ID   ATG11_PICAN             Reviewed;        1299 AA.
AC   Q67C55;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Autophagy-related protein 11;
DE   AltName: Full=Peroxisome degradation deficient protein 18;
GN   Name=ATG11; Synonyms=PDD18;
OS   Pichia angusta (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=870730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 14754 / CBS 1976 / JCM 3620 / NBRC 0799 / NCYC 495 / NRRL
RC   Y-1798 / VKM Y-1397;
RA   Komduur J.A., Kiel J.A.K.W., van der Klei I.J., Veenhuis M.;
RT   "Hansenula polymorpha PDD18 is involved in peroxisome degradation, but not
RT   in general autophagy.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION.
RX   PubMed=11810237; DOI=10.1007/s004380100584;
RA   van Dijk R., Faber K.N., Hammond A.T., Glick B.S., Veenhuis M.,
RA   Kiel J.A.K.W.;
RT   "Tagging Hansenula polymorpha genes by random integration of linear DNA
RT   fragments (RALF).";
RL   Mol. Genet. Genomics 266:646-656(2001).
RN   [3]
RP   NOMENCLATURE.
RX   PubMed=14536056; DOI=10.1016/s1534-5807(03)00296-x;
RA   Klionsky D.J., Cregg J.M., Dunn W.A. Jr., Emr S.D., Sakai Y.,
RA   Sandoval I.V., Sibirny A., Subramani S., Thumm M., Veenhuis M., Ohsumi Y.;
RT   "A unified nomenclature for yeast autophagy-related genes.";
RL   Dev. Cell 5:539-545(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       ECO:0000269|PubMed:11810237}.
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; AY366190; AAR12210.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q67C55; -.
DR   SMR; Q67C55; -.
DR   PhylomeDB; Q67C55; -.
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   PANTHER; PTHR13222; PTHR13222; 1.
DR   Pfam; PF10377; ATG11; 1.
PE   3: Inferred from homology;
KW   Autophagy; Coiled coil; Membrane; Protein transport; Transport; Vacuole.
FT   CHAIN           1..1299
FT                   /note="Autophagy-related protein 11"
FT                   /id="PRO_0000124551"
FT   COILED          294..367
FT                   /evidence="ECO:0000255"
FT   COILED          820..962
FT                   /evidence="ECO:0000255"
FT   COILED          1164..1194
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1299 AA;  149155 MW;  DF96B8D21F7F8E97 CRC64;
     MNISIIQNNN PLSMMSSVYR QNQSQDTNLP SALTIYNSLT GAKVVASAYQ FHNLEALKQF
     IGMSFNVATE NLFLLTPFGI KLKFSMIVHE EISEIYVFDR RYFNVNNIEA SGNMDNVNDL
     LAELNQTDFI NMIKPLASPL LSEELSVFVE KLTLVLENTT QIKAVDINLN MLRMLLNSLK
     RNSGWASALL SDFKKTVAFD ECTPEDNDLE TILTSLNVLI QYVGLVFKTL EKKFNDSIDA
     LVLLQSNSLV DQWRDQYALL KRIPFEFKSG SSNVPEKLFL SQLVNESHLD KCAEESRRLN
     KSMNERLVML RSKIEADVIK PRQELLQEYN GYMSQYIRPE TDATQKTQKI QDCKRILAEL
     EVHVSKLIQS SSSLPSFEEL ITTASQTSTT LSASSIANIK KLTQLYKYQE SELVPYIFQL
     ANNLYDIQIN KLNARKELQT KLICSTLINI TKIQLNIMRL STVLNTEVAK NIASIKENEL
     QLSVVSDLPL MFGIFVIANL NNLKFGISLN NIVKKANEIF EMLRFMESRN RAKWLKEFLA
     SSGADKVEFL HLDEEARERF INENMLSYKL EQVDAIRSKK SPSPVDHPAS PVSGQEKHYL
     TSINRLLHNI NGFPAPRPTA TELPKQRETN IMTNLARNIS VKSIVSYINT LRKEGIDLNI
     VNRLEECLKD FGITYGAIER KAIETEDGEE IVVKGKNAGD LGTFDVNDVN YMRLFKKFIK
     SFESEGIVIN INVNQQDSVS NDELIKGYER RIRKLENVLH TRNFQQFNEQ WSRHRPVHTL
     PNPVSRRQSD MSQEPAVHEN TILFNENVVL GRKTIDLPPS HYGERIERLE KENERYRGEI
     EELKKGTDLA ELDRLKKEIE DLQKADMEKD KRLAALEEEN KNLKESNEEL TNSNKELVNM
     CEELKSMKSD LLENMTQKES EFGKEAKVNQ QEINELKLRI EELEEDESNL VNVNKTLNER
     LAIKDGLLCQ LYELVQGAYG KLNQMSGEIF SNLTRVCLLL ESIGLLLIRE TPSFDNHPGT
     LTIKRVKGLR SRKRQIKQAS DSTHNGNLQN DTFEDSEHID NALMEVVSSE VVPEAEQYLH
     WVDTNVLNYT ISSDLGIEDE IEHKKNESSL IDMSLCEESS IEKKVKKLLA NYESFNVEQG
     FQNFLRFNHV DNELVIERVF RRFSDVETLA RKLQKDKTQQ KQELKMLTAE LDGKIAFRNF
     KVGDLVLFLK TLTPANEELG GGDEQPWAAF NVGCPNYYLK NTKGEGYIEL SDRDWLVGRV
     SKIEPRQVTE QNFHSKTENP FRLAKSVVWY YVEAREVKE