ID   ATG33_YEAS1             Reviewed;         197 AA.
AC   B3RHM5;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=Autophagy-related protein 33;
GN   Name=ATG33; ORFNames=SCRG_04299;
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: Involved in the selective degradation of mitochondria via
CC       autophagy during starvation and at post-log phase. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATG33 family. {ECO:0000305}.
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DR   EMBL; DS981519; EDV08669.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3RHM5; -.
DR   EnsemblFungi; EDV08669; EDV08669; SCRG_04299.
DR   HOGENOM; CLU_105986_1_0_1; -.
DR   Proteomes; UP000008335; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Autophagy; Membrane; Mitochondrion; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..197
FT                   /note="Autophagy-related protein 33"
FT                   /id="PRO_0000399769"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          135..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         127
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q06485"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q06485"
SQ   SEQUENCE   197 AA;  20356 MW;  FA63D87B885C4C01 CRC64;
     MSVCLAITKG IAVSSIGLYS GLLASASLIT STTPLEVLTG SLTPTLTTLK NAATALGAFA
     STFFCVSFFG APPSLRHPYL LYGMLAAPLS SFVLGCASNY QSRKYSKVSK ESSLFPEDSK
     PAASELSDSI IDLGEDNHAS ENTPRDGKPA ATTVSKPAEA LHTGPPIHTK NLIAATAIAI
     VGFVQAVIGV YGEGQFI