AT222_PENRW
ID AT222_PENRW Reviewed; 607 AA.
AC A7KAN0; B6GXV5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Autophagy-related protein 22-2;
GN Name=atg22-2; Synonyms=atg22a-2; ORFNames=Pc12g00720;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=17204848; DOI=10.4161/auto.3595;
RA Meijer W.H., van der Klei I.J., Veenhuis M., Kiel J.A.K.W.;
RT "ATG genes involved in non-selective autophagy are conserved from yeast to
RT man, but the selective Cvt and pexophagy pathways also require organism-
RT specific genes.";
RL Autophagy 3:106-116(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
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 ECO:0000269|PubMed:17204848}.
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; EF110896; ABO31317.1; -; Genomic_DNA.
DR EMBL; AM920427; CAP79699.1; -; Genomic_DNA.
DR RefSeq; XP_002556974.1; XM_002556928.1.
DR AlphaFoldDB; A7KAN0; -.
DR STRING; 500485.A7KAN0; -.
DR EnsemblFungi; CAP79699; CAP79699; PCH_Pc12g00720.
DR GeneID; 8308774; -.
DR KEGG; pcs:Pc12g00720; -.
DR VEuPathDB; FungiDB:PCH_Pc12g00720; -.
DR eggNOG; ENOG502QVD3; Eukaryota.
DR HOGENOM; CLU_017518_1_0_1; -.
DR OMA; QPWEIFP; -.
DR OrthoDB; 1460747at2759; -.
DR BioCyc; PCHR:PC12G00720-MON; -.
DR Proteomes; UP000000724; Contig Pc00c12.
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..607
FT /note="Autophagy-related protein 22-2"
FT /id="PRO_0000318029"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 521..543
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 552..572
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 9..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 607 AA; 65399 MW; 8EAFAF7BB3D3136C CRC64;
MLSYISAAFQ SPSPDEGVQQ RPPRYVGEDT TPTSRREILG WYSYGIAAEV FAVCGVGSFL
PLTLEQLARE RGTLQTSRLP CVGPSAGNST NATEHGQCVV PVFGLEINTA SFAMYTFSLA
VLIQALTLIS FSALADYENN RKTLLMVFGF AGALASMLFV FIAPPLFVIG SILVVVGVTC
LGSSFVVLNS YLPVLVANDP SLQEGKADDG TEMSSFDRDE GDSEGNPWGK DHTDNDSLDG
LQPSDQPQSS LEGGMGTKAP LSSSPELQLS TKISSRGIGL GYCAAVFVQI ISIIMLLTLS
KTKLAKVSAT LPMRFVLLLV GIWWGAFTLV TRNLLKTRPG PRLDTVSTKG TGRWRAWLRL
VGFAWKSLWE TVKVVSKLRE VLIFLVAWFL LSDAMATVSG TAILFARTEL KLSTPLIGLL
SITATLSGMT GAFLWPQVSR YFRLQPSHTI ILCIALFEMI PLYGLLAYIP FIKNWGVFGL
QQPWEIFPLA IVHGVVSGGL ASYCRSFFGL LIPPGSEAAF YALYAATDKG SSFIGPAIVG
GIVDATGQIR SGFFFMAILI VLPIPLVWMV NADKGRREGL AMAETLGKSH GGPAEDAQEA
EGLLARE
