ID   ATG11_PICST             Reviewed;        1162 AA.
AC   A3GG92;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 2.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Autophagy-related protein 11;
GN   Name=ATG11; ORFNames=PICST_86449;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(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; AAVQ01000001; EAZ63894.2; -; Genomic_DNA.
DR   RefSeq; XP_001387917.2; XM_001387880.1.
DR   AlphaFoldDB; A3GG92; -.
DR   SMR; A3GG92; -.
DR   STRING; 4924.XP_001387917.2; -.
DR   EnsemblFungi; EAZ63894; EAZ63894; PICST_86449.
DR   GeneID; 4851291; -.
DR   KEGG; pic:PICST_86449; -.
DR   eggNOG; ENOG502QVZE; Eukaryota.
DR   HOGENOM; CLU_272501_0_0_1; -.
DR   InParanoid; A3GG92; -.
DR   OMA; GLRWYLI; -.
DR   OrthoDB; 287492at2759; -.
DR   Proteomes; UP000002258; Chromosome 1.
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..1162
FT                   /note="Autophagy-related protein 11"
FT                   /id="PRO_0000317925"
FT   REGION          620..648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          949..971
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          563..591
FT                   /evidence="ECO:0000255"
FT   COILED          659..760
FT                   /evidence="ECO:0000255"
FT   COILED          798..870
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        625..648
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1162 AA;  133410 MW;  31472524B5F6C6BA CRC64;
     MTDLSYLIIY NAHTGTSSRI PKPIRYHSLG DFKRFLQTQL HVDSIDNLFL LTSFGIKLNF
     GLINELNEVY VFDKRLFGNS YDPEVLSQYT AESFEVVKPT PSTALASTET QIRIISSSLK
     SNQGWARAIV QDCHHTEELA KELVRNINAI FKSLNTIFQF ATNFINEIEK NFNSYLNYIK
     LINYKTLHRT WIDSYNILKQ YPPFKIKDAS VFLVDFLNHD KLLEAANYVS SNLPLVVSKF
     NGMSETINSV GEEKLTVDKE IESLRNGSIN EFKDVNLSEL MAKIYSLSRS ITNDLEQVSN
     NDSIKLDEVY KEHKENYSPL LYDNAVELHN YFLGLRKFKE KLTKQSVSIF NSIANLQMKM
     VSIKSNLKTL TTPSESTDPI SFETINTIKK YEDYLSLNID LPLLFGFVLI EKRRQFEWYD
     FYSKGIVNNV SEQLSTIIDH EKLFRKIWLR KFGNFLTLLS DETPTTSLPN IDVTLVGIKE
     ETFKILHDIQ VERSDIVNYI AFVESSKASK NFVELLNKNF RDLIRSTNNM KKITRVISSL
     GTYTSLSGEE KSKILSKEDE EGEIDFDLNL IKGLKTRIKK LESLLHQQQY KNLTSWPVTR
     NNVAPSSSDN RLSLIIEPQK KTVTPPKSDP KQLLQKQSVP TRTSSAQSAV LDSTNIDIRL
     ELIKIKKENT ELINENSALH QSNDESQKLI KDLRKEIEEL KAINASHRQE ADAKLLMKEE
     EFRLFKLDNK VDTKLVENLE KKVEQRDAQV SKLKEDLSRV MEINTTSDKE IIALNSTISS
     MRNELNDTVV MKNDLLSNIS AKEVEHSKER NGLENEIKTL SAKVDELTED YENLMEITQS
     RQKNADLLVN DLNNIIIKLM NDMKRLAENI FEYFLEFCFV LESMGLLLTM DGDVYKITRV
     KGLRSKKTVD DPNDTSFISI EKPSSKVIDE VDKSMSWVTT ISNLSSILPE VPGTSSTASE
     NGHESNEEES NKFNSQSLKL ITIFNEIFTA NNAKFEDFLR IISFQENVQL QEDSAHNSKF
     FLNAISKRFR DVEGFAKRQT KENKIKEQEI HKLVGRLATK ISMNGFQIGD LVLFLPTRID
     RAVEVANESI QPWAAFNIGA PHYFLKVDDE ERTKNKEWMV GRVESIEENK VTDENAGDLS
     SNPFQLSVGV VWYLVEAKEE HF