ATG1_SCHPO
ID ATG1_SCHPO Reviewed; 830 AA.
AC Q9Y7T4;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Serine/threonine-protein kinase atg1 {ECO:0000312|PomBase:SPCC63.08c};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P53104};
DE AltName: Full=Autophagy-related protein 1 {ECO:0000250|UniProtKB:P53104};
DE AltName: Full=Serine/threonine-protein kinase ppk36 {ECO:0000305};
GN Name=atg1 {ECO:0000312|PomBase:SPCC63.08c};
GN Synonyms=ppk36 {ECO:0000312|PomBase:SPCC63.08c};
GN ORFNames=SPCC63.08c {ECO:0000312|PomBase:SPCC63.08c};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP IDENTIFICATION.
RX PubMed=15821139; DOI=10.1128/ec.4.4.799-813.2005;
RA Bimbo A., Jia Y., Poh S.L., Karuturi R.K.M., den Elzen N., Peng X.,
RA Zheng L., O'Connell M., Liu E.T., Balasubramanian M.K., Liu J.;
RT "Systematic deletion analysis of fission yeast protein kinases.";
RL Eukaryot. Cell 4:799-813(2005).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP FUNCTION, PHOSPHORYLATION, AND DEPHOSPHORYLATION.
RX PubMed=17295836; DOI=10.1111/j.1365-2443.2007.01041.x;
RA Kohda T.A., Tanaka K., Konomi M., Sato M., Osumi M., Yamamoto M.;
RT "Fission yeast autophagy induced by nitrogen starvation generates a
RT nitrogen source that drives adaptation processes.";
RL Genes Cells 12:155-170(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [6]
RP FUNCTION.
RX PubMed=19778961; DOI=10.1099/mic.0.034389-0;
RA Mukaiyama H., Kajiwara S., Hosomi A., Giga-Hama Y., Tanaka N., Nakamura T.,
RA Takegawa K.;
RT "Autophagy-deficient Schizosaccharomyces pombe mutants undergo partial
RT sporulation during nitrogen starvation.";
RL Microbiology 155:3816-3826(2009).
RN [7]
RP DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=23950735; DOI=10.1371/journal.pgen.1003715;
RA Sun L.L., Li M., Suo F., Liu X.M., Shen E.Z., Yang B., Dong M.Q., He W.Z.,
RA Du L.L.;
RT "Global analysis of fission yeast mating genes reveals new autophagy
RT factors.";
RL PLoS Genet. 9:E1003715-E1003715(2013).
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 (By similarity). Autophagy functions to supply nitrogen and is
CC activated when cells cannot access exogenous nitrogen, thus ensuring
CC that they can adapt and subsequently propagate (PubMed:17295836,
CC PubMed:19778961). Finally, atg13 is also required for glycogen storage
CC during stationary phase and has a role in meiosis and sporulation
CC (PubMed:17295836, PubMed:19778961). {ECO:0000250|UniProtKB:P53104,
CC ECO:0000269|PubMed:17295836, ECO:0000269|PubMed:19778961}.
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 -!- PTM: Phosphorylated. Dephosphorylated under depletion of nitrogen.
CC {ECO:0000269|PubMed:17295836}.
CC -!- DISRUPTION PHENOTYPE: Impairs atg8-processing.
CC {ECO:0000269|PubMed:23950735}.
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; CU329672; CAB40012.1; -; Genomic_DNA.
DR PIR; T41509; T41509.
DR RefSeq; NP_587982.1; NM_001022973.2.
DR AlphaFoldDB; Q9Y7T4; -.
DR SMR; Q9Y7T4; -.
DR BioGRID; 276024; 65.
DR STRING; 4896.SPCC63.08c.1; -.
DR iPTMnet; Q9Y7T4; -.
DR MaxQB; Q9Y7T4; -.
DR PaxDb; Q9Y7T4; -.
DR PRIDE; Q9Y7T4; -.
DR EnsemblFungi; SPCC63.08c.1; SPCC63.08c.1:pep; SPCC63.08c.
DR GeneID; 2539461; -.
DR KEGG; spo:SPCC63.08c; -.
DR PomBase; SPCC63.08c; atg1.
DR VEuPathDB; FungiDB:SPCC63.08c; -.
DR eggNOG; KOG0595; Eukaryota.
DR HOGENOM; CLU_006447_1_0_1; -.
DR InParanoid; Q9Y7T4; -.
DR OMA; EIRHVHV; -.
DR PhylomeDB; Q9Y7T4; -.
DR Reactome; R-SPO-1632852; Macroautophagy.
DR Reactome; R-SPO-8854214; TBC/RABGAPs.
DR Reactome; R-SPO-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Reactome; R-SPO-8934903; Receptor Mediated Mitophagy.
DR PRO; PR:Q9Y7T4; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; EXP:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000407; C:phagophore assembly site; IDA:PomBase.
DR GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:PomBase.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IMP:PomBase.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:PomBase.
DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; IMP:PomBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042594; P:response to starvation; IBA:GO_Central.
DR GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
DR GO; GO:0023052; P:signaling; NAS:PomBase.
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 1: Evidence at protein level;
KW ATP-binding; Autophagy; Cytoplasm; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Protein transport; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Transport.
FT CHAIN 1..830
FT /note="Serine/threonine-protein kinase atg1"
FT /id="PRO_0000085652"
FT DOMAIN 14..307
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 448..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 157
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 20..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 830 AA; 91585 MW; 8DB76C502BD83425 CRC64;
MNLQTSTNQT IGPYVIRSEI GRGSFAIVYK GKHTETNRVI SIKSVLTKKL TKKLLENLES
EISILKEIRH VHVVELIDCI KAGRFIHLVM EYCSLGDLSY FIRKREKFNS IPSLAWINID
HPPVYKAGLN ETLVRHFTQQ LASALQFLRS RSLIHRDVKP QNLLLQPPPT AAYLEEHPQF
VGSPKLPMLK LADFGFARYL QTSSMAETLC GSPLYMAPEI LRYEKYDAKA DLWSVGAVLY
EMAVGKPPFK APNHVELLRR IQKAKDVIKF PEEAFIHPDI KTLICALLKQ NPADRIDYDG
FFSSIVVTTP LDDASTLTGS DIQDAVKEIN IPSSSPAYIT DFFPKSNPGA PAPPGGLLRQ
AFQAQGSSIQ PSEITGRRVP HRYAQDGNTL PYTPVFPPES APAASIFPPR LTSKQPIPMA
SPAKLTSDTS NKSSAYVVVD HHPIISSTQL SNESLTHEQS INGNSPSPNE GVFQGSFSPE
SAPVNNHAFP HTSRMQIPYM KPNAFPSNPT YIASTPVTQL RRAFEQATAH VPQSGGGARN
KSALERALNV ANARLNEVVV DGMTDNGNTS LPTKESNLDN NVNIIQPSLP DTGKRLLDVL
ESIAMKSNSV YHLAEVKLAQ IIPSLSDEMK PGDTLLDRPL TPFSLVMLAK ESYVLYERDI
ELLQVAFDGV AAFWANSEER ASPDCQQAIE WFRQRYSESL EKSQFLREII ISQSAAHSLP
TTKPVSASQL IYHRALDLSR NAATSELSGN DAQACLQNYR LAAHLLESLL ESNFSTPDGA
NDSNNSVTIR NLIALITKRQ ELLQSKQIQA NVANKVTESV AKITLAPNLA
