ID A0A166UIF3_9AGAM Unreviewed; 487 AA.
AC A0A166UIF3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Autophagy-related protein 17 {ECO:0000256|ARBA:ARBA00013806, ECO:0000256|RuleBase:RU368080};
GN ORFNames=FIBSPDRAFT_907542 {ECO:0000313|EMBL:KZP31720.1};
OS Fibularhizoctonia sp. CBS 109695.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP31720.1, ECO:0000313|Proteomes:UP000076532};
RN [1] {ECO:0000313|EMBL:KZP31720.1, ECO:0000313|Proteomes:UP000076532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP31720.1,
RC ECO:0000313|Proteomes:UP000076532};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV417488; KZP31720.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166UIF3; -.
DR STRING; 436010.A0A166UIF3; -.
DR OrthoDB; 1359250at2759; -.
DR Proteomes; UP000076532; Unassembled WGS sequence.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006914; P:autophagy; 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 Reference proteome {ECO:0000313|Proteomes:UP000076532}.
FT DOMAIN 29..430
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT REGION 121..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 54634 MW; 945494D8B245A3BD CRC64;
MSLHSSASPE HPHLISYLVV QSHQALQIGE QLCTRANSLS NASAQCAVDV MALDAKVKWI
SEAVLEQLKL AASVAKSIEH KRAQLDTRVH EWDEIRARRA SSLDTILDSL GKQLVPPDFH
QASSGSSLFG SQHSDEEAED AIGPSPQPQR SPTLTLRDQR TARREKELRD RKRWKTLRDF
VDERGIEDEL DAIESDRNDL DIVLGTTDSY PENLMDTVSG IEKSLPGKAA LPPINAIINS
QAQASTHMAN HLESLASHYE QMAGAMRESE AGETFSQDDL QDMNRDTEEL PSIMAELEEG
IRSIESSHEQ LSSGKTALSQ HLELLPDTLR DLDELGEIMG EMLQCQESVE ADADEHITTL
HQRLVTLEDL HQRFVAFQMS FDKLLVEMAR RRQYREAAEK IVEGMMVQLE TMAEEERLVR
VRFNADQGAH LPADICLCIE NPPTRWEVLP WNGEVMEELP DIDYDLIVEA RERVAGVEDV
VPGNESL
//
