ATG13_KLULA
ID ATG13_KLULA Reviewed; 684 AA.
AC Q6CWK2;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Autophagy-related protein 13;
GN Name=ATG13; OrderedLocusNames=KLLA0B03432g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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 -!- INTERACTION:
CC Q6CWK2; Q6CSX2: ATG1; NbExp=4; IntAct=EBI-16151385, EBI-16151357;
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; CR382122; CAH02080.1; -; Genomic_DNA.
DR RefSeq; XP_451687.1; XM_451687.1.
DR AlphaFoldDB; Q6CWK2; -.
DR SASBDB; Q6CWK2; -.
DR SMR; Q6CWK2; -.
DR DIP; DIP-61492N; -.
DR IntAct; Q6CWK2; 4.
DR STRING; 28985.XP_451687.1; -.
DR EnsemblFungi; CAH02080; CAH02080; KLLA0_B03432g.
DR GeneID; 2896881; -.
DR KEGG; kla:KLLA0_B03432g; -.
DR eggNOG; KOG4573; Eukaryota.
DR HOGENOM; CLU_411076_0_0_1; -.
DR InParanoid; Q6CWK2; -.
DR OMA; YAKLHRP; -.
DR Proteomes; UP000000598; Chromosome B.
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 1: Evidence at protein level;
KW Autophagy; Cytoplasm; Protein transport; Reference proteome; Transport.
FT CHAIN 1..684
FT /note="Autophagy-related protein 13"
FT /id="PRO_0000157970"
FT REGION 260..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 684 AA; 76008 MW; 28E8D62F3596A514 CRC64;
MSEGEVQVIE LINNFFLKSA LLLEQSKVAH NFDTEEALRD GNHLFNIETR GDPLLEAQIQ
PWITFDGVKT MPPLVIETYL DLRALQPNHM VYLHDADGNP WMVCKGGKKT EIVLERWLVE
LDKQTIDDSI DSNDPENLHK QLVLLFRYLY TLTQLLPAND IITKPHNSQQ PALINVQTRL
LDGSKPILSK GRVGLSKPII ASYSNTMNET NIASHLEQRK ITPIKTTFGS LRITVSYRKD
VDFYVIDSDD LQKRYMTPSL SNETTTVPDR RASSNCSRSM SVSPKTNTIN ATLFPLEGSS
ARRQSISSKL QPFKVGSVGS GSFVQSGSAQ STTSLVPSLS RNVSSSSVVA ALKVQRGSAG
STIVNGDVPP ELSSVGSGSK YSSSFGRIRR HSSIRRSESF DRTAKPRKST ENPPEDLLEF
VKLLEDKKEL NMKPNTILPQ QDISNSLMRF QSMKSNNDAL SDNLSMSMSI DQPNVRFGSN
SHSPIPSFSP NYGSIPSRLS QGSRNNSNAE LITSRKSSLD RHKHNLLSRT GSNVDINRRG
SVGTMETTNE DSKEDEQSHM KGMHFSNEAT INKDDDEDEM LMKRSFNAGT STTEQVMGSP
RSIRSISVSS YPRNQLPLKH LNLSHPTTSA TTTHAKFHKS EMSPDPLHTE GAQPHTSSQH
HNSSQKNDED DDLLFVMSDM NLTN
