ID   ATG30_KOMPG             Reviewed;         384 AA.
AC   C4R5T1;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Autophagy-related protein 30;
GN   Name=ATG30; OrderedLocusNames=PAS_chr3_1230;
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864;
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(2009).
RN   [2]
RP   SUBCELLULAR LOCATION, FUNCTION, PHOSPHORYLATION AT SER-112, MUTAGENESIS OF
RP   SER-112, AND INTERACTION WITH 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).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH ATG11 AND ATG17.
RX   PubMed=19605559; DOI=10.1091/mbc.e09-03-0221;
RA   Nazarko T.Y., Farre J.C., Subramani S.;
RT   "Peroxisome size provides insights into the function of autophagy-related
RT   proteins.";
RL   Mol. Biol. Cell 20:3828-3839(2009).
RN   [4]
RP   SUBCELLULAR LOCATION, INTERACTION WITH ATG37 AND PEX3, AND FUNCTION.
RX   PubMed=24535825; DOI=10.1083/jcb.201307050;
RA   Nazarko T.Y., Ozeki K., Till A., Ramakrishnan G., Lotfi P., Yan M.,
RA   Subramani S.;
RT   "Peroxisomal Atg37 binds Atg30 or palmitoyl-CoA to regulate phagophore
RT   formation during pexophagy.";
RL   J. Cell Biol. 204:541-557(2014).
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, ECO:0000269|PubMed:19605559,
CC       ECO:0000269|PubMed:24535825}.
CC   -!- SUBUNIT: Interacts with ATG11, ATG17, ATG37, PEX3 and PEX14.
CC       {ECO:0000269|PubMed:18331717, ECO:0000269|PubMed:19605559,
CC       ECO:0000269|PubMed:24535825}.
CC   -!- SUBCELLULAR LOCATION: Vacuole lumen. Preautophagosomal structure.
CC       Peroxisome membrane; Peripheral membrane protein. Note=Surrounds the
CC       peroxisome cluster, but a small amount is also inside the vacuole in
CC       methanol-grown cells. Upon induction of micropexophagy, localizes
CC       inside the vacuolar lumen. Also localizes near peroxisomes during early
CC       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; FN392321; CAY70917.1; -; Genomic_DNA.
DR   RefSeq; XP_002493096.1; XM_002493051.1.
DR   AlphaFoldDB; C4R5T1; -.
DR   STRING; 644223.C4R5T1; -.
DR   iPTMnet; C4R5T1; -.
DR   EnsemblFungi; CAY70917; CAY70917; PAS_chr3_1230.
DR   GeneID; 8200351; -.
DR   KEGG; ppa:PAS_chr3_1230; -.
DR   eggNOG; ENOG502STYG; Eukaryota.
DR   HOGENOM; CLU_754524_0_0_1; -.
DR   InParanoid; C4R5T1; -.
DR   OMA; DDAYNIS; -.
DR   Proteomes; UP000000314; Chromosome 3.
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   Reference proteome; Transport; Vacuole.
FT   CHAIN           1..384
FT                   /note="Autophagy-related protein 30"
FT                   /id="PRO_0000422169"
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: Blocks 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