ATG22_ASHGO
ID ATG22_ASHGO Reviewed; 507 AA.
AC Q751W1;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Autophagy-related protein 22;
GN Name=ATG22; OrderedLocusNames=AFR714W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS54086.1; -; Genomic_DNA.
DR RefSeq; NP_986262.1; NM_212398.1.
DR AlphaFoldDB; Q751W1; -.
DR STRING; 33169.AAS54086; -.
DR EnsemblFungi; AAS54086; AAS54086; AGOS_AFR714W.
DR GeneID; 4622551; -.
DR KEGG; ago:AGOS_AFR714W; -.
DR eggNOG; ENOG502QR9I; Eukaryota.
DR HOGENOM; CLU_017518_1_0_1; -.
DR InParanoid; Q751W1; -.
DR OMA; QPWEIFP; -.
DR Proteomes; UP000000591; Chromosome VI.
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..507
FT /note="Autophagy-related protein 22"
FT /id="PRO_0000207616"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 507 AA; 56467 MW; 72048489F5B53FA1 CRC64;
MSYETIPTSD ENFDRDVSAT NRNVFGWYLY AFSSEPFIVS AMSTYFPLLL EEFARNNGVQ
VDDHTVACGA EDKHCVLPLF GRRVFVDTSS FALYTFALGV LLQTVLVISV SGVVDVCKTV
RFKRNVLLSF GMVGGLATCS TVLLRGNQYY ILALLTVISN CCYGVINVVG NSLLPDVVSD
LKRVLYLYRV IDSDQLTTVI SGRGSGIGYI AAFVVQLCSV WLLRQPEYRD DIRVAVLLVG
GWWMLFQLPL IWMLDDVVVR ENSTQFKWSR SRQYLKAGWQ SLGHAAMHAN LLKDVLIFLV
GWFIISDSIT TINSAAILFS KTELHMSTVN LVVISILTMI NAVIGAYFVP QLLSERLELP
PHQSLIYLIC WAGVIPFYGT LGFVFQSIGL KHPFEMYILA VWYGISMGGL AAVSRSVFSL
LIPRGKESTF FSLFSITDKG SSVVGPLLIG LITDKTHNIR YSFYFLFLFV VASIPVFNAL
NVQRGKVEAE ELAGINESRL ETNDGFA