ATG22_MAGO7
ID ATG22_MAGO7 Reviewed; 679 AA.
AC Q51IZ9; A4R0M3; G4MR55;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Autophagy-related protein 22;
GN Name=ATG22; ORFNames=MGG_09904;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001231; EHA57387.1; -; Genomic_DNA.
DR RefSeq; XP_003709999.1; XM_003709951.1.
DR AlphaFoldDB; Q51IZ9; -.
DR STRING; 318829.MGG_09904T0; -.
DR EnsemblFungi; MGG_09904T0; MGG_09904T0; MGG_09904.
DR GeneID; 2680874; -.
DR KEGG; mgr:MGG_09904; -.
DR VEuPathDB; FungiDB:MGG_09904; -.
DR eggNOG; ENOG502QR9I; Eukaryota.
DR HOGENOM; CLU_017518_1_1_1; -.
DR InParanoid; Q51IZ9; -.
DR OMA; MYPLGAV; -.
DR OrthoDB; 1460747at2759; -.
DR Proteomes; UP000009058; Chromosome 1.
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..679
FT /note="Autophagy-related protein 22"
FT /id="PRO_0000207625"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 569..589
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 598..618
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 679 AA; 75229 MW; 5EC54EEB20A3DF5F CRC64;
MAPRNPELPP TPLRHPQPQR PTIPRLFSRL SHASKRSFRS YSSSFEADDE RSGSDSRSQF
DSDSDSDMDT STERGQSRER RCRRSYGGEQ YADEDTRPTS EKELAGWYMY SFAAETYVIC
AISSFIPILL ESLARENGVL LKDRTSPCKA SYDKTPDGGN DDNQCVVHVL GMEINTASFA
MYTFSVSVLL QALLVVSISC AADHGNYRKK LLLAFAWIGS FSVMAYIFVS KEIYLLGAIL
AIISNTSFGA SFVLLNSFLP LLVRHHPRIE YAEPATGDDL DFESEDQMRN SASHLLADEH
DDHYALSRVH TKEELTSIEL QLSTEISAKG IGIGYCAGLF VQCIAIAIVF KLKNSTWSQR
VVLLFVGAWW AIFTIPAAMW LRPRPGPPLP AASESSRGGV AAFVSYTLYA WKALFRTVSL
ARRLIDIVLF LGAWFLLSDA IATTSSTAIL FAKTQLRMEP WALAMINVIS TTAGIAGAFS
WAFISRRLGL RPHQTILACI VLFELIPLYG LMGYLPFVKN WGVLGLQKPW EMFPLAAVYG
FVLGGLSGYC RSLFGELIPP GSEAAFYALY AITDKGSSIF GPAIVGAIID ATEEIRPAFW
FLAVMVGLPA PLIYFIDVDR GKVEGEKLAA VIEGYRRHQD ESFDDGRFPS DDDDDGRGPI
LGGRDDEDEH DTEREVRGR
