ATG1_DICDI
ID ATG1_DICDI Reviewed; 668 AA.
AC Q86CS2; Q54D55;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
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; Synonyms=apg1; ORFNames=DDB_G0292390;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=AX3 / DH1;
RX PubMed=12626495; DOI=10.1074/jbc.m212467200;
RA Otto G.P., Wu M.Y., Kazgan N., Anderson O.R., Kessin R.H.;
RT "Macroautophagy is required for multicellular development of the social
RT amoeba Dictyostelium discoideum.";
RL J. Biol. Chem. 278:17636-17645(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP FUNCTION.
RX PubMed=15358773; DOI=10.1074/jbc.m408924200;
RA Kosta A., Roisin-Bouffay C., Luciani M.-F., Otto G.P., Kessin R.H.,
RA Golstein P.;
RT "Autophagy gene disruption reveals a non-vacuolar cell death pathway in
RT Dictyostelium.";
RL J. Biol. Chem. 279:48404-48409(2004).
RN [4]
RP FUNCTION.
RX PubMed=16810325; DOI=10.1038/sj.cdd.4401994;
RA Laporte C., Kosta A., Klein G., Aubry L., Lam D., Tresse E., Luciani M.F.,
RA Golstein P.;
RT "A necrotic cell death model in a protist.";
RL Cell Death Differ. 14:266-274(2007).
RN [5]
RP FUNCTION.
RX PubMed=17557329; DOI=10.1002/prot.21444;
RA Miranda-Saavedra D., Barton G.J.;
RT "Classification and functional annotation of eukaryotic protein kinases.";
RL Proteins 68:893-914(2007).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19667176; DOI=10.1073/pnas.0813319106;
RA Jia K., Thomas C., Akbar M., Sun Q., Adams-Huet B., Gilpin C., Levine B.;
RT "Autophagy genes protect against Salmonella typhimurium infection and
RT mediate insulin signaling-regulated pathogen resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:14564-14569(2009).
CC -!- FUNCTION: Serine/threonine protein kinase involved in autophagy
CC (PubMed:12626495, PubMed:17557329). Involved in the control of
CC autophagic vacuolar cell death (PubMed:15358773, PubMed:16810325).
CC Required for normal survival when exposed to pathogenic bacteria
CC S.typhimurium by promoting autophagic degradation of intracellular
CC S.typhimurium (PubMed:19667176). {ECO:0000269|PubMed:12626495,
CC ECO:0000269|PubMed:15358773, ECO:0000269|PubMed:16810325,
CC ECO:0000269|PubMed:17557329, ECO:0000269|PubMed:19667176}.
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 -!- DISRUPTION PHENOTYPE: Impaired survival when exposed to pathogenic
CC bacteria S.typhimurium associated with the accumulation of
CC S.typhimuriumin in large vacuoles which fail to undergo autophagy.
CC {ECO:0000269|PubMed:19667176}.
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; AY191011; AAO39074.1; -; Genomic_DNA.
DR EMBL; AAFI02000190; EAL61174.1; -; Genomic_DNA.
DR RefSeq; XP_629641.1; XM_629639.1.
DR AlphaFoldDB; Q86CS2; -.
DR SMR; Q86CS2; -.
DR STRING; 44689.DDB0185178; -.
DR PaxDb; Q86CS2; -.
DR EnsemblProtists; EAL61174; EAL61174; DDB_G0292390.
DR GeneID; 8628705; -.
DR KEGG; ddi:DDB_G0292390; -.
DR dictyBase; DDB_G0292390; atg1.
DR eggNOG; KOG0595; Eukaryota.
DR HOGENOM; CLU_411314_0_0_1; -.
DR InParanoid; Q86CS2; -.
DR OMA; CCEGGDF; -.
DR Reactome; R-DDI-1632852; Macroautophagy.
DR Reactome; R-DDI-8854214; TBC/RABGAPs.
DR Reactome; R-DDI-8934903; Receptor Mediated Mitophagy.
DR PRO; PR:Q86CS2; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IDA:dictyBase.
DR GO; GO:0005776; C:autophagosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
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:0004672; F:protein kinase activity; IDA:dictyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:dictyBase.
DR GO; GO:0048102; P:autophagic cell death; IMP:dictyBase.
DR GO; GO:1905037; P:autophagosome organization; IMP:dictyBase.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IMP:dictyBase.
DR GO; GO:0042742; P:defense response to bacterium; IMP:dictyBase.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:dictyBase.
DR GO; GO:0035891; P:exit from host cell; IMP:dictyBase.
DR GO; GO:0016236; P:macroautophagy; IMP:dictyBase.
DR GO; GO:0070265; P:necrotic cell death; IDA:dictyBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IMP:dictyBase.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:dictyBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0009617; P:response to bacterium; IMP:dictyBase.
DR GO; GO:0001878; P:response to yeast; IMP:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
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 PANTHER; PTHR24348; PTHR24348; 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..668
FT /note="Serine/threonine-protein kinase atg1"
FT /id="PRO_0000327584"
FT DOMAIN 7..266
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 281..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 135
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 36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 668 AA; 77175 MW; 41B9D9DFD83A2D0C CRC64;
MKRVGDYILD KRIGWGAFAQ VYKGFSIKTN EPFAIKVVDV CRLADKNSKL TENLNYEIRI
LKELSHTNIV RLYDVLNEET DPTFIYMIME CCEGGDFSKY IRTHKKLTEE KALYFMKQLA
NGLKFLRQKQ IVHRDLKPQN LLLSDDSEHP ILKIGDFGFA KFIDPFSLSD TFCGSPLYMA
PEILHRKNYT VKADLWSVGI ILYEMLVGEP AYNSGSVPDL LNQLQNKKIK LPSHISSDCQ
NLIYSLLQID VEKRISWEDF FNHKWLNLNN NDSYKNNSGN YFNNNNINNN NNNNTNNNNN
NISYPISINS NNTNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNYY NNNNSPPNVY
HASSLPYDFN NNNNNNNSNN YNNNTNVPNS LPFAYNNNIY SSPTEAIPQP TTLNKSKSLE
NTGNTIRAHP FKDDKKSTTI QQPQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ NRQLSNLSTD
FERDLVILDG EELESMERVF NRAVAIAELG DLRQNEPLEC VPLYILALKL MKSKIPNDPS
SSPDKFINTF TEYKRKLVHI FSTSNTSVKN QDHHSSFSPN RFIYENALEF GKKGAVEELY
NNYPTSLQFY TDGTLLLEYL SSIVIDSDDQ EIIKKYLNAF EVRTQICKKN YENSKNTVLN
TNSIQNNT
