ATG13_ASHGO
ID ATG13_ASHGO Reviewed; 659 AA.
AC Q758N2;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Autophagy-related protein 13;
GN Name=ATG13; OrderedLocusNames=AEL277C;
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: Activates the ATG1 kinase in a nutritional condition
CC dependent manner through the TOR pathway, leading to autophagy. Also
CC involved in cytoplasm to vacuole transport (Cvt) and more specifically
CC in Cvt vesicle formation. Seems to play a role in the switching
CC machinery regulating the conversion between the Cvt pathway and
CC autophagy. Finally, ATG13 is also required for glycogen storage during
CC stationary phase (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ATG1 to form the ATG1-ATG13 kinase complex.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06628}.
CC Preautophagosomal structure {ECO:0000250|UniProtKB:Q06628}.
CC -!- SIMILARITY: Belongs to the ATG13 family. Fungi subfamily.
CC {ECO:0000305}.
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DR EMBL; AE016818; AAS52407.1; -; Genomic_DNA.
DR RefSeq; NP_984583.1; NM_209936.2.
DR AlphaFoldDB; Q758N2; -.
DR SMR; Q758N2; -.
DR STRING; 33169.AAS52407; -.
DR EnsemblFungi; AAS52407; AAS52407; AGOS_AEL277C.
DR GeneID; 4620763; -.
DR KEGG; ago:AGOS_AEL277C; -.
DR eggNOG; KOG4573; Eukaryota.
DR HOGENOM; CLU_411076_0_0_1; -.
DR InParanoid; Q758N2; -.
DR OMA; YAKLHRP; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0120095; C:vacuole-isolation membrane contact site; IEA:EnsemblFungi.
DR GO; GO:0019887; F:protein kinase regulator activity; IEA:EnsemblFungi.
DR GO; GO:0032147; P:activation of protein kinase activity; IEA:EnsemblFungi.
DR GO; GO:0071255; P:Cvt vesicle assembly; IEA:EnsemblFungi.
DR GO; GO:0044805; P:late nucleophagy; IEA:EnsemblFungi.
DR GO; GO:0000423; P:mitophagy; IBA:GO_Central.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
DR GO; GO:0071211; P:protein targeting to vacuole involved in autophagy; IEA:EnsemblFungi.
DR Gene3D; 3.30.900.10; -; 1.
DR InterPro; IPR040182; ATG13.
DR InterPro; IPR018731; Atg13_N.
DR InterPro; IPR036570; HORMA_dom_sf.
DR PANTHER; PTHR13430; PTHR13430; 1.
DR Pfam; PF10033; ATG13; 1.
PE 3: Inferred from homology;
KW Autophagy; Cytoplasm; Protein transport; Reference proteome; Transport.
FT CHAIN 1..659
FT /note="Autophagy-related protein 13"
FT /id="PRO_0000157964"
FT REGION 260..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 659 AA; 71590 MW; 0D82A58B6A741150 CRC64;
MAMESECNVV ELIGGFFLKA TLLVCQPRTG AIEGDGEEDR TFNISSAADA GVAEAVRAWT
AYDGAQELPP LVIEMFLDLR RLGPQHTVVL KDQDGNPWNV CKGGKKSEIM LERWLVELDV
GNEEARPEEP PNAAEIYKQL VLLFRYLYTL TQLLPANELY ARLHGPSNQG EAAMPLINIG
TRILDGSKPI LSKGRVGLSR SIIATYTNVI NETNVASHLE QKKITPISTG YGSLRITVSY
RRDCNFDVNE VLDYEGNNCS SSSVVDTHTK PGVGPLSSLR RVSIHSNRSM SISPQTVYSG
TVIPDPSPQR KSSSSRIQPF KAGSVGSGSL AIARNPSGSS AVATLRAQRS GSASISTHVA
DQAVGEPSSV GSGGSKYSSS FGKIRRQSSM RRSGSLELPA AKQAKPGERG SDELLDFVKM
LEEKQELNVK KLYGTTTDIS SSLVRFQSMK SNNDTLSEDL SMSYSLEPTH APQVRYRSNS
HSPIPSISPS VQYTSIPMRL SQSRNVSQTE LASRKNSAER LKTLISSRTG SFSESRRQSN
AGQEDILEDE DDEAEEILLS KSHLSNPTGT RLQSMSPQSL KSISSYNRAA VPFKPVSNFS
CPTTMATPAH AKLHKASISS SPDNQSGLVK KDHEHSTMTG GDDDDDLLFF MSDMNLSSQ
