AT221_PHANO
ID AT221_PHANO Reviewed; 566 AA.
AC Q0TWF4; Q0TWF5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Autophagy-related protein 22-1;
GN Name=ATG22-1; ORFNames=SNOG_16086/SNOG_16087;
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=EAT76458.2; Type=Erroneous gene model prediction; Note=SNOG_16086 and SNOG_16087 have been merged into one gene.; Evidence={ECO:0000305};
CC Sequence=EAT76459.2; Type=Erroneous gene model prediction; Note=SNOG_16086 and SNOG_16087 have been merged into one gene.; Evidence={ECO:0000305};
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DR EMBL; CH445367; EAT76458.2; ALT_SEQ; Genomic_DNA.
DR EMBL; CH445367; EAT76459.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001806215.1; XM_001806163.1.
DR RefSeq; XP_001806216.1; XM_001806164.1.
DR AlphaFoldDB; Q0TWF4; -.
DR STRING; 13684.SNOT_16087; -.
DR GeneID; 5983145; -.
DR GeneID; 5983146; -.
DR KEGG; pno:SNOG_16086; -.
DR KEGG; pno:SNOG_16087; -.
DR eggNOG; ENOG502QR9I; Eukaryota.
DR InParanoid; Q0TWF4; -.
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..566
FT /note="Autophagy-related protein 22-1"
FT /id="PRO_0000318030"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 547..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 566 AA; 61876 MW; B6270785CF46510E CRC64;
MSLNSEEDEA ELVQLQPRYN GEDTSATTNR ELNGWYAYPI AAEVFAVVAV GAFLPVILEQ
LARENGYFFS DSTKSCVDHG GSRRMRAEDG LKGSEQCMIK ILNSTISTSS FAMYTFSAAV
IVQAVTLVCF SSFADHGPYR KKMLMAFAYT GSVASALFIF ISPTVYFLAP ILVIVGVTSL
GCSFVLLNAF LPLLVANHAN NTGAKFATAD SSSDFELEAL NPNTQCGQSH ARSAHMSSRG
VGYGYMAAVF VQVISILILW LFSKTAIQKR HPSLPIRVIL LLVGMWWAAL TTPTLLWLRP
RPGPPLPSQE AKTLSAPTSR FRTFLFYTRF SLRSFWRTLL RAISLRQTLM FLISWFLLSD
AVATISGTAV LFARTELHMG TIAIALLSIT SIGSGIIGAF AWPRVQKRFS LQPKTILLCC
VAGMEMIPLY GLLGFIPLFK KLGFIGLQQP WEIYPVAVLH GIVMGGVSSY ARSVYAPLIP
EGSEAAFFAL YAVTDKGSSA FGPALVGWLV DHAGSIRPAF IFLAVLVVLP APLLWMLDVE
KGREDAKAMA DGEGRGRGTY ERVREE
