ATG1_PICPA
ID ATG1_PICPA Reviewed; 796 AA.
AC Q8TGI1;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 79.
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};
DE AltName: Full=Glucose-induced selective autophagy protein 10 {ECO:0000303|PubMed:11533052};
DE AltName: Full=Pexophagy zeocin-resistant mutant protein 1;
GN Name=ATG1 {ECO:0000303|PubMed:14536056};
GN Synonyms=GSA10, PAZ1 {ECO:0000303|PubMed:11533052};
OS Komagataella pastoris (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=4922;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=11533052; DOI=10.1074/jbc.m104087200;
RA Stromhaug P.E., Bevan A., Dunn W.A. Jr.;
RT "GSA11 encodes a unique 208-kDa protein required for pexophagy and
RT autophagy in Pichia pastoris.";
RL J. Biol. Chem. 276:42422-42435(2001).
RN [2]
RP NOMENCLATURE.
RX PubMed=14536056; DOI=10.1016/s1534-5807(03)00296-x;
RA Klionsky D.J., Cregg J.M., Dunn W.A. Jr., Emr S.D., Sakai Y.,
RA Sandoval I.V., Sibirny A., Subramani S., Thumm M., Veenhuis M., Ohsumi Y.;
RT "A unified nomenclature for yeast autophagy-related genes.";
RL Dev. Cell 5:539-545(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 (PubMed:11533052).
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:11533052}.
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; AY075104; AAL77195.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TGI1; -.
DR SMR; Q8TGI1; -.
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; Serine/threonine-protein kinase; Transferase; Transport.
FT CHAIN 1..796
FT /note="Serine/threonine-protein kinase ATG1"
FT /id="PRO_0000085651"
FT DOMAIN 9..304
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 360..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 155
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 15..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 796 AA; 90050 MW; 3CFAAE3FE61413FA CRC64;
MPDRKIGDYV VGAEIGRGSF ANVYKGYNSK TQVSVAIKSV IKSRLRNKKL IENLEVEISI
LKNLKHPHVV ALLDCEQSKH YFHLLMEYCS LGDLSYFITK REELISNHPL ITGVFKKYPS
PENSKGLNEV ITINFVQQLA SALKFLRSQN LVHRDIKPQN LLLSPPVSRE VFEDRKYTGL
WELPVLKIAD FGFARFLPAT SMAETLCGSP LYMAPEILRY EKYNAKADLW SVGAVVYEMS
VGTPPFPAHN HVELLRNIER QKDKISFPKV AQVPPEIIQL ICGLLKQQAT ERMSFQEFFN
DPVITTKLQP CSDEPLLPQN QHIDENLFIS EYLPRNSITD KNINNNITNI AKNGVEEALL
EEEDEEEDQD QLPSKNDNIQ HMEPDSSMLL NKTTQKQTEV QSQPRRELVS EKDYVVVEKR
AVEVNALADE LEHAGSGALA MQLTNNVGTP YTRRYSSSSR SSSTGSNQRR PSFGDRKVPI
SISPTNALSK AINIASNRLF KQPSPPKATP VLLEEKDKDK NTERLTSTVF NQNMLNSTTT
REITRPLHSL TITSSTSDEE IIQRLSNLTT KAYAIKLLAE IKFSQLAPLP PSNETAVFDN
YGDDEGTQSG YNNEPLSPIL IKTIGEEGIA LYVKTLFLLS KAMNIAMEWW RLNSLSRPAS
PKLNDLVQWI RGKFNESLEK AEFIKLKLQN AKEQLEESES DTDKTVVAEK LIFDRAIEIS
RIAVVNELKN DDLVGTELSY ATAIWMLEAL LEPDDTEESK LDDEDRKMIE KFISSIGNRL
SVLRKKIEST SQETRK
