ID   ATG22_NEUCR             Reviewed;         737 AA.
AC   Q7SG38;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Autophagy-related protein 22;
GN   Name=apg-11; Synonyms=atg22; ORFNames=NCU07504;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002236; EAA35815.3; -; Genomic_DNA.
DR   RefSeq; XP_965051.3; XM_959958.3.
DR   AlphaFoldDB; Q7SG38; -.
DR   STRING; 5141.EFNCRP00000007386; -.
DR   EnsemblFungi; EAA35815; EAA35815; NCU07504.
DR   GeneID; 3881200; -.
DR   KEGG; ncr:NCU07504; -.
DR   VEuPathDB; FungiDB:NCU07504; -.
DR   HOGENOM; CLU_017518_1_1_1; -.
DR   InParanoid; Q7SG38; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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..737
FT                   /note="Autophagy-related protein 22"
FT                   /id="PRO_0000207626"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        232..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        289..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        395..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        426..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        487..507
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        524..544
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        559..579
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        593..613
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        632..652
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        661..681
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          115..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          327..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        354
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        419
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   737 AA;  80544 MW;  532FBC1F9EB2E686 CRC64;
     MAKISGLCVF KWYPLYAYQC PATGPSVQLK YSAMTPRHNN NVNHVYNGPD IQWEDESLRP
     PPAPRLFSRS SYASYASKAS KRSFYSYTSS CFEADDERSD TLSFADWITT TMSGRMSPAN
     AGDNSDSYPY GDDTDGDSSS GLPPPRYPGD DTRPTSQKEL AGWYAYAFAA EVYVICGIGS
     FIPILLESLA RENGVLLSDR SKPCGSSSDK HTTSAEGQCV VYVLGMEINT ASFAMYTFSV
     SVLLQALLVV SISCAADHGN FRKKLLLAFA WIGSACVMAY IFISKSTYLI GALLAIISNT
     SFGASFVLLN SFLPLLVRHH PEIDQVGDYG SPGYATTEEG DDEDDEYQED STRNSTTALL
     GSRRYEEGEP LSRVQTTEEL TSRELELSTQ ISAKGIGIGY IAGLFLQCVA IAILITLKNT
     TWSQRIVLCV IGAWWAIFTI PAAMWLRPRP GPPLPTKSNT GGIRALFHYT IYAWKSLFRT
     IHLARRLVDI VLFLAGWFLL SDAIATTSST AILFAKTQLH MEPWALGMIN VISTASGILG
     AFSWSFISRK FRLKAHQTIL ACIALFELIP LYGLMGYLPF VQAWGVGGLQ QPWEMYPLAA
     IYGFVLGGLS GYCRSLYGEL IPPGSEAAFY ALYAITDKGS SVFGPAIVGA IIDASGEIRP
     AFWFLAAIVG TPALFIWFIN VERGRTEGEA LAEIIEGFKM NGQNGLNGNG ADGLADDRRG
     SDASRAILGR YDDEDEE