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AT221_EMENI
ID   AT221_EMENI             Reviewed;         588 AA.
AC   Q5AW93; C8VBB1;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 2.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Autophagy-related protein 22-1;
GN   Name=atg22-1; ORFNames=AN7437;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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=EAA62017.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AACD01000129; EAA62017.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001304; CBF79380.1; -; Genomic_DNA.
DR   RefSeq; XP_680706.1; XM_675614.1.
DR   AlphaFoldDB; Q5AW93; -.
DR   STRING; 162425.CADANIAP00000528; -.
DR   EnsemblFungi; CBF79380; CBF79380; ANIA_07437.
DR   EnsemblFungi; EAA62017; EAA62017; AN7437.2.
DR   GeneID; 2869459; -.
DR   KEGG; ani:AN7437.2; -.
DR   VEuPathDB; FungiDB:AN7437; -.
DR   eggNOG; ENOG502QR9I; Eukaryota.
DR   HOGENOM; CLU_017518_1_0_1; -.
DR   InParanoid; Q5AW93; -.
DR   OMA; MYPLGAV; -.
DR   OrthoDB; 1460747at2759; -.
DR   Proteomes; UP000000560; Chromosome IV.
DR   Proteomes; UP000005890; 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..588
FT                   /note="Autophagy-related protein 22-1"
FT                   /id="PRO_0000207622"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        301..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        365..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        399..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        434..454
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        471..493
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        507..527
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        536..556
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        255
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   588 AA;  64450 MW;  FB74D536FA4E92F3 CRC64;
     MQEDGIAEPG LLLPRYPGDD TRPTNKKELL GWYSYGWAAE VFTVCAMGSF LPITLEQMAR
     ERGVLLSDKT TPCTAIWKTP ESSNTSWQNS SPAAAGQCIV YILGAEINTA SFAMYTFSVS
     VLIQAILIIS MSGAADHGSY RKTLLVSFAA IGSICTMLIL AVTPKVYLLG GLFAIVANTC
     LGASFVLLNS FLPLLVRYHP SLLKEESGYM VRSPTENSGQ PIATDCFSND DPRAALLQGD
     GMTPEDTREF ISSSNTSKEL TISTRISSYG IGIGYIGAVF LQGICILVIV QTRQTTFSLR
     LVLFLIGLWW FIFTIPAAFW LRPRPGPPLL RAQDGKAYQS WLGYMAYAWK SLGRTAMRTR
     HLKDILLFLA SWFLLSDGIA TVSGTAVLFA KTQLNMEPAA LGMINVITMI SGVFGAFSWS
     YVSRVLNLRA SQTIIACIFL FELVPLYGLL GFIPAIKNLG FLGLQQPWEM FPLGVIYGLV
     MGGLSSYCRS FFGQLIPPGY EASFYSLYAI TDKGSSVFGP AIVGFITDHY GEIRPAFFFL
     AILILLPLPL MLLVDADRGK RDALALAEVL EARSSLEQRD YGTFSQQQ
 
 
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