(data stored in ACNUC7421 zone)

SWISSPROT: ATG1_ASHGO

ID   ATG1_ASHGO              Reviewed;         972 AA.
AC   Q75CH3;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 97.
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   OrderedLocusNames=ACL054W {ECO:0000303|PubMed:15001715};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(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       {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}.
DR   EMBL; AE016816; AAS51174.1; -; Genomic_DNA.
DR   RefSeq; NP_983350.1; NM_208703.1.
DR   SMR; Q75CH3; -.
DR   STRING; 33169.AAS51174; -.
DR   EnsemblFungi; AAS51174; AAS51174; AGOS_ACL054W.
DR   GeneID; 4619475; -.
DR   KEGG; ago:AGOS_ACL054W; -.
DR   HOGENOM; HOG000246715; -.
DR   InParanoid; Q75CH3; -.
DR   KO; K08269; -.
DR   OMA; CEIAYVT; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:1990316; C:Atg1/ULK1 kinase complex; IEA:EnsemblFungi.
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; IEA:UniProtKB-SubCell.
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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000045; P:autophagosome assembly; IEA:EnsemblFungi.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IEA:EnsemblFungi.
DR   GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IEA:EnsemblFungi.
DR   GO; GO:0044805; P:late nucleophagy; IEA:EnsemblFungi.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR   GO; GO:0046777; P:protein autophosphorylation; IEA:EnsemblFungi.
DR   GO; GO:0061709; P:reticulophagy; IEA:EnsemblFungi.
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   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;
DR   PRODOM; Q75CH3.
DR   SWISS-2DPAGE; Q75CH3.
KW   ATP-binding; Autophagy; Cytoplasm; Kinase; Membrane; Nucleotide-binding;
KW   Protein transport; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase; Transport.
FT   CHAIN           1..972
FT                   /note="Serine/threonine-protein kinase ATG1"
FT                   /id="PRO_0000085638"
FT   DOMAIN          18..319
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   NP_BIND         24..32
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        166
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         48
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   972 AA;  109057 MW;  F2EFF374025DDFAE CRC64;
     MNNVKSGGRP VAIVAERYVV EKEIGRGSFA VVYKGHLADS SAGNVAIKAV SRSKLRNKKL
     LENLEIEIAI LKKIKHPHIV GLLECERTGT DFYLMMEYCA LGDLTFFIKK RRSLMDKHPL
     VRTLFEKYPP PSEHHNGLNR VLVVNYLQQL SSALKFLRSK NLVHRDIKPQ NLLLSTPLVD
     YNDPAEFHAR GFVGIYNLPI LKIADFGFAR FLPNTSLAET LCGSPLYMAP EILNYQKYNA
     KADLWSVGTV LYEMCCGKPP FKASNHLELF QKIKKANDVI QFPKHAALES AMVDLICGLL
     TFEPAKRMGF TEFFSNGLVN EDLSPYEVES EPDLETKSKN VAESNMFISE YLPTAERNKR
     ASPIRLGDSC TLRGPCESPQ GADPYPQDNT QSDQHEHLHA DYSFQVEMGQ DGQQADGEEK
     RKLYNNQEER SNEERQFGQV SNGRNQEDQL LLHQGRGQIP CEQNRQALQS HSHVAAKQIP
     DKDSKSSVSC QKHAASAPTK NDHRTTRLKE KTKCSYSDLL LEKEYVVVEK KSVEVNALAD
     EFAQAGSGAP AIRLPDQHHN DASQALQMAR HSSTSVSAAN TAKQTLLRRN SRTLSSSGAS
     TSRRPSLVDR RLSITSLGAT NALSKALGMA SLRLFGNSHQ QSSNGSSTFK QNPNVTSLLS
     PQTFQDMTEN AVLSADHQWD NSRQADVLHD DSIMKALENL TAKVYAIYSF AEVKFSQIIP
     LPPSSTQDPY THKRMSNGSC AIDDEEDDIE HSPGAETYRK NSSGANANTG NYNFSLDTIH
     EMNLNDLPPN DLYILCTEAI VLYMKSLSLL AYAMHLTSKW WHESADKICP LKLNLLVQWI
     RERFNECLEK AEFLRMKTQS IQLHNGNQLS ASTMVSEPVF VEKLIYDRAL DISKTAAKME
     MQGEYLEGCE VAYSTSLWML EALLDDVSDE DNYNDDNLGH TGVLDKSDKE VIKRYIDSIA
     NRLKALRRKL SR
//

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