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ATG22_COCIM
ID   ATG22_COCIM             Reviewed;         603 AA.
AC   Q1E8Z0; J3KIA5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 3.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Autophagy-related protein 22;
GN   Name=ATG22; ORFNames=CIMG_00973;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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; GG704911; EAS35619.3; -; Genomic_DNA.
DR   RefSeq; XP_001247202.2; XM_001247201.2.
DR   AlphaFoldDB; Q1E8Z0; -.
DR   STRING; 246410.Q1E8Z0; -.
DR   EnsemblFungi; EAS35619; EAS35619; CIMG_00973.
DR   GeneID; 4566561; -.
DR   KEGG; cim:CIMG_00973; -.
DR   VEuPathDB; FungiDB:CIMG_00973; -.
DR   InParanoid; Q1E8Z0; -.
DR   OMA; MYPLGAV; -.
DR   OrthoDB; 1460747at2759; -.
DR   Proteomes; UP000001261; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032974; P:amino acid transmembrane export from vacuole; IEA:InterPro.
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..603
FT                   /note="Autophagy-related protein 22"
FT                   /id="PRO_0000318025"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        342..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        368..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        401..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        439..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        464..484
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        539..559
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        254
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        582
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   603 AA;  65446 MW;  5C1ABB515EBE9327 CRC64;
     MTSSPPSTWR NLDENEALLR HPILNKYPGE DTRPTSKKEL AGWYSYGWAA EVFAVCAMGS
     FLPITLEQMT RDQGVLLSDK KTPCSASWPT APTAYAAADA TASPRVGPPQ CVIYVLGIEI
     NTASFAMYTF SISVLIQSVL IISMSAAADH GVYRKKFLLA FALMGALSMI LFLFLLPRFY
     LLAAVLAIIA NTGFGASFVL LNSFLPVLVR NDPSIQATRY AAASDEQTYY TQNPSGSNTI
     SPVDEPERLD VSSNDSALVS AELRLSTKLS SNGIGIGYIA AVLVQIGCIL LVVATHSTTF
     SLRLVLFIIG LWWLVFTIPA ALWLRPRPGP PVPDSAYGKG RWAWVSYIVF AWVSLGRTIV
     RARQLKDVLL FLAAWFLLSD GIATVSGTAV LFAKTQLGMN IAALGLINVI AMISGVLGAF
     SWSYISHHFN LRPSRTIVAC ICLFEVIPLY GLLGFLPFIK RLGVIGLQQP WEMYVLGAIY
     GLVLGGLSSY CRSFFGELIP PGFEASFYAL YAITDKGSSM FGPAIVGAIT DRYGEIRPAF
     GFLALLILLP LPLMLLVDVD RGKRDAKELA EALEGVKDMG TNGTGYATVA THEVEVGYEG
     DRE
 
 
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