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Database: UniProt
Entry: A0A0N0NHE7_9EURO
LinkDB: A0A0N0NHE7_9EURO
Original site: A0A0N0NHE7_9EURO 
ID   A0A0N0NHE7_9EURO        Unreviewed;       512 AA.
AC   A0A0N0NHE7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Autophagy-related protein 17 {ECO:0000256|ARBA:ARBA00013806, ECO:0000256|RuleBase:RU368080};
GN   ORFNames=AB675_4066 {ECO:0000313|EMBL:KPI34478.1};
OS   Phialophora attinorum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI34478.1, ECO:0000313|Proteomes:UP000038010};
RN   [1] {ECO:0000313|EMBL:KPI34478.1, ECO:0000313|Proteomes:UP000038010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI34478.1,
RC   ECO:0000313|Proteomes:UP000038010};
RA   Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA   de Vries M., Cruz L.M., Souza E.M.;
RT   "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT   131958.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPI34478.1}.
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DR   EMBL; LFJN01000059; KPI34478.1; -; Genomic_DNA.
DR   RefSeq; XP_017994441.1; XM_018144177.1.
DR   AlphaFoldDB; A0A0N0NHE7; -.
DR   STRING; 1664694.A0A0N0NHE7; -.
DR   GeneID; 28736057; -.
DR   OrthoDB; 1940609at2759; -.
DR   Proteomes; UP000038010; 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:UP000038010}.
FT   DOMAIN          44..453
FT                   /note="Autophagy protein ATG17-like"
FT                   /evidence="ECO:0000259|Pfam:PF04108"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          166..197
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   512 AA;  57007 MW;  937CE4C8F9CC96BA CRC64;
     MSLPVSTASL NRASNASSPS QSGQQAGPVT IDTLISYLVA AKRSLSSIHH VHRATTVLAE
     ARSAIESTAA LIARTTYLRR SLQSQLKILR GIQYELEGSA NAVQGEFQAL IQELDAAGKS
     LEHTIQRLKS TRIEDAFKPP PTPSEDQTSA VAPKDTLYDF VEESPAEQIR DAMKEVIDTV
     QDNQEETTAS IRNLEDDLQI INDLLTDRQD TSTSISDDYV PPDLTHLLRQ LESYAHSMAQ
     SLESLVKHFD LCATAIKHTE GAGAAVLRKY KAGNLPADVD VINEVEGPTE PMNDAERLEM
     LSVLQNDAAE VDDVVLEIAG QADDMDAHLN EILHWRRRHE RTHRDVSVEA FRRLETLGAK
     LSGFVAASNA AAQRWAASRE SLNDGIAGME DLEATYTNFL HAYDRLIIEA ARRRSVKKQM
     ERIVEDSQRT LDNLYEKDLG ERQMFREELG DFLPSDIWEG LHLGPARWDV RRVDQVREGK
     EEEGWLSVPE LERGVVEAAL RRVRADGEAA RS
//
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