ID   ATG11_ASPFU             Reviewed;        1264 AA.
AC   Q4WY31;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Autophagy-related protein 11;
GN   Name=atg11; ORFNames=AFUA_3G11590;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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; AAHF01000002; EAL92422.1; -; Genomic_DNA.
DR   RefSeq; XP_754460.1; XM_749367.1.
DR   AlphaFoldDB; Q4WY31; -.
DR   SMR; Q4WY31; -.
DR   STRING; 746128.CADAFUBP00003680; -.
DR   PRIDE; Q4WY31; -.
DR   EnsemblFungi; EAL92422; EAL92422; AFUA_3G11590.
DR   GeneID; 3512635; -.
DR   KEGG; afm:AFUA_3G11590; -.
DR   eggNOG; ENOG502QVZE; Eukaryota.
DR   HOGENOM; CLU_002803_1_0_1; -.
DR   InParanoid; Q4WY31; -.
DR   OMA; GLRWYLI; -.
DR   OrthoDB; 287492at2759; -.
DR   Proteomes; UP000002530; Chromosome 3.
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; 1.
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..1264
FT                   /note="Autophagy-related protein 11"
FT                   /id="PRO_0000124543"
FT   REGION          528..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1118..1140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1180..1264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          566..887
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        545..567
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1188..1229
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1264 AA;  143022 MW;  56A0EC731FFFEA65 CRC64;
     MTARGKNVRI QSLATEDEIF VYDRRFVSEP ENVELPELPS PEPFTPDTPP DTLTNQNDLQ
     AWRNLYMARR SWALGLVERC GAMDKSIHEH NERTDIIHRA AGVALENLKT HVGNLENRFQ
     EAQTWANDLL KEQRAALDGW QRALTTLESI PAPKVFPFLG RPSTPKEHRD RPTGTLRDFV
     DANEVQKAGA EAAAESSRFA RQIDDVAEAV RGITADTQRL IDDQLPSGAD AADGLQEMIT
     FAKKISSDYE HVIALPNNQK TLANISRLAL THTQDLLPSM LDISAEIHAG LEEAVRRHNT
     AMKVALDHMR TISAIELRLA DVQSQIINLN VQSDAFDVVF SVYHMPMVYG SILVESVRRR
     EFNEKMKADS LTLAEEMAVF RDEEQRRRKK WLKSMGDFIS LTETTTPGVE INLQGLDYEW
     PEVSRNDIES YIEHLKSRPA MASLADGLTQ QYKDLDAPTR HQRRRAKAFK QGSIFDLSRS
     SLLLRSDDML RSLREEKSKL EEKLKGSESR IRKLEDLLHR QSQLSRPVSG NFNLEFPSSP
     ASPYPDELSR RSSVSSRRMS ANQSSEDKTL AQRIVTLEAE LNAERETVQR LQKEAHAERL
     SNTDKIQEAQ STKRDLIDNL EARQREFDEE RRYLEGELKK YRLRTEELEE ELDRITDSRD
     HAKQDADERI NQLETELQNL HIHTEEELHR ANDLLEQMQA QKMTEESLQQ RINELEKQQS
     EIKATEQENL QTLQAAFMNL SPGGAVPAEI PSIIKAIEVL SEGLSIHVKN AEEKMAEAVA
     ENKALEERMN QLETEVQDAK QSAEQRESEL AQVRGELAQE KEKLAAVQSE LHDERSKLNA
     LQSQHADGDT GTDALRQRVV EDERKLGILS QRLAEVEAQA RESEKEVCAW KNKLKAISES
     EREATTRIEI RGSRAKELSQ QLFEQVEKME HMLEQLGFTV IRQDGEIVVQ RASKVNASSG
     IGDSLAQSGV VSVKPDPSLL DWMQAETAQE ETDRYMAFLE SLYQFDVDVF GDAVVKRVKD
     IELLARKWQK EARGYRDKYH RMQSEAHDKI AYRSFKEGDL ALFLPTRNQA IRSWAAFNVG
     APHYFLREQD AHKLQTRDWL LARITKIEER VVDLSKSMNG AHPDRRSIGG TSDAASIDDE
     NPFELSDGLR WYLLDANEEK PGAPATPGLG KSTVAPAHVD ARGSIRLKRT SNGGNVAKTL
     TKSLDSRRNS SSSKKGPPFA ISQRANESTA ELARPAEANT PLSPSAQEAA STPEEVRRDQ
     LQGP