AT222_PHANO
ID AT222_PHANO Reviewed; 680 AA.
AC Q0U103;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Autophagy-related protein 22-2;
GN Name=ATG22-2; ORFNames=SNOG_14513;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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 -!- SEQUENCE CAUTION:
CC Sequence=EAT78053.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAT78053.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CH445356; EAT78053.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001804697.1; XM_001804645.1.
DR AlphaFoldDB; Q0U103; -.
DR STRING; 13684.SNOT_14513; -.
DR PRIDE; Q0U103; -.
DR GeneID; 5981622; -.
DR KEGG; pno:SNOG_14513; -.
DR eggNOG; ENOG502QR9I; Eukaryota.
DR InParanoid; Q0U103; -.
DR OrthoDB; 1460747at2759; -.
DR Proteomes; UP000001055; 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..680
FT /note="Autophagy-related protein 22-2"
FT /id="PRO_0000318031"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 504..524
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 538..558
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 576..596
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..626
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 680 AA; 74817 MW; 6B016289E5FDCE25 CRC64;
MVPRAPRIGD FEPYRPQLLR GQTDDSDTSK LSVPLSSQSN EADDEQSLSD PSYDMESSAD
SPQYEGEDTR LTSNKELSGF YMYGWAAEVF VVCGIGSFIP VTLEQLAREN GVLLSDRTTP
CKAPRPITPS FSASSFEALL RPNPEKGQCV VHILGIEINT ASFAMYTFSI SVLIQALLII
SMSGAADHGE IQENIPLVFA FVGSIATMLF LPVVPKVYLL GAVLAIISNT CFGASFVLLN
SFLPLLVRFH PTVRYPESSA DTSYVSDEEE DDSQTPTQER IEHEARWANH LSQREAALDE
PANVTTALLP SRAPLTSPRV KPSTAPSQEL ALSTKISSYG IAIGYIAALL VQTMGIIVVI
FFQSSNFGLR LVLFIIGLWW FIFTIPTARW LRPRPGPPLH LAPQTSNFRT GLAYFSYSWK
ALARTATHAR LLKDVLLFLT AWFLLSDSIA TVSGTAVLFA KTTLGMSYAM LALINVIATL
SGVLGAFTWS RLSSFCALSP VQTILCCIFL FELIPLYGLL GYLPAVQRLG YLGLQQQWEM
YPLGAVYGFV LGGLSSYCRS LYGELIPRGY EAQFYALYAI TDKGSSVFGP AIVGAITDRW
GEIRPAFWFL AVLVGLPFPI MLFVNVERGR EEGAALARKL EELSRLRDEA VVAAEDEGED
ENLSRDVRQG LEESFSYQRS
