ID   ATG30_PICPA             Reviewed;         384 AA.
AC   I6LAD1;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Autophagy-related protein 30;
GN   Name=ATG30;
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], SUBCELLULAR LOCATION, FUNCTION,
RP   PHOSPHORYLATION AT SER-112, MUTAGENESIS OF SER-112, AND INTERACTION WITH
RP   ATG11; ATG17; PEX3 AND PEX14.
RX   PubMed=18331717; DOI=10.1016/j.devcel.2007.12.011;
RA   Farre J.C., Manjithaya R., Mathewson R.D., Subramani S.;
RT   "PpAtg30 tags peroxisomes for turnover by selective autophagy.";
RL   Dev. Cell 14:365-376(2008).
CC   -!- FUNCTION: Acts as the peroxisome receptor for pexophagy. Required for
CC       both micropexophagy and macropexophagy, but not for the cytoplasm to
CC       vacuole transport (Cvt) or autophagy pathways. Required for functional
CC       micropexophagic apparatus (MIPA) and relocation of ATG11 to the
CC       peroxisome-sequestering arms of the vacuole.
CC       {ECO:0000269|PubMed:18331717}.
CC   -!- SUBUNIT: Interacts with ATG11, ATG17, PEX3 and PEX14.
CC       {ECO:0000269|PubMed:18331717}.
CC   -!- INTERACTION:
CC       I6LAD1; Q8NJJ4: ATG8; NbExp=3; IntAct=EBI-8849497, EBI-8849485;
CC       I6LAD1; Q92262: PEX3; NbExp=3; IntAct=EBI-8849497, EBI-8849514;
CC   -!- SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:18331717}.
CC       Preautophagosomal structure {ECO:0000269|PubMed:18331717}. Peroxisome
CC       membrane {ECO:0000269|PubMed:18331717}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:18331717}. Note=Surrounds the peroxisome cluster,
CC       but a small amount is also inside the vacuole in methanol-grown cells.
CC       Upon induction of micropexophagy, localizes inside the vacuolar lumen.
CC       Also localizes near peroxisomes during early stages of micropexophagy.
CC   -!- PTM: Phosphorylation at Ser-112 is required for micro- and
CC       macropexophagy. {ECO:0000269|PubMed:18331717}.
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DR   EMBL; AY310405; AAQ63446.1; -; Genomic_DNA.
DR   AlphaFoldDB; I6LAD1; -.
DR   IntAct; I6LAD1; 3.
DR   MINT; I6LAD1; -.
DR   iPTMnet; I6LAD1; -.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000407; C:phagophore assembly site; IEA:UniProtKB-SubCell.
DR   GO; GO:0005775; C:vacuolar lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Autophagy; Membrane; Peroxisome; Phosphoprotein; Protein transport;
KW   Transport; Vacuole.
FT   CHAIN           1..384
FT                   /note="Autophagy-related protein 30"
FT                   /id="PRO_0000422168"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          266..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         112
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18331717"
FT   MUTAGEN         112
FT                   /note="S->A: Impairs pexophagy."
FT                   /evidence="ECO:0000269|PubMed:18331717"
SQ   SEQUENCE   384 AA;  44298 MW;  AE7440438C2B78A0 CRC64;
     MFSRKQVQKR NNELSSLHCS NSSNSLNRIH KNEETAKGTV GVNARGNNRS DNVASPGQLR
     PRTSSILTDN SEWILFSPEN AEGEYVITSS DGIRRTNSNH YYYNYNEDDI LSSSRRSSED
     VYDAEQEYTE QPVNNHVQVE DEEDDDSIIN DLTHVVDDYD YEEEDDKQDL TTRIDNWRKK
     QVSELLNELN HDDDLDPVLN RDKIDLIQSW GIENEKLNTK PRAKKRQRKS KRASFYGQDL
     LSKYSMEDLK IIKQIVAQLR DDLDKVKHDK PSSPLPNYHN TLKQAPSSNS QNPSFISYYS
     NYLTKNNSQQ TPNSQSTSGS LLNNPNLEKY LPLFLKNLLY EDSNGSHQHP ETSEKEHFWD
     NDLKSVNSSI LTLSSNSKLK QEIL