ATG1_PODAS
ID ATG1_PODAS Reviewed; 941 AA.
AC Q3ZDQ4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 69.
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:16278443};
OS Podospora anserina (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora.
OX NCBI_TaxID=2587412;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=16278443; DOI=10.1128/ec.4.11.1765-1774.2005;
RA Pinan-Lucarre B., Balguerie A., Clave C.;
RT "Accelerated cell death in Podospora autophagy mutants.";
RL Eukaryot. Cell 4:1765-1774(2005).
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:16278443).
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:16278443}.
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; AY953520; AAY28926.1; -; mRNA.
DR AlphaFoldDB; Q3ZDQ4; -.
DR SMR; Q3ZDQ4; -.
DR PRIDE; Q3ZDQ4; -.
DR VEuPathDB; FungiDB:PODANS_7_10890; -.
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 2: Evidence at transcript level;
KW ATP-binding; Autophagy; Cytoplasm; Kinase; Membrane; Nucleotide-binding;
KW Protein transport; Serine/threonine-protein kinase; Transferase; Transport.
FT CHAIN 1..941
FT /note="Serine/threonine-protein kinase ATG1"
FT /id="PRO_0000317797"
FT DOMAIN 26..331
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..887
FT /note="Basic and acidic 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 941 AA; 103814 MW; 1F79492F7F5392A3 CRC64;
MADRQLSSAS SSRRQKQPTD GAVGQFVIDK EIGKGSFAQV YSGRHKVTGA LVAIKSVELS
RLNKKLKENL YGEIKILKTL RHPHIVALHD CVESATHINL IMEYCELGDL SLFIKKREKL
ITHSATRDIA RRYPIEHNQG LHEVITRHFL KQLASALKFL REGNFVHRDV KPQNLLLLPS
PLFRETHHSA KQILSASYDS LMPAAGLPSL PMLKLADFGF ARVLPSTSLA ETLCGSPLYM
APEILRYERY DAKADLWSVG TVLYEMATGR PPFRAGNHVE LLRKIEAAED QVKFPRESVV
SPELKSLVRA LLKRNPVERI SFADFFNHTV ITGPIPNLHE DDLPKPEPQQ VKETVRPEGS
LSLSRRDSQR GKAATGVLSS PRPRPSSPLA TPIEKPNPLE QVPGPRAGLS YSPAGDGLGI
TRRPAVQPST SAPARPVMYV DRSRANSTAS QRPPRESIVP DPSQTLASQP RPKSRPTKPL
TEEEKAAQDV ALERDYIFID KKGVEVNALA DQISMYPQSV PKSGQIVRRA TQQGHPTSTT
GAVSARNNHL RQGSYDKPLS SSPGSTTSAI SKAIQDASLR LFGFNVAPHL LSKGQSPPQI
YSPFPAYPTP SAPAGLISDG KHTTPVDEDS RVAQCIEDWA TRSDVVYGFA EVKYKQLVPL
APSMDYGLGG VPADKMEEED GLTLEATVSL SEEALVLYVK ALSLLAKSMD IASLWWTRKS
RSDNSNSIHS AARDSVNSQA LALKINRVVQ WIRSRFNEVL EKAEIVRLKL IEAQKQLPED
HPSHPSNHQT EVSSVTGAEG VILSPGISAE KLMYDRAVEM SRTAAINEIA SEDLPGCEIF
YSTAIRMLEA VLDSDDDHLP KRRISTSSRD EKAEAAVRED TSEMSSEDKQ SIQKMIQMVK
ARLANLQKKM LAISRAQQQQ QQDIISVRRR SGEMAPRSVP V
