ID   ATG32_CANGA             Reviewed;         492 AA.
AC   Q6FRR4;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Autophagy-related protein 32;
GN   Name=ATG32; OrderedLocusNames=CAGL0H06545g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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   -!- 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   -!- SIMILARITY: Belongs to the ATG32 family. {ECO:0000305}.
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DR   EMBL; CR380954; CAG60013.1; -; Genomic_DNA.
DR   RefSeq; XP_447080.1; XM_447080.1.
DR   AlphaFoldDB; Q6FRR4; -.
DR   SMR; Q6FRR4; -.
DR   STRING; 5478.XP_447080.1; -.
DR   EnsemblFungi; CAG60013; CAG60013; CAGL0H06545g.
DR   GeneID; 2888646; -.
DR   KEGG; cgr:CAGL0H06545g; -.
DR   CGD; CAL0130627; CAGL0H06545g.
DR   VEuPathDB; FungiDB:CAGL0H06545g; -.
DR   eggNOG; ENOG502QY5V; Eukaryota.
DR   HOGENOM; CLU_039418_0_0_1; -.
DR   InParanoid; Q6FRR4; -.
DR   OMA; IPICQPG; -.
DR   PHI-base; PHI:6582; -.
DR   Proteomes; UP000002428; Chromosome H.
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   Reference proteome; Transmembrane; Transmembrane helix; Vacuole.
FT   CHAIN           1..492
FT                   /note="Autophagy-related protein 32"
FT                   /id="PRO_0000399757"
FT   TRANSMEM        374..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..91
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   492 AA;  55053 MW;  84D7D162CAFB2C98 CRC64;
     MLRFQRGTVK ESSSAKLAST SRNGPESSIL DPHHSVMELL QRQMEGSEVP SESGVLGESW
     QQIRESDVGD GGDSNFDQQS NTSAILSSSS EASEDEDLDI QQQLLGGQQE YKNFHMTAEE
     QLQEQAQGQG FGRPSLLKGT QSRLSEQDSN RSGSVRTIVD KGSCSSSLDE HELNSIFTSD
     SMSLTKSTGS SSTSFVMPKL SLTYKPSQAK KLLVVGRLSK RFHQDIPREY RQYFHISQSS
     DPSEFQNYIG IVIVFQELKE FVAMLNRIVQ YTDKKPIIPI CQPGQRIRVK NILKSFLKND
     AITLWYPPVT IANEKSMEKL FKHTVKLVNK LENEEDVLSL STSDKSLSDE TSGYRKNNRR
     KKHGGKPSTN YSKWITWGIS LTIGVSIGYY ATYMITTTLL YGKAESHHAN EAKGFSITNG
     NSGSSSISHS TEYYESTISQ KGLLRNTIVF IKRTIHNLNG KVGTFFASIT QVIKQTPVRE
     DNQFYTLGYM LS