRSSLPGGYR EPSDSTDGGL TVDAVVTLSE
EALVLYVKAL SLLAKSMDIA SAWWNRKNRV DVFGDSTINR TDASMTVVGS RINNVVQWVR
SRFNEVLEKA EFVRLKLIEG QKRLPPDHPS HPNNHSIGSS LGSGASVDVV VSPGVTAEKL
MYDRALEMSR AAAINELTGE DLSGCEIAYV TAIRMLEAVL EEDEMPSTAG DKADRKDGEQ
TMLDSVQAED RQVVVKLVSS IRGRLTALQK KLTVLAKRPT GSLGKTPSSN LTPVAHAVGA
TPPR
//
