ATG22_YARLI
ID ATG22_YARLI Reviewed; 589 AA.
AC Q6CD56;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Autophagy-related protein 22;
GN Name=ATG22; OrderedLocusNames=YALI0C03608g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382129; CAG81705.1; -; Genomic_DNA.
DR RefSeq; XP_501406.1; XM_501406.1.
DR AlphaFoldDB; Q6CD56; -.
DR STRING; 4952.CAG81705; -.
DR EnsemblFungi; CAG81705; CAG81705; YALI0_C03608g.
DR GeneID; 2909909; -.
DR KEGG; yli:YALI0C03608g; -.
DR VEuPathDB; FungiDB:YALI0_C03608g; -.
DR HOGENOM; CLU_017518_1_0_1; -.
DR InParanoid; Q6CD56; -.
DR OMA; MYPLGAV; -.
DR Proteomes; UP000001300; Chromosome C.
DR GO; GO:0071627; C:integral component of fungal-type vacuolar membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0032974; P:amino acid transmembrane export from vacuole; IBA:GO_Central.
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..589
FT /note="Autophagy-related protein 22"
FT /id="PRO_0000207628"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 525..545
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 554..574
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 48..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..73
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 589 AA; 63883 MW; 5718F8CC51276E44 CRC64;
MDIVATTQKE LYGWYAYAWA AEPFMVVAVA TYIPQLLQSY ARQNAVLADD HSQPCDSPPV
PFPGDPGVPT DPGIPPNNSL SSSVPWFLRA NEIQLLESPD TVHTMKDHKA KPTQPTCVIK
FFGIYIDTAS FPLYTFSLSV LLQVVVVISM SGAADRGRFR KQLLLFFGIA GALTTGLFVF
ITPKRYYLGS FLAIVSNAAF GAATVCGNAY LPVLAAGMKD GTTSEEPSEP STPSDTSKPA
SRSENTPLLS ASGVDYETGE SSNTAEIVKI DHRANVSARI SGTGVALGYL AGFIVQIISI
YLVITTGSTT WSLRLALLIV GVWWLIFQIP VLMWLKPRPG PPLPIKTDPQ NHPWTATLDR
VTNGGWSYVT YGWKTLLVTF KEARQMKDVA LFLVGWFLVS DGITTINSTA VLFAQGELRM
SPANLAVMGM LVVISGISGA KLTPLIGGTR ASPIKSIVVV VSLAAAVPAY GILGFFFTNI
GLKNPWELYV LAVWYGFALG GLNTVCRSTF SMLIPRGKEA VFFSLFSVTD KGSSVLGPLL
VGLIVDKTHN LRHAFYLLLV LLITPIGLFL MIDMERGRKE AEYLETVEE
