AT221_PENRW
ID AT221_PENRW Reviewed; 592 AA.
AC A7KAM9; B6HK49;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Autophagy-related protein 22-1;
GN Name=atg22-1; Synonyms=atg22a-1; ORFNames=Pc21g11290;
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}.
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DR EMBL; EF110895; ABO31316.1; -; Genomic_DNA.
DR EMBL; AM920436; CAP96026.1; -; Genomic_DNA.
DR RefSeq; XP_002568161.1; XM_002568115.1.
DR AlphaFoldDB; A7KAM9; -.
DR STRING; 1108849.XP_002568161.1; -.
DR EnsemblFungi; CAP96026; CAP96026; PCH_Pc21g11290.
DR GeneID; 8309762; -.
DR KEGG; pcs:Pc21g11290; -.
DR VEuPathDB; FungiDB:PCH_Pc21g11290; -.
DR eggNOG; ENOG502QR9I; Eukaryota.
DR HOGENOM; CLU_017518_1_0_1; -.
DR OMA; MYPLGAV; -.
DR OrthoDB; 1460747at2759; -.
DR BioCyc; PCHR:PC21G11290-MON; -.
DR Proteomes; UP000000724; Contig Pc00c21.
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..592
FT /note="Autophagy-related protein 22-1"
FT /id="PRO_0000318028"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 468..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 502..524
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 534..554
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 572..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 592 AA; 64082 MW; BA3659F9C8B7C275 CRC64;
MSIQENVESP QYPGDDTRPT SKRELAGWYC YGWAAEVFVV CAMGSFLPIT LEQMARDRGV
LLSDKTTPCS ATWRPPLPPP GSDAPVYLPQ VSDGGQCIIY FLGAEINTAS FALYTFSLSV
LVQAVIIISM SGAADHGTYR KKLLIVFAFI GSIATMLFLV VVPKVYLLGG LLAIISNTCF
GASFVLLNSF LPVLVRHHPS LKESEEVASP DDNVTGPRGD PLFSSTGDID RTNVDDSTPL
LGPNREAGKT SAATITSLEL RLSTRISSYG IGIGYIGAVI LQVISILVVV VVRPPTFSLR
LVLFLIGLWW FVFTIPASLW LRTRPGPPLL DSGGKPLHSW TGYMVYAWKS LGKTVTRARQ
LKDIVIFLAA WFLLSDGIAT VSGTAVLFAK TQLNMKPAAL GLINVIVMLA GVFGAFSWSY
ISNFFNLRAS QTIIACIILF ELIPLYGLLG FIPAVQRVGL GLHQPWEMYP LGALYGLVMG
GLSSYCRSFF GQLIPPGYEA AFYALYAITD KGSSIFGPAI VGAITDRYGE IRPAFVFLAV
LIFVPLPLML LVDVDRGKRD AVALGAELDG IPQGSEYGAI SDDQTTEDPI EE
