ID D4AM38_ARTBC Unreviewed; 587 AA.
AC D4AM38;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Autophagy-related protein 17 {ECO:0000256|ARBA:ARBA00013806, ECO:0000256|RuleBase:RU368080};
GN ORFNames=ARB_04728 {ECO:0000313|EMBL:EFE35794.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE35794.1, ECO:0000313|Proteomes:UP000008866};
RN [1] {ECO:0000313|Proteomes:UP000008866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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:EFE35794.1}.
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DR EMBL; ABSU01000002; EFE35794.1; -; Genomic_DNA.
DR RefSeq; XP_003016439.1; XM_003016393.1.
DR AlphaFoldDB; D4AM38; -.
DR STRING; 663331.D4AM38; -.
DR GeneID; 9521922; -.
DR KEGG; abe:ARB_04728; -.
DR eggNOG; ENOG502RYHP; Eukaryota.
DR HOGENOM; CLU_028356_0_0_1; -.
DR OMA; THVWRAN; -.
DR OrthoDB; 1940609at2759; -.
DR Proteomes; UP000008866; 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:UP000008866}.
FT DOMAIN 51..493
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 171..198
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 355..382
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 304..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 587 AA; 64873 MW; F8FA6F537641B244 CRC64;
MSSVASSASS VQSGRSGGTS HVHGHSYSPD QSRAQPDLDT LVSHLAAAKR SLSSIHHVWR
ANEIVTAARA ALEESVIVSA RTGFLRRGLD EQIRLLFKVR TEVEEVAHRG RAEFSAAIKE
LDTVDRRLQQ TLDSLREITL EPAFRSQEQR QEEAERGVSK TLHDFIDEHA VDDIRSLLKD
AIDNLSAAQT ELDVSNRAFD NDLQSIQQAL DKYRLSVKRG SVSSLSLSAS SSASRVKMPT
PAVIPEFLHS LELNAQEMAD LLESLVRHFD LCVTAVKHTE GGGVLARNIT GDLPTDVGVG
IRAGGNPQSN TSDGNNINND DAGNANLQLE PLTDSDYRDM INVIAKDAGE AEDVVLEIQD
RIAEMESILE RVLEQRDSLI AAGVSTTAVY RRLAEFQSTR LPGYVAQSHK FEQTWKTEHE
RMESGVADLN DLRGLYMGFL DAYDGLILEV ARRMSVKRAA EDILHDARAR LDALYEEDVR
AREAFRIDQG DYLPSDIWPG LSMPPSRVVF RRIREDDDTA QENKDETTSG AKPDDVEQQH
PEGDVQPTTK LDSSSKGDFG ESIPDLPKHV IEQAFARLNA RGTRLPP
//
