ATG11_YARLI
ID ATG11_YARLI Reviewed; 924 AA.
AC Q6CFR0;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Autophagy-related protein 11;
GN Name=ATG11; OrderedLocusNames=YALI0B04598g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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: Involved in cytoplasm to vacuole transport (Cvt), pexophagy,
CC mitophagy and nucleophagy. Recruits mitochondria for their selective
CC degradation via autophagy (mitophagy) during starvation. Works as
CC scaffold proteins that recruit ATG proteins to the pre-autophagosome
CC (PAS), the site of vesicle/autophagosome formation. Required for the
CC Cvt vesicles completion (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Vacuole
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Note=During pexophagy, accumulates in the vacuolar membrane region,
CC where the peroxisomes contact the vacuole. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATG11 family. {ECO:0000305}.
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DR EMBL; CR382128; CAG82729.1; -; Genomic_DNA.
DR RefSeq; XP_500502.1; XM_500502.1.
DR AlphaFoldDB; Q6CFR0; -.
DR SMR; Q6CFR0; -.
DR STRING; 4952.CAG82729; -.
DR EnsemblFungi; CAG82729; CAG82729; YALI0_B04598g.
DR GeneID; 2906710; -.
DR KEGG; yli:YALI0B04598g; -.
DR VEuPathDB; FungiDB:YALI0_B04598g; -.
DR HOGENOM; CLU_318616_0_0_1; -.
DR InParanoid; Q6CFR0; -.
DR Proteomes; UP000001300; Chromosome B.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IBA:GO_Central.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0030242; P:autophagy of peroxisome; IBA:GO_Central.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
DR InterPro; IPR040040; ATG11.
DR InterPro; IPR019460; Atg11_C.
DR InterPro; IPR045326; ATG17-like_dom.
DR PANTHER; PTHR13222; PTHR13222; 2.
DR Pfam; PF10377; ATG11; 1.
DR Pfam; PF04108; ATG17_like; 1.
PE 3: Inferred from homology;
KW Autophagy; Coiled coil; Membrane; Protein transport; Reference proteome;
KW Transport; Vacuole.
FT CHAIN 1..924
FT /note="Autophagy-related protein 11"
FT /id="PRO_0000124553"
FT REGION 514..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 552..682
FT /evidence="ECO:0000255"
FT COMPBIAS 538..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 924 AA; 104021 MW; C1E0853E5CB5AA03 CRC64;
MSEIRVSCAS SGVSVSAARD QFSSLPHLKA WIELEFSVSV SEQLLLTVAA EQVKMAHLGT
QNELFVFDRS VVGGTVSNEH KYSAPKLKTL TPGTDPSQWA LTVLTHCSRL VEETKRVTAE
IATIKRATNV AITQMKQHSQ NLDKNLLNVK EYSKELNQGI TPLLSVDLAQ LRDNTRAVKL
VAPAVFGKKQ FLNDWLDLQQ LQSIVVEFKA DFPSCMDKLQ TLEQDLAQLS KDTQTLVNST
DVWIGGTNSD VLCNEAVGIL RKLSELTSGD HVTNEAVKSV QNCQSQILDL HKALSKAKFQ
TVQHSQKVLQ SISQLQSRST KLKPKLTHIG SELTKYEEKR VQAMKQVDVE FVYGCVLVEM
LRRTVWSQSG GENGSVKSEI GTRVAWKKQF QDTFPFVDIL NEQEDLTIDT ISTSSPSIVH
NLVIARPVVT DYISQVSSKE VRNNLESLLG GVTGSAAATS SFPRSLFRNG SISGSLMAER
APISSATNAD DKIRGYEARI RKLEDLLYKQ RMSQDTSRWS VSPGTPSAGF AVVSPGQLSS
EARGSSLSPE PTETREQVKA REKAEEEARK AEEERLARDK AAAEALQSKV DQLSQSLLHT
ENEKNDLMAN LASMESDFSR ERRCLVQEIS ELKLRVEELE EQVETAAETS IERHQRADQE
TEELEQRLKA MTLAQNTVDD ENSRLKITLQ DMSQRLYTGY KRNCVLLESL GLQAQKEYDA
DGSEVVSFDI HRVKGLRKKH RGKKGEKTEK DSESDSTDDF SALYWATKTT PDSFESSYRT
FLARIFLDYD LYVEKVAKRF EDLEHLARKL QKEARNYRTM TQQLDDETRS KIALNRFKVG
DLVLFLPTRD PSRQPQPWAA FNVGAPHFFL KQKPGRELKD RDWLVGRITG MEERVVNGGI
GDREENPFDL GQGLRWWWLE AEEE
