ID A0A2G8RPE9_9APHY Unreviewed; 1403 AA.
AC A0A2G8RPE9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Autophagy-related protein 11 {ECO:0000256|RuleBase:RU367075};
GN ORFNames=GSI_14684 {ECO:0000313|EMBL:PIL23373.1};
OS Ganoderma sinense ZZ0214-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Ganoderma.
OX NCBI_TaxID=1077348 {ECO:0000313|EMBL:PIL23373.1, ECO:0000313|Proteomes:UP000230002};
RN [1] {ECO:0000313|EMBL:PIL23373.1, ECO:0000313|Proteomes:UP000230002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZZ0214-1 {ECO:0000313|EMBL:PIL23373.1,
RC ECO:0000313|Proteomes:UP000230002};
RX PubMed=26046933; DOI=10.1038/srep11087;
RA Zhu Y., Xu J., Sun C., Zhou S., Xu H., Nelson D.R., Qian J., Song J.,
RA Luo H., Xiang L., Li Y., Xu Z., Ji A., Wang L., Lu S., Hayward A., Sun W.,
RA Li X., Schwartz D.C., Wang Y., Chen S.;
RT "Chromosome-level genome map provides insights into diverse defense
RT mechanisms in the medicinal fungus Ganoderma sinense.";
RL Sci. Rep. 5:11087-11087(2015).
CC -!- FUNCTION: Involved in cytoplasm to vacuole transport (Cvt), pexophagy,
CC mitophagy and nucleophagy. Recruits mitochondria for their selective
CC degradation via autophagy (mitophagy) during starvation. Works as
CC scaffold proteins that recruit ATG proteins to the pre-autophagosome
CC (PAS), the site of vesicle/autophagosome formation. Required for the
CC Cvt vesicles completion. {ECO:0000256|RuleBase:RU367075}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU367075}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC Preautophagosomal structure membrane {ECO:0000256|RuleBase:RU367075};
CC Peripheral membrane protein {ECO:0000256|RuleBase:RU367075}. Vacuole
CC membrane {ECO:0000256|RuleBase:RU367075}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU367075}. Note=During pexophagy, accumulates in
CC the vacuolar membrane region, where the peroxisomes contact the
CC vacuole. {ECO:0000256|RuleBase:RU367075}.
CC -!- SIMILARITY: Belongs to the ATG11 family.
CC {ECO:0000256|ARBA:ARBA00009729, ECO:0000256|RuleBase:RU367075}.
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:PIL23373.1}.
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DR EMBL; AYKW01000068; PIL23373.1; -; Genomic_DNA.
DR STRING; 1077348.A0A2G8RPE9; -.
DR OrthoDB; 2727468at2759; -.
DR Proteomes; UP000230002; Unassembled WGS sequence.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000045; P:autophagosome assembly; IEA:UniProtKB-UniRule.
DR GO; GO:1903599; P:positive regulation of autophagy of mitochondrion; IEA:UniProtKB-UniRule.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR040040; ATG11.
DR InterPro; IPR019460; Atg11_C.
DR InterPro; IPR045326; ATG17-like_dom.
DR PANTHER; PTHR13222; RB1-INDUCIBLE COILED-COIL; 1.
DR PANTHER; PTHR13222:SF1; RB1-INDUCIBLE COILED-COIL PROTEIN 1; 1.
DR Pfam; PF10377; ATG11; 1.
DR Pfam; PF04108; ATG17_like; 1.
PE 3: Inferred from homology;
KW Autophagy {ECO:0000256|ARBA:ARBA00023006, ECO:0000256|RuleBase:RU367075};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|RuleBase:RU367075};
KW Protein transport {ECO:0000256|RuleBase:RU367075};
KW Reference proteome {ECO:0000313|Proteomes:UP000230002};
KW Transport {ECO:0000256|RuleBase:RU367075};
KW Vacuole {ECO:0000256|RuleBase:RU367075}.
FT DOMAIN 110..425
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT DOMAIN 915..1022
FT /note="Autophagy-related protein 11 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10377"
FT REGION 1027..1348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1374..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 488..582
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 611..708
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 742..804
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1027..1041
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1196
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1283..1341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1403 AA; 153964 MW; 2B149CE1FEE62D7B CRC64;
MIQLCRAEDG AVVQLDVSLW DLERLDNLES FICEKTGVPP EAVWAYLSDG RPLKGDNVRE
LAGLEDQTIY VFNKTYLNAD LEQVLHALHS EPQLQPTVED AIASTPPFRI SQLASSYMQA
ALAHVEHVNL TLTSLHYQQR ALRISSSALD HHVLATSDGF ETLAAIAERE LEKQARLLNG
LDADLEIASR VKVHKEFLSA SMRSAMETGG KARTLGDYVS RVKMQQVASS CLKTHEELKT
RFEEVQEAMA RLSRGGDEVR HAVGNNSSID DGEGCARRAQ ELWEKLSALN SAVERPGVVP
EKALQEFRQL DDALRIEVER VTDVKNAYTE QCIYTIRRIS ELNTDLVTIP SAMTSLQTSF
RAKTSFAHIA RLHSMLYAYG ATVVEVVRRK EFARFFYQRA QNILEVMAKL SSNERKRRQA
YKNEVQGELP FDVKAMDDVV PNIDFSPNGS NDPQYSLERI DIDDFLRVLD DLEHFAKDAK
DPAAEASVQE ARSKLDKLIG KMDSLESGFD RIAERSLLST SRLLSHRRRT TEDEQAYVEL
QQQLQELQQQ KAEGDAAQRQ SKAALEAEIA ALRDSLQMSE TARGQLERDL HATRAQLESE
ATSRRILDDR NSEMSKEADA KREALARALS EATEQTRTAE LLRQQLTQVR SEFEAVKELE
TRNADKVKLL LEEQARTLHR LEEARARGED LEAQIQTARA ESDDVKRALV EAGKEKDRLL
RAQASEHDRL LRDHIAEADG DRAVLEHQFS ELRAAVEDAE RQLKDARAQA EMANADAVGL
REELQRVEHE LRDTRRDERT VREDLRAGRA SQADFEHRLE QSERLVAQML DVALAFRDAH
VKALSNVQVM VAHPGSRAVG AANGDSGLSS SRHAIVAYSG DPASIDPSDP TAALEALRGF
DHDHFLDAIG KAGSTIRKWQ KQCKDYRERA KGKISFRNFA KGDLALFLPT RNSISKPWAA
FNVSFPHYFL QATGHLAEQL KTREWIVARI TSITERVVDS KDPATNPYGL GDGVKYYMLE
VEDWTQPSYP SKRRESSRKL PPIEPPSEPV TQPVPVTEAI PIPTGPPEPE VEESFSATRP
PTSRLFPRNR SASSPTAGPS SLSRLLAQAG PSEPPTSSSL GFGLASTDGK TSSDEALPLP
LPRVASPTMA ASPPDHDDHT SRSVSPNVPV SPPAIVPSQP PRAQSPVPPP SPTRHSKSPT
TPGAGPYPAN NHNPSQPSPL RSTSRASRGS SSSRFSRAIP TKAVPTTAIT EQAVSTLSTT
PSSASGSATS DHTLGVRPIP SALSNDVGTS TIPSPEGSPT LGMTSLLNQS HRRRTTSYHL
PNPRGSTVGL SSPTATAASS SPLAGAGIGA TASSRLANLA SSWGVSFGRR RRSELLEEHG
ASRSGRAPGG SSPIPESPTQ GSD
//
