ATG1_VANPO
ID ATG1_VANPO Reviewed; 994 AA.
AC A7TIZ4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
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 ORFNames=Kpol_541p49 {ECO:0000303|PubMed:17494770};
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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 -!- 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; DS480398; EDO17806.1; -; Genomic_DNA.
DR RefSeq; XP_001645664.1; XM_001645614.1.
DR AlphaFoldDB; A7TIZ4; -.
DR SMR; A7TIZ4; -.
DR STRING; 436907.A7TIZ4; -.
DR EnsemblFungi; EDO17806; EDO17806; Kpol_541p49.
DR GeneID; 5546060; -.
DR KEGG; vpo:Kpol_541p49; -.
DR eggNOG; KOG0595; Eukaryota.
DR HOGENOM; CLU_006447_0_0_1; -.
DR InParanoid; A7TIZ4; -.
DR OMA; INNVVQW; -.
DR OrthoDB; 1084750at2759; -.
DR PhylomeDB; A7TIZ4; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
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; 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; 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..994
FT /note="Serine/threonine-protein kinase atg1"
FT /id="PRO_0000317799"
FT DOMAIN 7..331
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 403..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 13..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 994 AA; 113085 MW; 9BD130D2C810CE81 CRC64;
MIISGKYVIE KEIGKGSFAT VLKGYIIDDN DNNGNDTNNE DVEVNDDKRK YTTRNQIAVK
AVPRSKLKNK KLLENLEVEI AILKKIKHPH IVRLIECERT STDFYLIMEY CALGDLTFLI
KKRQEIMENH PLLKSVFKRF PPPSKNHNGL HRAFILNYLQ QLSSSLKFLR SKNLVHRDIK
PQNLLLATPF VDYHDSKSFH DLGYVGISSL PILKIADFGF ARFLPNTSMA ETLCGSPLYM
APEILNYQKY NAKADLWSVG TVLYEMCYGK PPFKASNHLE LYKKIKKANN TISYSNDCEI
EDDLKDLINA LLTFDPNKRI GFQEFFDNKL VIEDLSKYEV ANEVYSELEL KSKSVLESNM
FISEYLPSEK KKDDTDNMII SNLSTNDRIN NITIFSNILP TVNENENDKT NDNSTTNYNN
NDNENNDNNN TNHNYNNDKV NNKSNDNNEK SDINRSNSNY KQHSTKQTTN ELIPNTNTIT
TNINDNSNSE MNSQSARMMQ KSKNYKSLRN NKLRNSKNDI INNSNSDLIL EKEYVVVEKK
SVEVNTLADE MAQIGQINNL NYKVPYPSRS PTLAGNVLQN NESLQHYQPF SVKSPRTSLS
SNGSGNSRRA SLVDRRLSIS SLNPSNALSR ALGVASTKLF GSNVLPNQNA GVGNANNINT
SMPLLNPQVF QDLTENILLR VDQLQGKDRI NIDSNSIVQI LESLAAKAFV VHSFAEVKFS
QTIPLKSLST STVNRPANDR RLNDRGCAIE EDDNIQTETY DTYIPSLKGR SLSSLSQTSI
CSQDLPHGEL YQLSKEAIIL YMKTLSILAT AMQITSNWWY QSNEKNCSLR LNLLVQWIRD
KFNECLERAD FLRIQILELE ECENKSNELN SDHTDVETSG VNETVHNNDN DANEEDQIYV
EKLLYDRALE ISRTAAKLEI QGDHLNNCEL AYATSLWMLE ILLDDRIEDD NFNEFSSKNS
AVLDDQDREI IKKYIDSIAN RLKALREKIS QGGS
