ID   ATG22_KLULA             Reviewed;         492 AA.
AC   Q6CUZ1;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Autophagy-related protein 22;
GN   Name=ATG22; OrderedLocusNames=KLLA0C01188g;
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: 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; CR382123; CAH01099.1; -; Genomic_DNA.
DR   RefSeq; XP_452248.1; XM_452248.1.
DR   AlphaFoldDB; Q6CUZ1; -.
DR   STRING; 28985.XP_452248.1; -.
DR   PRIDE; Q6CUZ1; -.
DR   EnsemblFungi; CAH01099; CAH01099; KLLA0_C01188g.
DR   GeneID; 2892359; -.
DR   KEGG; kla:KLLA0_C01188g; -.
DR   eggNOG; ENOG502QR9I; Eukaryota.
DR   HOGENOM; CLU_017518_1_0_1; -.
DR   InParanoid; Q6CUZ1; -.
DR   OMA; QPWEIFP; -.
DR   Proteomes; UP000000598; Chromosome C.
DR   GO; GO:0071627; C:integral component of fungal-type vacuolar membrane; IEA:EnsemblFungi.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
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; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF11700; ATG22; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
PE   3: Inferred from homology;
KW   Amino-acid transport; Autophagy; Glycoprotein; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..492
FT                   /note="Autophagy-related protein 22"
FT                   /id="PRO_0000207624"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        229..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        292..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        326..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        362..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        391..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        430..450
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        459..479
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        158
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   492 AA;  55407 MW;  DA776C7857EE518C CRC64;
     MSYEAVPAEN SAFIPDQAKR NIKGWYFYCF SSEPFIVSAV STYVPLLLEQ FGRINGVKLD
     DHSLRCEVND DKCVLPMFNG RWFIDTSSFA LYTFSLSVLF QTLLVISVSG IVDKCQSIAF
     KKRVLLFFGT VGALATWFIG TLRSDQYYVL PLLAIVGNCS YGVINVVGNS LLPVFVGFLV
     GNEDQLEVDI KTSIISGRGA SYGYFSALIV QLFSILLVKQ SKNHDNLQIA ILFVGLWWLL
     WQIPIAFLLQ DIPRDTDQEQ HEFTWANTGN YMEYGWNSLW ESLKHARLLK DVVIFLIGWF
     IISDSLTTIN STAILFAKTE LKMTAINLIT LSIITMVMAM LGAVYIPHLL SERLRLPLQQ
     VLIIIIIWSS VIPLYGMTGF VFQNIGLKHK FEMYILGVWY GVSLGGLAAV SRSLFSLLVP
     RGKESTFFSL FSVTDKGSSI LGPLLIGLIT DKTHNIRYAF YLLFLFLVVS LPVFHGLDVE
     RGKREARQLS TM