ID   ATG22_YEAS7             Reviewed;         528 AA.
AC   A6ZTF2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Autophagy-related protein 22;
GN   Name=ATG22; Synonyms=AUT4; ORFNames=SCY_0545;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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}.
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; AAFW02000089; EDN62091.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZTF2; -.
DR   EnsemblFungi; EDN62091; EDN62091; SCY_0545.
DR   HOGENOM; CLU_017518_1_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032974; P:amino acid transmembrane export from vacuole; IEA:InterPro.
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; 1.
PE   3: Inferred from homology;
KW   Amino-acid transport; Autophagy; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..528
FT                   /note="Autophagy-related protein 22"
FT                   /id="PRO_0000318036"
FT   TOPO_DOM        1..98
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..130
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        152..153
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        175..210
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        232..241
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        263..318
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        319..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        340..352
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        353..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        374..388
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        389..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        410..417
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        418..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        439..485
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        486..506
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        507..528
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         278
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P25568"
SQ   SEQUENCE   528 AA;  58816 MW;  FC216DAD5817FDDB CRC64;
     MSYGTINDMN ESVTNYRIKK AQNNIKGWYA YSFSSEPFVV SAVSTYIPLL LQQFASINGV
     KVHDHSIPCL SETGSDSDKC VLGLFNNRIF VDTSSFALYV FSLSVLFQTI IVISVSGIVD
     LWGSVKFKGR ILVWFGIVGA LSTVAISKLN DTQIYSLAGL YIVANGCFGV INVVGNSLLP
     IFVKDSLKCQ SQGAYEPDKV DSLTTVISGR GASLGYSSAL IVQIVSMFLV ASKKGSKQDV
     QVAVLFVGIW WFVWQLPMIW LIDDVTIPIR ADDSTLASAR SPYPGEQDAL GQLNWKNYLS
     YGWVSLFESF KHARLLKDVM IFLIAWFIIS DSITTINSTA VLFSKAELHM STLNLIMISV
     LTVVNAMLGA FMIPQFLATK FRWTSSQTLM YIIIWASFIP FYGILGFFFN AFGLKHKFEM
     FLLAIWYGLS LGGLSAVSRS VFSLIVPPGK ESTFFSMFSI TDKGSSILGP FLVGLLTDKT
     HNIRYSFYFF FLLLMLSLPV LNCLDVKRGR REAEELSQVL PESERRLD