ATG1_KLULA
ID ATG1_KLULA Reviewed; 831 AA.
AC Q6CSX2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
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 OrderedLocusNames=KLLA0C17160g {ECO:0000303|PubMed:15229592};
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 -!- INTERACTION:
CC Q6CSX2; Q6CWK2: ATG13; NbExp=4; IntAct=EBI-16151357, EBI-16151385;
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; CR382123; CAH01818.1; -; Genomic_DNA.
DR RefSeq; XP_452967.1; XM_452967.1.
DR AlphaFoldDB; Q6CSX2; -.
DR SASBDB; Q6CSX2; -.
DR SMR; Q6CSX2; -.
DR DIP; DIP-61491N; -.
DR IntAct; Q6CSX2; 1.
DR STRING; 28985.XP_452967.1; -.
DR PRIDE; Q6CSX2; -.
DR EnsemblFungi; CAH01818; CAH01818; KLLA0_C17160g.
DR GeneID; 2892164; -.
DR KEGG; kla:KLLA0_C17160g; -.
DR eggNOG; KOG0595; Eukaryota.
DR HOGENOM; CLU_006447_1_0_1; -.
DR InParanoid; Q6CSX2; -.
DR OMA; INNVVQW; -.
DR Proteomes; UP000000598; Chromosome C.
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:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; 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: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 1: Evidence at protein 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..831
FT /note="Serine/threonine-protein kinase ATG1"
FT /id="PRO_0000085647"
FT DOMAIN 21..321
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 360..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 27..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 831 AA; 94026 MW; E9C29F1492D9A489 CRC64;
MSSESHDKVV AKAIRLPTEN YSVEKEIGKG SFAVVYKGLS LRDGRNIAIK AVSRSKLKNK
KLLENLEVEI AILKKIKHPH IVGLIDCERT SSDFYLIMEY CALGDLTFFI KKRKNLVLKH
PLIKTVFEHY PPPSTEHNGL NRVLVVNYLQ QLSSALKFLR SKNLVHRDIK PQNLLLCTPL
LDYNDPKTFH ELGFVGIYNL PILKIADFGF ARFLPNTSLA ETLCGSPLYM APEILNYQKY
NAKADLWSVG TVLYEMCCGR PPFKASNHLE LFQKIKKAND EITVPSNCYI EPKLFNLIRG
LLTFDPDSRM GFTDFFNNEV VTEDLTRYEQ SYEPDLESKS KDVAESNMFV SEYLVKPLKQ
QESAHIPPTQ TDENTSVQTG VRRTSGKERL ATNHPPHQQI HPEDNSQNPE QSYQSASQKR
LKSSYNDLIL EKEYVVVEKK TVEVNSLADD FANNGPITNN QGAQVIKPLR YRTSSSSDAS
GGRRASLVER RLSISSLSPS NALSKALGLA SVRLFGYQHN TKATSSPPQQ TLLNPQIFQE
LTENAVLRAD HKLNPFSEQM LDSNITPAVE SLAAKAFVMY SFAEMKFSQI LPTPPSSTDY
DPLSDKRLSN GSCAIEDEED LDQGRPPSNQ TLTSATTKIS SATNVDTQIP APELKKLCTE
SLLLYLKALT ILAASMKLTS KWWYENESKN CTLKLNILVQ WIRDRFNECL DKAEFLRLKL
HAINTSPNSQ WSDDDPVIFV EKLIYDRALD ISRNAARMEM ESGNYNTCEL AYATSLWMLE
ILLDENFQFN EVYDDEYASN ITSLDESDKE MIKKYISSIA NRLKALKSKM V
