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}.
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; 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