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Database: UniProt
Entry: S7Q3D2_GLOTA
LinkDB: S7Q3D2_GLOTA
Original site: S7Q3D2_GLOTA 
ID   S7Q3D2_GLOTA            Unreviewed;       484 AA.
AC   S7Q3D2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Autophagy-related protein 17 {ECO:0000256|ARBA:ARBA00013806, ECO:0000256|RuleBase:RU368080};
GN   ORFNames=GLOTRDRAFT_77963 {ECO:0000313|EMBL:EPQ54057.1};
OS   Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS   rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX   NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ54057.1, ECO:0000313|Proteomes:UP000030669};
RN   [1] {ECO:0000313|EMBL:EPQ54057.1, ECO:0000313|Proteomes:UP000030669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ54057.1,
RC   ECO:0000313|Proteomes:UP000030669};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
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; KB469304; EPQ54057.1; -; Genomic_DNA.
DR   RefSeq; XP_007867398.1; XM_007869207.1.
DR   AlphaFoldDB; S7Q3D2; -.
DR   STRING; 670483.S7Q3D2; -.
DR   GeneID; 19308761; -.
DR   KEGG; gtr:GLOTRDRAFT_77963; -.
DR   eggNOG; ENOG502RYHP; Eukaryota.
DR   HOGENOM; CLU_024595_0_0_1; -.
DR   OMA; THVWRAN; -.
DR   OrthoDB; 1359250at2759; -.
DR   Proteomes; UP000030669; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU368080};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030669}.
FT   DOMAIN          25..429
FT                   /note="Autophagy protein ATG17-like"
FT                   /evidence="ECO:0000259|Pfam:PF04108"
FT   REGION          116..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          292..322
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        118..146
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   484 AA;  54200 MW;  29C4B529431DD626 CRC64;
     MSAERTPPPE QPHVVALVLQ SKKALQHGQA LCARAHAIST ESARHAVDVL ALDAKVKWTS
     NAVREQLKLA ASVARRIEAR RADVERQAKE WDIQKAQRSD ALDAILESLG EQVVPPDFYE
     TSSGTSPFGS QDSSEEEAQG QRRPVTQGSH DGLAPNGTHA RKKRPREDWS RWKTLRDFVD
     ERAIDEVLET MDNDRLALED VLATTADYST VLNGHITTIR EGMPGANTAP TIESVLLAQE
     KVSTDMAGHL ESLAAHYDQM AAALHDHEAG EAFSDEDLQE MNRDTEELPA IITELEDNVS
     SIERLNEQLQ RAKAAAQEHV SLHRSTLDDL EELGEVMTDM LQHQDQVQAD CVERMSHLQG
     HLMTLEELHH KYTSYQLSYN KLLIEIARRR QYREAAENIV RGMMAQLDAM TEEERIVRQD
     FNEEHGQYLP SDLCLCIENP PTKWAIVPWN GEPEEVLPDV DNDLLLEAKD RTVNSGGLAG
     SQSL
//
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