ID   ATG32_KLULA             Reviewed;         524 AA.
AC   Q6CYG2;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Autophagy-related protein 32;
GN   Name=ATG32; OrderedLocusNames=KLLA0A00660g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382121; CAH02615.1; -; Genomic_DNA.
DR   RefSeq; XP_451027.1; XM_451027.1.
DR   AlphaFoldDB; Q6CYG2; -.
DR   SMR; Q6CYG2; -.
DR   STRING; 28985.XP_451027.1; -.
DR   EnsemblFungi; CAH02615; CAH02615; KLLA0_A00660g.
DR   GeneID; 2896568; -.
DR   KEGG; kla:KLLA0_A00660g; -.
DR   eggNOG; ENOG502QY5V; Eukaryota.
DR   HOGENOM; CLU_039418_0_0_1; -.
DR   InParanoid; Q6CYG2; -.
DR   OMA; IPICQPG; -.
DR   Proteomes; UP000000598; Chromosome A.
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..524
FT                   /note="Autophagy-related protein 32"
FT                   /id="PRO_0000399758"
FT   TRANSMEM        396..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          165..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   524 AA;  57980 MW;  952455DB58A3CBFF CRC64;
     MSGSKGVWGA PPGNNNRQLY SLDAGSSGSG VSASSAQRHS ILDPHDSVMD LLNGQQSCAF
     DSRLIQNQDL IDRKGKSNNI DHNDINTHTH SKGLTDSWQA IDRDEYSFLN AGNHNNYHNT
     SNGDFNQQFG GVLSSDTSEE EVEINAAPSP NLSASQQHNQ FLAYPLSSTG FGDQGNSETT
     VHQFSDGDPV KSTKTGQFSK AELGAGTGED ETIMVNLGHS WAGSFFVMPK LSLSESMKRF
     KILILSDGDS ANSFYNRLSR YHRLMFDVGK LNEASKEEAL KYTAFMIIFS DSKKVTTILN
     RMWKKYGDFT LIPICQKGQK QSVTEKVKTF ANSNKIKLMS YPVVISDHYE IHGLLRHLHS
     LYVEVDSDYE TDIPKKTKPR KGAKKKPAPH LAKRWWFWPI SIALGVGIGC CVTFYFSKFE
     TSSYNSSVGV IQTADKEIDA IVDAIEGNSP SILEESSPQS ISDFLGQVCK LVKDTAIQIN
     ELLKQFLSAH LMTSAWIQSI GKEFMQPDSQ STISKVTALD LVMF