AT222_NEOFI
ID AT222_NEOFI Reviewed; 613 AA.
AC A1DI95;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Autophagy-related protein 22-2;
GN Name=atg22-2; ORFNames=NFIA_090600;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027696; EAW19102.1; -; Genomic_DNA.
DR RefSeq; XP_001260999.1; XM_001260998.1.
DR AlphaFoldDB; A1DI95; -.
DR STRING; 331117.A1DI95; -.
DR EnsemblFungi; EAW19102; EAW19102; NFIA_090600.
DR GeneID; 4587557; -.
DR KEGG; nfi:NFIA_090600; -.
DR VEuPathDB; FungiDB:NFIA_090600; -.
DR eggNOG; ENOG502QVD3; Eukaryota.
DR HOGENOM; CLU_017518_1_0_1; -.
DR OMA; QPWEIFP; -.
DR OrthoDB; 1460747at2759; -.
DR Proteomes; UP000006702; 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..613
FT /note="Autophagy-related protein 22-2"
FT /id="PRO_0000318027"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 613 AA; 66090 MW; 0CD224326FF1191E CRC64;
MVLNSTPPAS PGAEAQQRPP RYPGEDTAPT SRKEIWGWYA YGIAAEVFAV CGVGSFLPLT
LEQLARERGT LLSSHLPCVG SSSPSTAPGN GTTTATLRRD GTDNDQCVVS VLGLQVNTAS
FAMYTFSLAV LVQALTLISF SALADYENNR KTLLLAFGFI GSMTSMLFIF IAPPVYILGS
LLVVIGVTCL GSSFVVLNSF LPVLVANDPS IQTAHKEEGE ELSPVNSSGE FARSEDLDEE
NVRDSDDHFT TGHGLKTKAA GSASPELQLS TRISSKGVGL GYCAAVLVQI LSILMLFALS
KTSLPKISGT LPMRFVLLLV GIWWFSFTMV SRRWLRDRPG PPLASSKGAA SNSRWRIWLR
LIGFAWKSLW KTVKVAVKLR EVIVFLIAWF LLSDAMATVS GTAILFARTE LKMSTTAVGL
LSITATLSGM AGAFLWPVVS RRLRLKSNHT IMLCIALFEV IPLYGMLAYI PLFKKWGVIG
LQQPWEIFPL GIVHGLVSGG LSSYCRSFFG LLIPPGSEAA FYALYAATDK GSSFIGPAIV
GMLIDATGQV RSGFFFIAVL ILLPIPLIWM VNAEKGRQDG LAMADILEKS HGEHASEYGG
PSEEAEGLLA RDI
