ATG1_NEUCR
ID ATG1_NEUCR Reviewed; 968 AA.
AC Q7RX99;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Serine/threonine-protein kinase apg-1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P53104};
DE AltName: Full=Autophagy-related protein 1 {ECO:0000250|UniProtKB:P53104};
GN Name=apg-1 {ECO:0000312|EMBL:EAA27175.2};
GN Synonyms=atg1 {ECO:0000250|UniProtKB:P53104};
GN ORFNames=NCU00188 {ECO:0000312|EMBL:EAA27175.2};
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(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. 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM002238; EAA27175.2; -; Genomic_DNA.
DR RefSeq; XP_956411.2; XM_951318.2.
DR AlphaFoldDB; Q7RX99; -.
DR SMR; Q7RX99; -.
DR STRING; 5141.EFNCRP00000000238; -.
DR PRIDE; Q7RX99; -.
DR EnsemblFungi; EAA27175; EAA27175; NCU00188.
DR GeneID; 3872551; -.
DR KEGG; ncr:NCU00188; -.
DR VEuPathDB; FungiDB:NCU00188; -.
DR HOGENOM; CLU_006447_0_0_1; -.
DR InParanoid; Q7RX99; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0097635; C:extrinsic component of autophagosome membrane; IEA:EnsemblFungi.
DR GO; GO:0061908; C:phagophore; IEA:EnsemblFungi.
DR GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR GO; GO:0120095; C:vacuole-isolation membrane contact site; IEA:EnsemblFungi.
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; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
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 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..968
FT /note="Serine/threonine-protein kinase apg-1"
FT /id="PRO_0000085649"
FT DOMAIN 24..329
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 334..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 30..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 968 AA; 107010 MW; EB47F9F22ACDC3FB CRC64;
MSDRTSASSS SRRTKQNYDA IGSFVIDQEI GKGSFAKVYL GRHKVTGALV AVKSVELARL
NKKLKENLYG EIQILKTLRH PHIVALHDCV ESSTHINLIM EYCELGDLSL FIKKRDKLIT
NPYTHDLARK YPVYPNAGLN EVVTRHFLKQ LASALQFLRA GDFVHRDVKP QNLLLLPSPH
MMANNKTAKH IMSGSYDSFT PAAGLASAPM LKLADFGFAR VLPSTSLAET LCGSPLYMAP
EILRYEKYDA KADLWSVGTV LYEMVTGRPP FKASNHVELL RKIESSGDVI KFTRESVVSQ
EMKGLIRALL KKNPVERISF EDLFNHPVVT EPIPGLVEDD IPKPPRRRSL KEERPVSRAE
DSLVPSRKQS LRKDLADREG APQTAGPSSP KPRRSSPLAT PNEPVEISKP NYFQIPPRED
RLSYSPRKEA ADGLGIKRPQ VQPSTSAPTR PSSYVDRRHR SSNASLRAPV REANPPPNDV
TRTKPRGMGT KPMTEEERAA QDIAFERDYV LVDKKHLEVN ALADQISMYP QQPQSPKSAQ
IVRRATQQGS PTSTSGAVPS PPSRALQLAQ GHSRQGSYDK ALGTSPSKAT SVISKAIQDA
SLRLFGFKYA PHLLSKGPSP VPMYNPFPTY PAPNTPTGLI SDGKQGTPVD EDSRVAQCIE
DHATRSDVVY GFAEVKYKQL VPLAPSMDHG LGGAPIEKSA EEDGLTAEAI VSLSEEALVL
YVKALTLLAK SMDIASLWWS RKNKVESTNS ITSAARDSAN SEALALRING AVQWIRSRFN
EVLEKAEIVR LKLAEAQKRL PEDHPSHPNN HANDSTALNS LSTVGVFLSE GISAERLMYD
RAIEMSRAAA INEIANEDLP GCEISYITAI RMLEAVLDQD DDHLPKRKVS GASKEEKTGA
NELSDEMNNE DKQVVQNVIN MVNNRLTVLR KKLRLIESAS KAQQQEEQKQ QNLMRRRSGE
MTSRSVPA
