ATG1_PENRW
ID ATG1_PENRW Reviewed; 960 AA.
AC A7KAL2; B6HBB5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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:17204848};
GN ORFNames=Pc18g03490 {ECO:0000303|PubMed:18820685};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=17204848; DOI=10.4161/auto.3595;
RA Meijer W.H., van der Klei I.J., Veenhuis M., Kiel J.A.K.W.;
RT "ATG genes involved in non-selective autophagy are conserved from yeast to
RT man, but the selective Cvt and pexophagy pathways also require organism-
RT specific genes.";
RL Autophagy 3:106-116(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
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:17204848).
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:17204848}.
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; EF107734; ABO31072.1; -; Genomic_DNA.
DR EMBL; AM920433; CAP94573.1; -; Genomic_DNA.
DR RefSeq; XP_002562187.1; XM_002562141.1.
DR AlphaFoldDB; A7KAL2; -.
DR SMR; A7KAL2; -.
DR STRING; 1108849.XP_002562187.1; -.
DR PRIDE; A7KAL2; -.
DR EnsemblFungi; CAP94573; CAP94573; PCH_Pc18g03490.
DR GeneID; 8305112; -.
DR KEGG; pcs:Pc18g03490; -.
DR VEuPathDB; FungiDB:PCH_Pc18g03490; -.
DR eggNOG; KOG0595; Eukaryota.
DR HOGENOM; CLU_006447_0_0_1; -.
DR OMA; INNVVQW; -.
DR OrthoDB; 1084750at2759; -.
DR BioCyc; PCHR:PC18G03490-MON; -.
DR Proteomes; UP000000724; Contig Pc00c18.
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; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Transport.
FT CHAIN 1..960
FT /note="Serine/threonine-protein kinase atg1"
FT /id="PRO_0000317795"
FT DOMAIN 22..327
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 333..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 28..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 960 AA; 104745 MW; D54DFC78DA5C4B30 CRC64;
MASQHSRRSR EAPRPEMSIG RYTRLDEIGR GSFATVYQGV HTKSKTYVAI KSVNLSKLNK
KLKENLSSEI DILKGLHHPH IVALIDCHES TSHIHLVMEY CALGDLSLFI KRRDTLGSHK
YTRDMIAKYP NPPGGSLNEV VTRHFLKQLS SALKFLRDRN LIHRDIKPQN LLLCPSPSSY
RSGHAQVMPY KGSDDSYEPT TGLESLPMLK IADFGFARSL PATSLAETLC GSPLYMAPEI
LRYEKYDAKA DLWSVGTVLY EMVVGRPPFR ATNHVELLRK IEKGEDRIRF PEDNPASDDI
KKLIRGLLKR NPVERLNFPE FFSNNVINDP IPGLLADDAP GPPQSPRPRQ LVGKAEESPY
DTGPEDKLAY PPGQRPVTTH PKSGTPPTAT DMRRMGSADR PAPAISKEQQ PGGTPPQRPG
PVSLATAPGR QELIDRNATT AAMDRQRHRN TYAGAPKASD STIRAQEARD RAAQEVAFER
DYVVVEKRAV EVNAFADELA HSPRLQGGLS RPGQTGAGSR RTTTQGLPTV SPSSPHANAA
KAMQVVSGRA RADSTHQRQH SYERRYGQSP TSATSAISKA LNMASGRLFG MGFSPPLAIT
KGGRSPPLAY NPFPAYPPVH ASLLITGDGS KPNATGDEDC KAVQEIEECA TRSDVVFGFA
EVKYKQLIPL APSASTDPSA RPMDTNVEPD SADSDDGLTV DAIVTLSEEA LVLYVKALSL
LAKSMDIAGA WWSRKNREEV YGESPTKDSM SAVAGTRINY VVQWVRSRFN EVIEKAEFVR
LKLIEGQRRL PPDHPSHPDN HSISSTAGSS STADVVVSPG VTAERLMYDR ALEMSRAAAI
NELTGEDLAN CEITYVTAIR MLEAVLEDDG MRSMPGSNIE RQSSSQGGEK VVLDELQVED
RQVVVKLVSS MRGRLASVRK KVAVLAKRSS APTPTAGSAG KTPTSNISPV TYATGVTPPR
