ID   ATG11_PICPA             Reviewed;        1313 AA.
AC   Q9C438;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Autophagy-related protein 11;
DE   AltName: Full=Glucose-induced selective autophagy protein 9;
DE   AltName: Full=Pexophagy zeocin-resistant mutant protein 6;
DE   Flags: Fragment;
GN   Name=ATG11; Synonyms=GSA9, PAZ6;
OS   Komagataella pastoris (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=4922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11309418; DOI=10.1083/jcb.153.2.381;
RA   Kim J., Kamada Y., Stromhaug P.E., Guan J., Hefner-Gravink A., Baba M.,
RA   Scott S.V., Ohsumi Y., Dunn W.A. Jr., Klionsky D.J.;
RT   "Cvt9/Gsa9 functions in sequestering selective cytosolic cargo destined for
RT   the vacuole.";
RL   J. Cell Biol. 153:381-396(2001).
RN   [2]
RP   FUNCTION.
RX   PubMed=11856375; DOI=10.1046/j.1356-9597.2001.00499.x;
RA   Mukaiyama H., Oku M., Baba M., Samizo T., Hammond A.T., Glick B.S.,
RA   Kato N., Sakai Y.;
RT   "Paz2 and 13 other PAZ gene products regulate vacuolar engulfment of
RT   peroxisomes during micropexophagy.";
RL   Genes Cells 7:75-90(2002).
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). Involved in glucose-induced
CC       micropexophagy. {ECO:0000250, ECO:0000269|PubMed:11309418,
CC       ECO:0000269|PubMed:11856375}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:11309418};
CC       Peripheral membrane protein {ECO:0000269|PubMed:11309418}.
CC       Note=Vacuolar and perivacuolar punctate structures. Appears to be
CC       concentrated in a region of the vacuolar membrane that contacts the
CC       peroxisome during the engulfment process.
CC   -!- SIMILARITY: Belongs to the ATG11 family. {ECO:0000305}.
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DR   EMBL; AF309870; AAG30291.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q9C438; -.
DR   SMR; Q9C438; -.
DR   IntAct; Q9C438; 1.
DR   MINT; Q9C438; -.
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..>1313
FT                   /note="Autophagy-related protein 11"
FT                   /id="PRO_0000124552"
FT   REGION          557..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          814..1027
FT                   /evidence="ECO:0000255"
FT   NON_TER         1313
SQ   SEQUENCE   1313 AA;  151234 MW;  D70EB9E6DC4C8627 CRC64;
     MDSSRHGLHP LQNSLLHQSQ MDIYNSITGI RISAIPYNFN SYDQFKQYIS ASFGIAPADL
     FLLTAFGIKL KFSMIMNGDV REVYVFDRRF YDGQQMVDDK LDTALESLNQ CEMLNMIKPM
     RSPLENADIL RFVSYLKDIT NRPNLSTEDL DLNKLRLVLN SLKRSSGWAA ALLSDLKKTN
     YYKKVNEEVL CDNKKEIEII LISHNALIQY TNLMFKTLEK SFNESVDSLI MLQEQSLLEN
     WKSYYQILKG VRFKGNYVLS DLLDEKMLEN VAADSKALMG NVNDKLTRLR SRIDSEIISK
     RVMINDLYES LKKKYLDVPN LNSNSRTEND SDTLNRLTEL VNQVVKDSKE LPILDELLTT
     SGGNSTTLSA ESVKKINVLV SVFETHSSTI IPQITELSNK LYDEKVEALN LKQDLQRTLL
     SDTIHKIVGV QLSILKATNL INNDLSKNIS NLDFNELKMS IVKDLPLVFG LWLAGNLKKL
     KWLENFNKVA FKANEILEML KFIESNYRSK WIDGFSKTNP CVNSNQGQRI LALQINEDLK
     QQFVRDHLAS SRIVLKTGSN VPTPGGSKGN SRAPTPEHDP HPPHLNAINK LLHNFNKDYN
     FGNLRQASEE VVRTHSPATK RDDRFGNQFW LTLIDNITTE DFYHYIDSLK ENKVNIKVIK
     QLEKNLTDLG LGRIYETSND KVISAGGGTI GPLNSQDTSY MNLLKKFLKN FEINDVTIQI
     NISTLETENG NNNEKEKEPS FSNHELLQGY QRRVKKLESL LYQQSLHQSG PPPINMAYPP
     IRDYQQRSSA NLMTSATATE MLMDTHARIH DTDMKQKREN VDEIQVLQTR IEQLQANLEQ
     TSKERDDERE QKEILHLKLM KRDEEGDEDE KINGLVAANH QLQIRLEALQ KQNQELQSLQ
     ERNNNEIHAS QEREIEALKK QVVQLTEEKT QMSDEKDRLD LSNEHWKTQY EEAAMMKKDL
     LDNMTAQEQE YKNELNTHIK EVEDLKVKVE NLEDEEANLI EIKENYESKL AQNESHFEEL
     ESIIKSLYGK LRLVIERTFQ NVVTVCLMLE AIGLLMKRDE QYEENDPSNG IRIHRVKGLR
     SRRRSTTSKA ASPLGNDEIL ELSSQIVAEA DKQLVYFHQE PVKELESLET VLDFKFNQDF
     DKFTRLTYMD QKLLVESVTK RFKDVEQLAR KLQKESNYSK TEIDGLIKEV NTRISIKDFK
     VGDLVLFLPT RDDTINMNMA NTVEAVNRRA STVASFETYQ PWAAFNVGAP HYFLINDVSK
     IDLNGRDWVL ARIESMEEHK VTREGHRRNV GNPYNLNPDA VWYGVRAKEE TVG