ATG1_PICAN
ID ATG1_PICAN Reviewed; 804 AA.
AC Q8TFN2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 83.
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};
DE AltName: Full=Peroxisome degradation deficient protein 7 {ECO:0000303|PubMed:12702243};
GN Name=ATG1 {ECO:0000303|PubMed:14536056};
GN Synonyms=PDD7 {ECO:0000303|PubMed:12702243};
OS Pichia angusta (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=870730;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC Y-5445;
RX PubMed=12702243; DOI=10.1016/s1567-1356(02)00135-6;
RA Komduur J.A., Veenhuis M., Kiel J.A.K.W.;
RT "The Hansenula polymorpha PDD7 gene is essential for micropexophagy and
RT microautophagy.";
RL FEMS Yeast Res. 3:27-34(2003).
RN [2]
RP NOMENCLATURE.
RX PubMed=14536056; DOI=10.1016/s1534-5807(03)00296-x;
RA Klionsky D.J., Cregg J.M., Dunn W.A. Jr., Emr S.D., Sakai Y.,
RA Sandoval I.V., Sibirny A., Subramani S., Thumm M., Veenhuis M., Ohsumi Y.;
RT "A unified nomenclature for yeast autophagy-related genes.";
RL Dev. Cell 5:539-545(2003).
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:12702243).
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:12702243}.
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; AY053423; AAL23618.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TFN2; -.
DR SMR; Q8TFN2; -.
DR PhylomeDB; Q8TFN2; -.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
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:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; Serine/threonine-protein kinase; Transferase; Transport.
FT CHAIN 1..804
FT /note="Serine/threonine-protein kinase ATG1"
FT /id="PRO_0000085650"
FT DOMAIN 12..308
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 339..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 18..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 804 AA; 89844 MW; 052186AA1F7FC585 CRC64;
MSKHQTQVVG DFTIGPEIGR GSFANVYKGY DNRTKAPVAV KSVFRSRLKN QKLVENLEIE
ISILKNLKNP HIVALLDCVK TDQYFHLFME YCSLGDLSYF IRRRDQLVQT HPLISSILER
YPSPPNSHGL NKVLVVNFLK QLASALEFLR DQNLVHRDIK PQNLLLSPPV HSKEEFKRKG
YSGLWELPVL KIADFGFARF LPSTSMAETL CGSPLYMAPE ILRYEKYNAK ADLWSVGAVI
YEMSVGKPPF RASNHVELLR KIEKSKDEIT FPVSAEVPDD LVRLICGLLK ANPTERMGFQ
EFFNDPLIVY DVQCADEPLE CSNVDEQLFI SEYLPNLKTS PPAKPAPETI KEESEEEERA
ERAPTDSLLI GKEADLRIPR PMEGSGKDEV IKKLINKSSP PPDTVKDGQI KKGARRDKDD
FVYEKDYVVV EKRTVEVNAI ADELAKAGAG AVAIPSPHLG TNEHSAANPS GPTETQTQRR
FSPSSRTSSI GSNRRPSWGD RKMPISISPT NALTKALGYT SNRLFGQQQQ QPQQAQQAAI
ESAITNVTTN LLATKTLRPL KPSQETSLED TEVINQLELL ATMAHAISLF AEVKFSQLIP
LPPSSSSPGS ADYDEMYQND AFPPQMVKSI SSEGVALYVE TLSLLAKAMS IASDWWHQNS
SKPSTSPKLN DLVQWIRSRF NESLEKAEFL RLRLADANEQ LVGESGSSLN KPVVAEKLIF
DRALEMSRTA AMNELKNEDL LGCELSYSTA IWMLEALLSN DEEPVTGNEK LDAEDKKIIE
LFINSIGNRL KVLRQKIDKQ GVRS
