ID   ATG11_EMENI             Reviewed;        1285 AA.
AC   Q5B993; C8VJ96;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 2.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Autophagy-related protein 11;
GN   Name=atg11; ORFNames=AN2887;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CBF83808.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAA63458.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AACD01000051; EAA63458.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001306; CBF83808.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_660491.1; XM_655399.1.
DR   AlphaFoldDB; Q5B993; -.
DR   SMR; Q5B993; -.
DR   STRING; 162425.CADANIAP00010202; -.
DR   EnsemblFungi; EAA63458; EAA63458; AN2887.2.
DR   GeneID; 2874085; -.
DR   KEGG; ani:AN2887.2; -.
DR   eggNOG; ENOG502QVZE; Eukaryota.
DR   HOGENOM; CLU_002803_1_0_1; -.
DR   InParanoid; Q5B993; -.
DR   OrthoDB; 287492at2759; -.
DR   Proteomes; UP000000560; Chromosome VI.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
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..1285
FT                   /note="Autophagy-related protein 11"
FT                   /id="PRO_0000124547"
FT   REGION          32..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          523..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1116..1142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1181..1285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          73..150
FT                   /evidence="ECO:0000255"
FT   COILED          486..523
FT                   /evidence="ECO:0000255"
FT   COILED          563..726
FT                   /evidence="ECO:0000255"
FT   COILED          769..937
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        547..568
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1195..1255
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1285 AA;  145160 MW;  91DDB200A3730AB1 CRC64;
     MTARGKNVKI QTLATENEIF LYDRRYVSEQ DNADLPKLPS PQPLVLDKPP DTLSDRNDLQ
     AWRNLYAARK TWAAELTERC EMADTSIREL NERTGIVNRA ASVALENLKT HVAALENRFQ
     EAQAWAKELS REQKSALEEW KRALANLENI PARKEFSFLG RPSTPKKDAD RATGTLLDYV
     DAVEVQKAGP EASAASSRFA QQIQDIERAV GEITAGTQRL LDDVPNSRTD TADGLLQEIE
     PLSRKIQSDY EHVLGLSNNS KTLANISRLA LNHTQDILPS MLEIAMEIRE SLAAAVRQYD
     AATKSALGRT KLISAIQSRL ADVQAHIANL TFQSDAFDLL YSVFHMPLVY GSVLIESVRR
     HEFNEKMKSD SLTLAEELSI FQDEEQRRRK KWVKNMEDFL SVTDTTTPGI EVNLRGHEFD
     WPIVTRKDIE TYIEDLRSNP GTANAAQELA QAFKELDAPT RVQRRRAKAF KQGSIFDLSR
     SSLLLHSDEI VRSLRDEKLK LEEKLRGSES RIRKLEDLLH RHSHLGRPSS GNFSIDFPAS
     PASPHPDPMS RRSSVSSRRL SSNQTSEEKN LVNRIVHLEA DLAIERETVQ RLQREADAER
     QSNTNKMQEA QSTKNDLIGN LEARQREFSD ERRYLEGEVK RFKIRVEELE EELDRLTDSR
     DHEKQDADER MHQLELELQD AHARADAEMR KANNLLEQMQ SHREAADRSK LRMDELEKQA
     TERTQKDQEV RHALQAAFMN LSPGGSVPDE IVDIIKAIDV LSEGLTIHAK TAEDNAMKAA
     AENKTLIEQL EKMESNYENA KSASEQYQTQ LTQAREEVEQ EQSKVKAIES ELNDERASLL
     ELESKLAAGE TGAGALREHV AEEEQKLNNM SQQLAETEAR ARRSEEEALQ WRKRAEALSE
     SDKQVAARID IRTARLEELS RQLFGQVEKL ERMLEQLGFT VIRQDGEIVV QRSSKVNALS
     ATADTLSQSG VVSVKPDPSL LNWMQGEHPE EETERFNAFL ESLHQFSVDI FGDAVVKRVK
     DIEVLARKWQ KEARGYRDKY HRMQSEAHDK IAYRSFKEGD LALFLPTRNQ AIRSWAAFNV
     GAPHYFLREQ DVHKLQARDW LLARITKIEE RVVDLSKSMN GGNPDRRSIG EASDGASIDD
     ENPFELSDGL RWYLLDATEE KPGAPATPGL GKSTVAPAHV DAKGSIRLKR TPAGGNVTKT
     LTRSLDSRRN SSASASIKRG TPPSRANDST TDLVRPAQAE SESIAAATDS KSQSQSQSQE
     RERRQEAQGT AVIFDEVRRD QLQGP