AT221_ASPCL
ID AT221_ASPCL Reviewed; 610 AA.
AC A1C7M3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Autophagy-related protein 22-1;
GN Name=atg22-1; ORFNames=ACLA_074310;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027045; EAW14394.1; -; Genomic_DNA.
DR RefSeq; XP_001275820.1; XM_001275819.1.
DR AlphaFoldDB; A1C7M3; -.
DR STRING; 344612.A1C7M3; -.
DR EnsemblFungi; EAW14394; EAW14394; ACLA_074310.
DR GeneID; 4707740; -.
DR KEGG; act:ACLA_074310; -.
DR VEuPathDB; FungiDB:ACLA_074310; -.
DR eggNOG; ENOG502QVD3; Eukaryota.
DR HOGENOM; CLU_017518_1_0_1; -.
DR OMA; QPWEIFP; -.
DR OrthoDB; 1460747at2759; -.
DR Proteomes; UP000006701; 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..610
FT /note="Autophagy-related protein 22-1"
FT /id="PRO_0000318014"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
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 485..507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 550..570
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 610 AA; 66051 MW; 39CD625705E26036 CRC64;
MIFTSTPPAP PPADAQQRQP RYPGEDTTPT SRREIWGWYT YGIAAEVFAV CGVGSFLPLT
LEQLARERGT LLSSHLPCVG PGSPSAAPGN GTTPAMLRRD GLGSDQCVVG LFGLQINTAS
FAMYTFSLAV LVQALTLISF SALADYEKNR KTLLLTFGLI GSVSSMLFVF ISPRLYILGA
ILVVIGVTCL GSSFVVLNSF LPVLVANDPS IQTARKTEGE ELPHLDSSGE YTRSGSFNRG
DNRGFDDYVA PEHGLKPKTT DSTSPEMQLS TKISSKGVGL GYCAAVLVQV LSILLLFTLS
KTSLPKISGT LPLRFVLLLV GIWWFSFTVV TRRWLRNRPG PPLDTSKGGA RWRIWLRLVG
FAWKSLWKTV KVAAKLREVV IFLIAWFLLS DAMATVSGTA ILFARTELKM STTAVGLLSI
TATLSGMTGA FLWPVVSRRL KLKSNHTIML CIALFEIIPL YGMLAYIPLV KKWGVIGLQQ
PWEIFPLGIV HGLVSGGLSS YCRSFFGVLI PPGSEAAFYA LYAATDKGSS FIGPAVVGVL
IDATGQVRSG FFFIAVLIVL PIPLIWMVNA EKGRQEGLAM AEMLEKSHGE NSSEFGHPSE
EAEGLLARNP
