ID   ATG22_CANGA             Reviewed;         541 AA.
AC   Q6FX92;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Autophagy-related protein 22;
GN   Name=ATG22; OrderedLocusNames=CAGL0B00770g;
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: Vacuolar effluxer which mediate the efflux of amino acids
CC       resulting from autophagic degradation. The release of autophagic amino
CC       acids allows the maintenance of protein synthesis and viability during
CC       nitrogen starvation (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}. Note=Vacuole and punctate structures.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATG22 family. {ECO:0000305}.
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DR   EMBL; CR380948; CAG57904.1; -; Genomic_DNA.
DR   RefSeq; XP_445004.1; XM_445004.1.
DR   AlphaFoldDB; Q6FX92; -.
DR   STRING; 5478.XP_445004.1; -.
DR   EnsemblFungi; CAG57904; CAG57904; CAGL0B00770g.
DR   GeneID; 2886601; -.
DR   KEGG; cgr:CAGL0B00770g; -.
DR   CGD; CAL0127816; AUT4.
DR   VEuPathDB; FungiDB:CAGL0B00770g; -.
DR   eggNOG; ENOG502QR9I; Eukaryota.
DR   HOGENOM; CLU_017518_1_0_1; -.
DR   InParanoid; Q6FX92; -.
DR   OMA; MYPLGAV; -.
DR   Proteomes; UP000002428; Chromosome B.
DR   GO; GO:0071627; C:integral component of fungal-type vacuolar membrane; IEA:EnsemblFungi.
DR   GO; GO:0032974; P:amino acid transmembrane export from vacuole; IEA:EnsemblFungi.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   CDD; cd17483; MFS_Atg22_like; 1.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR044738; Atg22.
DR   InterPro; IPR024671; Atg22-like.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF11700; ATG22; 1.
DR   SUPFAM; SSF103473; SSF103473; 2.
PE   3: Inferred from homology;
KW   Amino-acid transport; Autophagy; Glycoprotein; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..541
FT                   /note="Autophagy-related protein 22"
FT                   /id="PRO_0000207620"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        332..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        402..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        431..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        470..490
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        499..519
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        308
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   541 AA;  60074 MW;  843DBCCB9143EB78 CRC64;
     MAYESLASEP NDGVTDHNDD ALYVGIDTLK AARDNIKGWY LYSFSSEPFV VSAVATYVPL
     LLEQFARING VQLDDHNAPC STSSSDKCVL GLFNNRVFVD SSSFALYVFS LSVLFQTVVV
     ISVSGMVDRW KTISFRKNVL VTFGMVGAFA TVLISLLNET QYYSLVVYYI VANSCYGVIN
     VVGNSLLPLF VDDLVRLQPD HTVPAAEELS LDTDDKDGLT TVISGRGASI GYSAALVVQL
     MSILLVRLSP SKQDIQYAVF FVGLWWAVWQ FPMYWLLSDS IIPDQQSNQA IANGRYYDID
     GSIFTFVNLS SLKYGWKLLG EALKHATLLR DVVIFLIGWF ILSDSLTTIN STAIIFAKTE
     LHMSTINLIS LSIITMISAM VGAFAIPQIV STSLHVPPQR TILLIICWAS IIPLYGMLGF
     IFQSFGLKHQ FEMFILGVWY GISMGSVAAV SRSLFTIIIP KGRESTFFSL FSITDKGSSI
     VGPFIIGIVT DKTHNIRYSF FILFILLVFS LPIFKMLNVE RGKREAEEIS KLHVNIDPIQ
     D