ID B0XTS0_ASPFC Unreviewed; 551 AA.
AC B0XTS0;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Autophagy-related protein 17 {ECO:0000256|ARBA:ARBA00013806, ECO:0000256|RuleBase:RU368080};
GN ORFNames=AFUB_029720 {ECO:0000313|EMBL:EDP54912.1};
OS Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804 {ECO:0000313|EMBL:EDP54912.1, ECO:0000313|Proteomes:UP000001699};
RN [1] {ECO:0000313|EMBL:EDP54912.1, ECO:0000313|Proteomes:UP000001699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163
RC {ECO:0000313|Proteomes:UP000001699};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- FUNCTION: Autophagy-specific protein that functions in response to
CC autophagy-inducing signals as a scaffold to recruit other ATG proteins
CC to organize pre-autophagosomal structure (PAS) formation. Modulates the
CC timing and magnitude of the autophagy response, such as the size of the
CC sequestering vesicles. Plays particularly a role in pexophagy and
CC nucleophagy. {ECO:0000256|ARBA:ARBA00024948}.
CC -!- FUNCTION: Autophagy-specific protein that functions in response to
CC autophagy-inducing signals as a scaffold to recruit other ATG proteins
CC to organize preautophagosomal structure (PAS) formation. Modulates the
CC timing and magnitude of the autophagy response, such as the size of the
CC sequestering vesicles. Plays particularly a role in pexophagy and
CC nucleophagy. {ECO:0000256|RuleBase:RU368080}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU368080}.
CC Preautophagosomal structure membrane {ECO:0000256|RuleBase:RU368080};
CC Peripheral membrane protein {ECO:0000256|RuleBase:RU368080}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the ATG17 family.
CC {ECO:0000256|ARBA:ARBA00006259, ECO:0000256|RuleBase:RU368080}.
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DR EMBL; DS499595; EDP54912.1; -; Genomic_DNA.
DR AlphaFoldDB; B0XTS0; -.
DR SMR; B0XTS0; -.
DR EnsemblFungi; EDP54912; EDP54912; AFUB_029720.
DR VEuPathDB; FungiDB:AFUB_029720; -.
DR HOGENOM; CLU_028356_0_0_1; -.
DR PhylomeDB; B0XTS0; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR007240; Atg17.
DR InterPro; IPR045326; ATG17-like_dom.
DR PANTHER; PTHR28005; AUTOPHAGY-RELATED PROTEIN 17; 1.
DR PANTHER; PTHR28005:SF1; AUTOPHAGY-RELATED PROTEIN 17; 1.
DR Pfam; PF04108; ATG17_like; 1.
PE 3: Inferred from homology;
KW Autophagy {ECO:0000256|RuleBase:RU368080};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU368080};
KW Kinase {ECO:0000313|EMBL:EDP54912.1};
KW Transferase {ECO:0000313|EMBL:EDP54912.1}.
FT DOMAIN 43..467
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 551 AA; 60950 MW; 2FF58BAF901C3FDF CRC64;
MSSSESSSVS GGGRPDAGRL PGEEQAMPRL DTLISHLVAA KRSLSSINHV WRANEIVTAA
RAALEECVVV SARTAFLRRG LNNQLRLLYS VRTEVEEISL RGRSEFAAVL KDLDDADTRL
RRTLELLRET IVHPAFRPEG EDPKSLHDFV DERGVEELHA ALKSSIDRTT AAQAQLDSSN
HAFDDELLSI KEALGTYRTA AKLASSRSSS SASSSSTSNS SLPSISTMPS MLHSLEMHAQ
EMANLLESLV RHFDLCVTAV KHTEGGGAAA KSITGDMPVG VPVSGRMGSN IEEEINNNLN
APLDPLSNSE YQEMVNVLFK DAAEAEDVVM EIQDRIGEME SVLENVLAQR DALRSIYNAT
TDIYQHLSSL GSTRLPGYIA QAHNFTQVWH EENDRISGGL ADLSDLNSLY NGFLDAYDGL
IVEVARRKHV RQRVEKVLRD TRHKLDQLYE EDVTARETFR VEKGDYLPSD IWPEIGREPM
RIEFRRISGA KVQAVNLQSP NEQEAITDEQ KTANRLAPVE SKDGDEIIPD LPRELVEQAF
ARLKARAKDA T
//
