AT221_SCLS1
ID AT221_SCLS1 Reviewed; 598 AA.
AC A7E7N1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Autophagy-related protein 22-1;
GN Name=atg22-1; ORFNames=SS1G_01309;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476622; EDN96383.1; -; Genomic_DNA.
DR RefSeq; XP_001597115.1; XM_001597065.1.
DR AlphaFoldDB; A7E7N1; -.
DR STRING; 665079.A7E7N1; -.
DR EnsemblFungi; EDN96383; EDN96383; SS1G_01309.
DR GeneID; 5494038; -.
DR KEGG; ssl:SS1G_01309; -.
DR VEuPathDB; FungiDB:sscle_01g009780; -.
DR eggNOG; ENOG502QVD3; Eukaryota.
DR HOGENOM; CLU_017518_1_0_1; -.
DR InParanoid; A7E7N1; -.
DR OMA; QPWEIFP; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
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..598
FT /note="Autophagy-related protein 22-1"
FT /id="PRO_0000318033"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 534..554
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 598 AA; 64598 MW; 49BAC5C0BC56D0B4 CRC64;
MEDGGAGLRA PRYPAEDTSP TTDRELRGFF CYGLAAEVFA VCAVGSFLPV TLEQLAREQG
VLFIDKVTPC TAKNATVIAN ATVNALMSRA EGSDTHQCII NVFGAELTTA SFAMYTFSAS
VFMQALALVS VSSVADHGTW RKKLLAGFGL TGSVSAMLFL LVVPQIFVVG SFLTVICVVC
LGCSFVILNS YLPLLVLNHP VVQSDEDHPT ASSSIPLQPI SPQRSSRKSE ESLHQVNRKE
VDIGSKADSS DLQLSTKISS KGVGIGYMAA VSVQVICILI LYIMNKTGVS STLPLRTVLF
FVGSWWLTFT IPSVMWLRDR PGPPLPTALY EGRAFVRTCM SYTIFAWKSL WKTVKVAVKL
RQVLLFLIAW FLLSDAVATI SATAILFART ELQMGTVAVA LLSIIATSSG IIGATVWPII
SKRFTLKTNH IIVCCLLLLE LVPLYGLLGF LPFVQAWGVG GLQKWYEIYP LGIIHGMVMG
GLSSYCRSFY GLLIPPGSEA AFYALFAITD KGSSAVGPAI VGKIVDATGQ IRPAFGFLAV
LIALPIPLIW MVDVEKGQED AIRMAGLMKT TDDGHEDFES FEGSSDGHEA EGLMRDHD
