ID   AT222_ASPTN             Reviewed;         591 AA.
AC   Q0CL24;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Autophagy-related protein 22-2;
GN   Name=atg22-2; ORFNames=ATEG_05610;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476600; EAU34679.1; -; Genomic_DNA.
DR   RefSeq; XP_001214788.1; XM_001214788.1.
DR   AlphaFoldDB; Q0CL24; -.
DR   STRING; 341663.Q0CL24; -.
DR   EnsemblFungi; EAU34679; EAU34679; ATEG_05610.
DR   GeneID; 4320790; -.
DR   VEuPathDB; FungiDB:ATEG_05610; -.
DR   eggNOG; ENOG502QR9I; Eukaryota.
DR   HOGENOM; CLU_017518_1_0_1; -.
DR   OMA; MYPLGAV; -.
DR   OrthoDB; 1460747at2759; -.
DR   Proteomes; UP000007963; 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; Glycoprotein; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..591
FT                   /note="Autophagy-related protein 22-2"
FT                   /id="PRO_0000318021"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        372..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        406..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        441..461
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        478..500
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        512..534
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        543..563
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          214..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        300
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   591 AA;  64183 MW;  5D39479DD0FE36EA CRC64;
     MQDDEITENI QPPPQYPGDD TRPTSKKELV GWYSYGWAAE VFTVCAMGSF LPITLEQMAR
     DSGVLLADKT TPCSATWKTP QGTSPTLSAD TTGLWSSQAP RTSQCIVHIL GAEINTASFA
     MYTFSVSVFV QAILIISMSG AADHGSYRKI LLVACALIGS ISTMMFIAVK PNLYILGGLF
     AVVANTCFGA SFVLLNSFLP LLVRHHPSLL AKHRQAGASP NGDRPPATHR AHRTEDEVNV
     TTPLLPSGST NTDGATQESV SDTSLELKLS TKISSNGIGI GYIAAVILQI ICIVVVVNTN
     QTTFSLRLVL FLIGLWWFIF TFPAALWLRP RPGPPLRYAD GGKERRSWLG YIAYAWKSLG
     RTAMRTRHLK DILLFLASWF LLSDGIATVS GTAVLFAKTQ LDMEPAALGM INVIAMMAGV
     FGAFSWSYVS RVLNLRASQT IIACIILFEL VPIYGLLGFI PAIKRLGFIG LQQPWEMYPL
     SFVYGLVMGG LSSYCRSFFG ELIPPGYEAA FYALYAITDK GSSIFGPAIV GAITDRYGEI
     RPAFGFLAIL ILLPLPLMLL VDVDRGKRDA QALSAELEGT RDEPVADGSL E