ID A0A0A2IA16_PENEN Unreviewed; 554 AA.
AC A0A0A2IA16;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Autophagy-related protein 17 {ECO:0000256|ARBA:ARBA00013806, ECO:0000256|RuleBase:RU368080};
GN ORFNames=PEX2_089120 {ECO:0000313|EMBL:KGO54881.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO54881.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO54881.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO54881.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO54881.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JQFZ01000212; KGO54881.1; -; Genomic_DNA.
DR RefSeq; XP_016597178.1; XM_016746182.1.
DR AlphaFoldDB; A0A0A2IA16; -.
DR STRING; 27334.A0A0A2IA16; -.
DR GeneID; 27681602; -.
DR HOGENOM; CLU_028356_0_0_1; -.
DR OrthoDB; 1940609at2759; -.
DR PhylomeDB; A0A0A2IA16; -.
DR Proteomes; UP000030143; 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:UP000030143}.
FT DOMAIN 41..465
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 554 AA; 60989 MW; 8F0A7C8B7ED545ED CRC64;
MASLQSSSSS IRPQVGLNEG DQQSLPQVDT LISYLLGAKR SLSSITHVWR ANEIVTASHS
ALEKSVVLCS RTGFLRRGLN GQLRLLYDVR TEVEQISYRG RDEFSVALKN LDAADAQLRN
TLELLRGTIV HASFRPGDEE QKSLHDFVDE RGVEELHASL KSSIDRTNTA RAELDTSNRE
FDDELQATRQ SLRHYHTATK LASSRLSITS SSSSASDSGL LTLSSMPGQI QSLEAHAQEM
AILLEALVRH FDLCVTAVKH TDGGGAVARS ITGDMPTGVD GSNDGMPNIG AEINANLNAP
LDPMTDAEYQ EMVAVLIKDA PEADDVVMEI QDRINEMESI FEQVQAQRDA LLSISKATIE
VHSHLSSLAS SRLPRYISQA HNFTRVWHEE NDRINSGLAE LSDLHSLYDG FLNAYDSLML
EVARRHHVRQ RVEKVLRDTR HKLDQLHDED AAARDTFRVE QGDFLPSDIW PGVGLAPMQV
QFLRLSGGHL DNGAVAQNAL EEPSVHQCTG SAKARVSDGS AEGEQIPDLP KDLIEEAFAR
VKARNNVVSQ MHTA
//
