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Serine/threonine-protein kinase ATG1 (EC 2.7.11.1) (Autophagy-related protein 1)

 ATG1_KLULA              Reviewed;         831 AA.
Q6CSX2;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 1.
23-MAY-2018, entry version 86.
RecName: Full=Serine/threonine-protein kinase ATG1 {ECO:0000250|UniProtKB:P53104};
EC=2.7.11.1 {ECO:0000250|UniProtKB:P53104};
AltName: Full=Autophagy-related protein 1 {ECO:0000250|UniProtKB:P53104};
Name=ATG1 {ECO:0000250|UniProtKB:P53104};
OrderedLocusNames=KLLA0C17160g {ECO:0000303|PubMed:15229592};
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC
1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
NCBI_TaxID=284590;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
WM37;
PubMed=15229592; DOI=10.1038/nature02579;
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
-!- FUNCTION: Serine/threonine protein kinase involved in the
cytoplasm to vacuole transport (Cvt) and found to be essential in
autophagy, where it is required for the formation of
autophagosomes. Involved in the clearance of protein aggregates
which cannot be efficiently cleared by the proteasome. Required
for selective autophagic degradation of the nucleus (nucleophagy)
as well as for mitophagy which contributes to regulate
mitochondrial quantity and quality by eliminating the mitochondria
to a basal level to fulfill cellular energy requirements and
preventing excess ROS production. Also involved in endoplasmic
reticulum-specific autophagic process, in selective removal of ER-
associated degradation (ERAD) substrates. Plays a key role in ATG9
and ATG23 cycling through the pre-autophagosomal structure and is
necessary to promote ATG18 binding to ATG9 through phosphorylation
of ATG9. {ECO:0000250|UniProtKB:P53104}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000250|UniProtKB:P53104}.
-!- SUBUNIT: Homodimer. Forms a ternary complex with ATG13 and ATG17.
{ECO:0000250|UniProtKB:P53104}.
-!- INTERACTION:
Q6CWK2:ATG13; NbExp=4; IntAct=EBI-16151357, EBI-16151385;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53104}.
Preautophagosomal structure membrane
{ECO:0000250|UniProtKB:P53104}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P53104}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. APG1/unc-51/ULK1 subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
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EMBL; CR382123; CAH01818.1; -; Genomic_DNA.
RefSeq; XP_452967.1; XM_452967.1.
ProteinModelPortal; Q6CSX2; -.
SMR; Q6CSX2; -.
DIP; DIP-61491N; -.
IntAct; Q6CSX2; 1.
STRING; 284590.XP_452967.1; -.
PRIDE; Q6CSX2; -.
EnsemblFungi; CAH01818; CAH01818; KLLA0_C17160g.
GeneID; 2892164; -.
KEGG; kla:KLLA0C17160g; -.
eggNOG; KOG0595; Eukaryota.
eggNOG; ENOG410XR01; LUCA.
HOGENOM; HOG000246715; -.
InParanoid; Q6CSX2; -.
KO; K08269; -.
OMA; EKLMYDR; -.
OrthoDB; EOG092C4IKY; -.
Proteomes; UP000000598; Chromosome C.
GO; GO:1990316; C:Atg1/ULK1 kinase complex; IEA:EnsemblFungi.
GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
GO; GO:0097635; C:extrinsic component of autophagosome membrane; IEA:EnsemblFungi.
GO; GO:0061908; C:phagophore; IEA:EnsemblFungi.
GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
GO; GO:0120095; C:vacuole-isolation membrane contact site; IEA:EnsemblFungi.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0000045; P:autophagosome assembly; IEA:EnsemblFungi.
GO; GO:0000422; P:autophagy of mitochondrion; IEA:EnsemblFungi.
GO; GO:0044805; P:late nucleophagy; IEA:EnsemblFungi.
GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
GO; GO:0046777; P:protein autophosphorylation; IEA:EnsemblFungi.
GO; GO:0032258; P:protein localization by the Cvt pathway; IEA:EnsemblFungi.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0061709; P:reticulophagy; IEA:EnsemblFungi.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR022708; Ser/Thr_kinase_C.
Pfam; PF12063; DUF3543; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Autophagy; Complete proteome; Cytoplasm; Kinase;
Membrane; Nucleotide-binding; Protein transport; Reference proteome;
Serine/threonine-protein kinase; Transferase; Transport.
CHAIN 1 831 Serine/threonine-protein kinase ATG1.
/FTId=PRO_0000085647.
DOMAIN 21 321 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 27 35 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 168 168 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 50 50 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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


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