ID   ATG11_NEUCR             Reviewed;        1429 AA.
AC   Q7S055;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 2.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Autophagy-related protein 11;
GN   Name=apg-8; Synonyms=atg11; ORFNames=NCU09998;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002236; EAA28680.2; -; Genomic_DNA.
DR   RefSeq; XP_957916.2; XM_952823.3.
DR   AlphaFoldDB; Q7S055; -.
DR   SMR; Q7S055; -.
DR   STRING; 5141.EFNCRP00000009736; -.
DR   PRIDE; Q7S055; -.
DR   EnsemblFungi; EAA28680; EAA28680; NCU09998.
DR   GeneID; 3874063; -.
DR   KEGG; ncr:NCU09998; -.
DR   VEuPathDB; FungiDB:NCU09998; -.
DR   HOGENOM; CLU_002803_1_0_1; -.
DR   InParanoid; Q7S055; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000045; P:autophagosome assembly; IEA:InterPro.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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..1429
FT                   /note="Autophagy-related protein 11"
FT                   /id="PRO_0000124550"
FT   REGION          71..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1024..1061
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1209..1241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1336..1429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          143..173
FT                   /evidence="ECO:0000255"
FT   COILED          553..590
FT                   /evidence="ECO:0000255"
FT   COILED          632..815
FT                   /evidence="ECO:0000255"
FT   COILED          851..989
FT                   /evidence="ECO:0000255"
FT   COILED          1105..1143
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1032..1061
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1209..1229
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1341..1372
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1383..1421
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1429 AA;  161923 MW;  C09F3171CA9CC600 CRC64;
     MVTQVLIAHT GQRLEIDSRT ITSLNGLKES VASQTSIPVE CLIALTPQGR SLRWQPTQPE
     TEIYIYDSRL TQRSQPGASS PPLSELPLPR YNAHTPPNSI EDTRSIPAWQ KLFETRRAWA
     IDVVEDCARM DAATRERYAE MDVMLRCLDA AVANLENAVK GLENKYVELK EWSTSAQAEY
     SALATGFDRY LSLARGIAIS SSMARFMTSR DDGGWKGRPQ RQSTLEDLVD LELARQAGKL
     APSALRKFKD RITNLDKAAT HLFQDADTLM HKFETTMSRS ALSHDGESLH LLKDIEALAN
     KIDNDYNVTL EYTSSTRDTL LQVSKTAAHH TERLLPSIQK RALEMGDILC YATKARNSLA
     AESIEFMRSI TEITSDSHSV KSQISETGQE DELATFDHLR LIQQIPYLYA SFVAEAIRRR
     EWLDKVKQDS TTLANEMAIF HEEEAKRRRR WHKSIGAVFG PAPTADSKVP NLEINLRGDD
     GEWPLMTRKD LDDFFNALRN QKADPELVVE IEKLIADMDK STRQQSRRMK AFKNGSVHET
     ALGRSGLLVR GDDDLLRSLQ ADKTRLESKL KTAESRVRRL EDLLHRQTQA SRPNVGNLFQ
     NPSQQVLDRN DSISSLRNPR AVDDRSRSLD GLETLIHRTQ QLETELNTER ERCVVLEREI
     NALTTLHNDL KGQMDEANST KKDLLQNMEA LKREFTEERK SLEEEVKQLK ARLEYTEDEI
     EHFGESRENE KASYDEKVHF LELEVERLTR ERRDDSLKAD DQVVLLQNEA RLQRERIAAQ
     DIELRAAQDE IRVLSKRLEA VTEDKQKYRQ ALEDIWECLA PADDVPTELP DLLEGITGKA
     ADILNTKQGV EGDMSLMKLN VDTLQNNIRT LRSEMDFTKD RLTEEESVSL RLREKFSEER
     AKVVAMEGEL AHGREQLHEF RVKIADGETG SEYMRKRLED EEQNLASMTE ELAAGQTQVQ
     KMEEEVTRFK AKLHQTQMQL SELSIRLESR TECAKDLTQL LWSQNDRLTR LLERLGFSIS
     REEDGTMHIQ RTPRSERSLA TTANPNDSDP SSSLRRSSTL NARPVTDNAD LELLQWMSSA
     TPEAEVEKYK IFMGLIGSLD MDVFADAVYR RVKDVEHMAR KLQREARAYR EKAHSFQKEA
     HDKIAFKHFK EGDLALFLPT RNQSTGAWAA FNVGFPHYFL REQDSHRLRN REWLVARIMR
     IQERVVDLSK SLQHDQAGET RKDGARGETE SLDDDENDNP FDLSDGLRWY LIEAVEDKPG
     APSTPGLAKS TVAANNVEAM ADMRTQGHIS KARGLTGRGG TPLGIEGVSK TLSKSLESRR
     SSTGSRKTLP FVIGASSRGR ESALASETNS LRAVPADNNS SAPTNAAQQH MSPTDKLKDE
     SLQETPQQTN SISAEGESMT IAARNDQAIL QPSQTHSEVR NEIESLIGP