ATG13_CANGA
ID ATG13_CANGA Reviewed; 660 AA.
AC Q6FSJ9;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Autophagy-related protein 13;
GN Name=ATG13; OrderedLocusNames=CAGL0G09999g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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}.
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; CR380953; CAG59722.1; -; Genomic_DNA.
DR RefSeq; XP_446795.1; XM_446795.1.
DR AlphaFoldDB; Q6FSJ9; -.
DR SMR; Q6FSJ9; -.
DR STRING; 5478.XP_446795.1; -.
DR EnsemblFungi; CAG59722; CAG59722; CAGL0G09999g.
DR GeneID; 2888156; -.
DR KEGG; cgr:CAGL0G09999g; -.
DR CGD; CAL0129383; CAGL0G09999g.
DR VEuPathDB; FungiDB:CAGL0G09999g; -.
DR eggNOG; KOG4573; Eukaryota.
DR HOGENOM; CLU_411076_0_0_1; -.
DR InParanoid; Q6FSJ9; -.
DR Proteomes; UP000002428; Chromosome G.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IEA:EnsemblFungi.
DR GO; GO:0019898; C:extrinsic component of membrane; IEA:EnsemblFungi.
DR GO; GO:0000407; C:phagophore assembly site; IEA:UniProtKB-SubCell.
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:0000422; P:autophagy of mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0071255; P:Cvt vesicle assembly; 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:0034497; P:protein localization to phagophore assembly site; IEA:EnsemblFungi.
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..660
FT /note="Autophagy-related protein 13"
FT /id="PRO_0000157967"
FT REGION 315..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 660 AA; 74347 MW; 348E33C259E4DB11 CRC64;
MSNGNDNQVI ELIQNFFLKS AGLVTTVESN RYSLDDTSIE FDDEWFDMNI DVLHDLPPII
DKWTNFDGTQ ELPPLVIETF LDLHLLPSSY TVRLRDDESH LWAVSKGNKK SEIVLERWLI
ELDKESTSFK NHVQSGSGVS PEKLDQQLRL LFRYLFTLLQ LLPSNDLMMA LNNQSESHNT
PIPVDIKTRI LDGSQPILSK GRIGLSRPII SSYSNIINNS NIPAHLEQKK ITPVWTKYGL
LRISVSYRRD CQFIFQDLNE DNSPNTQITN QPAKTNEISI SLSPRSKNDL NQISHPSWQK
KFISSSKQFQ PFIVGSVGSA NTPNQNSSRN PSNSSVVGPH YHPQHRLSIG SSTSVSTQPN
YEGTSVGSTS KFASSFNNLR RHSSVRYHES TEKLAKTDKN NYEDTDDLME FVRLIEAKPE
LQPKKGLSGL QDKNLSGSIL RYQKLRPSND MLSEDLALSV SIDPIHGSQR RNSNSHSHSP
VASFSPSGHF SSINSKLSQP HLAVRGSSST VNSRRNSVDK VLASALSPIY GGDIPEYHTK
SHNPVFNEVD DEEEGNDDLL VNKIPININK HKMSTSPRSI DSISNSLTRN RTPFRQPYQY
SQPTTIATQA YAKMHRPTVR SSDAISEINS RKGDNFHQLI NDNDEDDLVF FMSDMNLPRE
