ID   ATG32_ZYGRC             Reviewed;         503 AA.
AC   C5DZR8;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Autophagy-related protein 32;
GN   Name=ATG32; OrderedLocusNames=ZYRO0G06666g;
OS   Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS   / NRRL Y-229) (Candida mogii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=559307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC   Y-229;
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(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   -!- 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}.
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; CU928179; CAR29352.1; -; Genomic_DNA.
DR   RefSeq; XP_002498285.1; XM_002498240.1.
DR   AlphaFoldDB; C5DZR8; -.
DR   SMR; C5DZR8; -.
DR   STRING; 559307.C5DZR8; -.
DR   PRIDE; C5DZR8; -.
DR   EnsemblFungi; CAR29352; CAR29352; ZYRO0G06666g.
DR   GeneID; 8206085; -.
DR   KEGG; zro:ZYRO0G06666g; -.
DR   HOGENOM; CLU_039418_0_0_1; -.
DR   InParanoid; C5DZR8; -.
DR   Proteomes; UP000008536; Chromosome G.
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..503
FT                   /note="Autophagy-related protein 32"
FT                   /id="PRO_0000399765"
FT   TRANSMEM        380..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          98..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          151..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          328..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..131
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..174
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..343
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   503 AA;  55997 MW;  B627F7A50B416C15 CRC64;
     MTSTEGTGGG DGKGISGFSD IERRSILDPH LSVLELLRRP SDTRPHEALK GEVSDIVGNC
     AGTTGTGNGS ISQSWQTIHR NDSCLSVVPE RCPSQATAAG ILSSSDTSED EPDAVNSPSA
     VHQQLHATPP QKHTKSLEDY RSLNVGIPLV LPEDSNNINN NNKNGSTTGS NGEEDDNDTI
     TKSLNSSSNS FIMPKLSLSQ KTQKFRILVL GRPGLKFYHS IPKKYQHMFE LPRSHDPAEF
     KQYTGILVVF QELKEMVSLL NRVCQCNPNR PVIPVCQSGQ RQQVRNLLES LLKNRLVSLL
     YPPVVVNNQP DLLGMFRFLQ ELSKTVSDNS DMDAEEPNNG SKRLKRSLQR KKKKFIETSA
     ERNGRPHKKR HNNEKVNRWV LWGVSLTLGV GVGYCISHLV SSTWISLTTN PLGPVDPESV
     SKDLFVFDRQ ELKLGEMDMD SDHPFGHALF LFKQALKQWN LAVKQFLGRH LSCMERIGPA
     NCLEWPTSDE HTNRVLALGY VML