ID   ATG32_YEAS1             Reviewed;         529 AA.
AC   B3LTZ3;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Autophagy-related protein 32;
DE   AltName: Full=Extracellular mutant protein 37;
GN   Name=ATG32; Synonyms=ECM17; ORFNames=SCRG_05318;
OS   Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=285006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM11-1a;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA   Kruglyak L.;
RT   "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CH408055; EDV09624.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LTZ3; -.
DR   SMR; B3LTZ3; -.
DR   PRIDE; B3LTZ3; -.
DR   EnsemblFungi; EDV09624; EDV09624; SCRG_05318.
DR   HOGENOM; CLU_039418_0_0_1; -.
DR   Proteomes; UP000008335; 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_0000399760"
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;  58938 MW;  DB6A78AFD50F0619 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 LLNRIVQYSP 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