ID   ATG22_PICAN             Reviewed;         559 AA.
AC   A7KAK4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Autophagy-related protein 22;
GN   Name=ATG22;
OS   Pichia angusta (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=870730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC   Y-5445;
RX   PubMed=17204848; DOI=10.4161/auto.3595;
RA   Meijer W.H., van der Klei I.J., Veenhuis M., Kiel J.A.K.W.;
RT   "ATG genes involved in non-selective autophagy are conserved from yeast to
RT   man, but the selective Cvt and pexophagy pathways also require organism-
RT   specific genes.";
RL   Autophagy 3:106-116(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       ECO:0000269|PubMed:17204848}.
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; EF107726; ABO31064.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7KAK4; -.
DR   PhylomeDB; A7KAK4; -.
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; Glycoprotein; Membrane; Transmembrane;
KW   Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..559
FT                   /note="Autophagy-related protein 22"
FT                   /id="PRO_0000318032"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        358..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        393..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        425..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        453..473
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        493..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        523..543
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   559 AA;  61494 MW;  C282C4BA9160A3D8 CRC64;
     MTEPLLDSSS DDEPSLVLPE NINQPFTTGA EVFGWCLYSW AAEPFIVSVV GTYVPLLLEQ
     IARDNGVKLI DKITPCNQPH DPTIPIPSPP KDGDFPNSTL TYASQNDSCV LPMFGGRFYI
     DTSSYALYTF SMSVLIQTIL VISMSGAADR GSHRKSMLVG FGVTGGLITM CYWLVDDRNY
     YMASMLAILA NSAFGGVNVC GNSFLSLLVN NHPSVRQIHL SKSLKLARMG EISSKISGIC
     AASGYISALL MQIITMLVIL HVRNNPNIDS LIYPLKLVIG LVGLWWFVFQ LPIQFLLKPR
     LSKELHVSIE PPDPSKPGYS VNIVRYKMLV VGAYILHGYK TLFSAARAAS QLKDIMAFLL
     GWFIISDSLT TINSTAILFA KSDLQMTTVQ LSQIGVLTMI SAIAGSVLLP NVIQPYFKLG
     LKQTMILIIV WASLIPLYGI LGFFIRSLGL HHAVEMYVLA IWYGFSLGGV ATISRSLYSM
     LIPPGQESVF FALFSITDKG SSIVGPFLVG LIIDKTHDIR KCFWLLFVFL IAAVPVFWYG
     IDVDRGINEA TVLEHEQDG