ID   ATG11_VANPO             Reviewed;        1219 AA.
AC   A7TL57;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Autophagy-related protein 11;
GN   Name=ATG11; ORFNames=Kpol_1065p36;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480412; EDO17020.1; -; Genomic_DNA.
DR   RefSeq; XP_001644878.1; XM_001644828.1.
DR   AlphaFoldDB; A7TL57; -.
DR   SMR; A7TL57; -.
DR   STRING; 436907.A7TL57; -.
DR   EnsemblFungi; EDO17020; EDO17020; Kpol_1065p36.
DR   GeneID; 5545192; -.
DR   KEGG; vpo:Kpol_1065p36; -.
DR   eggNOG; ENOG502QVZE; Eukaryota.
DR   HOGENOM; CLU_272501_0_0_1; -.
DR   InParanoid; A7TL57; -.
DR   OMA; EIDVHYF; -.
DR   OrthoDB; 287492at2759; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
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..1219
FT                   /note="Autophagy-related protein 11"
FT                   /id="PRO_0000317926"
FT   REGION          811..882
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          895..926
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          636..824
FT                   /evidence="ECO:0000255"
FT   COILED          1052..1081
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        817..863
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        907..926
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1219 AA;  141693 MW;  16C5EA5589BF8523 CRC64;
     MSSNIINAIT GELITIDITL FISLNEFKKF LINRWQIDFN NLLLLLPFGN KINDRIFIDL
     IGKKNDQSTI YVFDRRLFSL VNNPDNELSS DYLTNIKNLL KGINHPTNNL NQLVKPVNSP
     YEEVEINEKF LNYHTITSLI TTNLGWLSAL EIDMHYFQIQ ISDTLDYIKN IIESLKICQN
     YLELYCYDVE NLYNSNVKFL NQLANNEILK NWLNYYDNIL TKLSDINGNK LSSYLNKNEL
     VSISSKIEEL DQRVNSNLKK FKIVIDKNID LRNNINKEIS SLSEKITPSS EKYKLEETML
     EKFTELVKNL RNDSKVILEK DENEFDKNYM QNLAKSLEKD KKVTVTNLLT ISKALYSQAN
     DISEIKSKLQ VDSIKLFGQI SFIQIETLNI KKLLLNELNK DLEKYQGFEL KLAHVQDIPL
     VYGLYSIENY RRESWVLQIN YKHLDFNKSL KTIVEKEKST RNKWVDNFGS TAVYFTEDMD
     TLRDFNYLNN IAKGNQSMIK KLEELFKNIS NESHNKNLVF IETYIKEVED LDLDKDVIEL
     FKRYLAVAQG FVIEQPSTKN IISDKETGEL INGYQSRIKK LELLLHSARY SNVESWPTGL
     LNYSNVKLFR NNVATVNSKL SLQSDYMGNI SYGSDQLRIK ELENVNKQYK TDFKALTDEN
     KLLKDKVTKF NTDISDIQIE RNAYKETLTK LNEELSRLTS IEGDFEKHKG EKEIELKIKI
     DGLVDSNKTL LNQISDLKIE SKELESSNRD LLAQLNQKRE EHKVLEDSLK QRENEGLRYK
     DEYEAKLKEL TEKFEADRRA LEDEIKAAKE QNMKESMEQQ TEQSANQSID QSIEQSTEQS
     TEQSTEQSME QSMEQSMEQS VEQSMEHSME HSMEQSEKQN MGQNDATIDN QSIETPTSED
     MHSLDEQSPE SQLLKSNTTE LQPIKSQELA EDSKAIELKN IQEMLVSKLY EIFSSNVFIL
     ENIGLLLTFD EHDNFQIRRV KGLKKNLNQS VLEETGLLNE IEMPVKSDVF SEVKTLFSNY
     KETFDSRSYI SLLSKINQLY DCKLYETAVI KRFEDIELLA KKLAKENKAK KNLFEKYRCE
     RITLKNFEVG DLALFLPTRE NCITEDVSVA SWNSSFSSVD LSTPPPFGEP ITNQSHSGTA
     KDKNKHNLEK RPWAAFTAFE ETARYFLKDP ENIPNNREWF VGKIMHLQRF VVEDHISNPY
     KLPKGAVWFQ VTATVVSHQ