ID   ATG32_YEAS2             Reviewed;         529 AA.
AC   C7GUR3;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Autophagy-related protein 32;
DE   AltName: Full=Extracellular mutant protein 37;
GN   Name=ATG32; Synonyms=ECM17; ORFNames=C1Q_04175;
OS   Saccharomyces cerevisiae (strain JAY291) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=574961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAY291;
RX   PubMed=19812109; DOI=10.1101/gr.091777.109;
RA   Argueso J.L., Carazzolle M.F., Mieczkowski P.A., Duarte F.M., Netto O.V.C.,
RA   Missawa S.K., Galzerani F., Costa G.G.L., Vidal R.O., Noronha M.F.,
RA   Dominska M., Andrietta M.G.S., Andrietta S.R., Cunha A.F., Gomes L.H.,
RA   Tavares F.C.A., Alcarde A.R., Dietrich F.S., McCusker J.H., Petes T.D.,
RA   Pereira G.A.G.;
RT   "Genome structure of a Saccharomyces cerevisiae strain widely used in
RT   bioethanol production.";
RL   Genome Res. 19:2258-2270(2009).
CC   -!- FUNCTION: Mitophagy-specific receptor that recruits the autophagic
CC       machinery to mitochondria and regulates selective degradation of
CC       mitochondria. Mitophagy contributes to regulate mitochondrial quantity
CC       and quality by eliminating the mitochondria to a basal level to fulfill
CC       cellular energy requirements and preventing excess ROS production.
CC       Recruits ATG11 to the surface of mitochondria. Promotes also autophagy-
CC       dependent peroxisome degradation (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: interacts with ATG8 and ATG11. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}. Vacuole membrane
CC       {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC       Preautophagosomal structure membrane {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}. Note=Is recruited to the
CC       preautophagosomal structure during mitophagy and imported into the
CC       vacuole along with mitochondria during starvation. {ECO:0000250}.
CC   -!- PTM: Phosphorylation of Ser-114 and Ser-119 are critically important
CC       for mitophagy and for the ATG11-ATG32 interaction. Phosphorylation
CC       depends on both HOG1 and PBS2. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATG32 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ACFL01000319; EEU05446.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7GUR3; -.
DR   SMR; C7GUR3; -.
DR   Proteomes; UP000008073; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
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:0006914; P:autophagy; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Autophagy; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW   Phosphoprotein; Transmembrane; Transmembrane helix; Vacuole.
FT   CHAIN           1..529
FT                   /note="Autophagy-related protein 32"
FT                   /id="PRO_0000399761"
FT   TRANSMEM        389..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          345..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        348..366
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..381
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         114
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P40458"
FT   MOD_RES         119
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P40458"
SQ   SEQUENCE   529 AA;  58969 MW;  DB6A3DAFD50FB619 CRC64;
     MVLEYQQREG KGSSSKSMPP DSSSTTIHTC SEAQTGEDKG LLDPHLSVLE LLSKTGHSPS
     PMGQNLVTSI DISGNHNVND SISGSWQAIQ PLDLGASFIP ERCSSQTTNG SILSSSDTSE
     EEQELLQAPA ADIINIIKQG QEGANVVSPS HPFKQLQKII SLPLPGKEKT PFNEQDDDGD
     EDEAFEEDSV TITKSLTSST NSFVMPKLSL TQKNPVFRLL ILGRTGSSFY QSIPKEYQSL
     FELPKYHDSA TFPQYTGIVI IFQELREMVS LLNRIVQYSQ GKPVIPICQP GQVIQVKNVL
     KSFLRNKLVK LLFPPVVVTN KRDLKKMFQR LQDLSLEYGE DVNEEDNDDE AIHTKSRSYC
     RNKKAENSKK KSPKSNKKPK RKKQKFFTSW FTWGISITIG ISFGCCVTYF VTAAYEHQTV
     KSLSLRPSIL ASLLSLDSSS DTINTPATAS PSSTEQFLWF DKGTLQINFH SDGFIMKSLT
     IIKETWGKMN TFVLHALSKP LKFLENLNKS SEFSIDESNR ILALGYILL