AT221_ASPOR
ID AT221_ASPOR Reviewed; 606 AA.
AC Q2UMJ2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Autophagy-related protein 22-1;
GN Name=atg22-1; ORFNames=AO090001000734;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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; AP007154; BAE57223.1; -; Genomic_DNA.
DR RefSeq; XP_001819225.2; XM_001819173.2.
DR AlphaFoldDB; Q2UMJ2; -.
DR STRING; 510516.Q2UMJ2; -.
DR PRIDE; Q2UMJ2; -.
DR EnsemblFungi; BAE57223; BAE57223; AO090001000734.
DR GeneID; 5991196; -.
DR KEGG; aor:AO090001000734; -.
DR HOGENOM; CLU_017518_1_0_1; -.
DR Proteomes; UP000006564; Chromosome 2.
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..606
FT /note="Autophagy-related protein 22-1"
FT /id="PRO_0000318018"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..500
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..534
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 543..563
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 596
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 606 AA; 66123 MW; F246945EAD43EE89 CRC64;
MREDEGLSPP QYPGDDTRPT SRKELAGWYS YSWAAEVFTV CAMGSFLPIT LEQMARDRGV
LLSDKVTPCQ ATWKAPKQLS PHETLSQTLI NALRYGRDVP GASQCVVYIF GVEVNTASFA
MYTFSVSVLV QAVLIISMSG AADHGTYRKV FLLTFALVGS ISTMSFLSVV PKLYLLGALF
AIIANTCFGA SFVLLNSFLP LLVRYHPSLL RGRNEISRQG AMGDDTWGNT SHDVNNVTTP
LLRSAQVDNG TITENAARVS LADTSLELEL STRISSYGIG IGYIGAVLLQ IVCILVVIST
HQTTFSLRLV LFVIGLWWFV FTIPAALWLR PRPGPPLSCA QDGKQHSWPG YIIHAWKSLG
RTVIRTRRLK DIMLFLASWF LLSDGIATVS GTAVLFAKTQ LGMQPAALGM INVVAMLAGV
FGAFSWSYIS RLLNLRASQT IIACIILFEL VPLYGLLGFI PAIRDLGFLG LQQPWEMFPL
SIVYGLVMGG LSSYCRSFFG ELIPPGYEAA FYALYAITDK GSSIFGPAVV GIVTDRYGEI
RPAFVFLAIL ILLPLPLMLL VDVDRGKRDA LALSAELEGS QELNAPTYGA VPCNRNDSES
AVVQSE
