AT221_NEOFI
ID AT221_NEOFI Reviewed; 609 AA.
AC A1DG37;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Autophagy-related protein 22-1;
GN Name=atg22-1; ORFNames=NFIA_082950;
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; EAW18344.1; -; Genomic_DNA.
DR RefSeq; XP_001260241.1; XM_001260240.1.
DR AlphaFoldDB; A1DG37; -.
DR STRING; 36630.CADNFIAP00007751; -.
DR EnsemblFungi; EAW18344; EAW18344; NFIA_082950.
DR GeneID; 4586798; -.
DR KEGG; nfi:NFIA_082950; -.
DR VEuPathDB; FungiDB:NFIA_082950; -.
DR eggNOG; ENOG502QR9I; Eukaryota.
DR HOGENOM; CLU_017518_1_0_1; -.
DR OMA; MYPLGAV; -.
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..609
FT /note="Autophagy-related protein 22-1"
FT /id="PRO_0000318026"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..509
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 552..572
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 214..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 609 AA; 65794 MW; C1AD5911BED30635 CRC64;
MRAGDETETS IMRPQYPGDD IRPTSKKELA GWYSYGWAAE VFTVCAMGSF LPITLEQMAR
DRGVLLSDKV TPCSATLNGP SKTSTQAQWT LSSRYYAGGP TVVSQCVVYI FGVEINTASF
AMYTFSVSVF IQAILIISMS GAADHGSHRK LLLVAFAVIG SVSTMLFLGV VPKIYMVGAV
IAIIANTCFG ASFVLLNSFL PLLVRHHPSV LRGAREPPPA LDGSRAQEGH SDTTNDIDHG
VESNATSPLL HAHQGNSENA EADMHPATPI TVSQELKLST RISSFGIGIG YIGAIILQIV
CILVVIATNQ TTFSLRLVLF LIGLWWFIFT IPAALWLRSR PGPPFTTTHQ GKHTRSWIGY
MAYAWKSLYR TAVRTRHLKD ILLFLAAWLL LSDGIATVSG TAVLFAKTQL NMQPAALGLI
NVIAMVAGVL GAFSWGSVSR VFNLSASQTI IACILLFELV PLYGLLGFIP AVKSLGFLGL
QQPWEMFPLG IVYGLVMGGL SSYCRSFFGE LIPPGNEAAF YALYAITDKG SSIFGPAIVG
IITDRYGEIR PAFVFLAILI FLPLPLMLLV DVERGKRDAL ALAAELQPSG AQTYGTLPAN
EDRAPPSEL
