ID A0A3M2SD90_9HYPO Unreviewed; 1441 AA.
AC A0A3M2SD90;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Autophagy-related protein 11 {ECO:0000256|RuleBase:RU367075};
GN ORFNames=CDV36_004806 {ECO:0000313|EMBL:RMJ15540.1};
OS Fusarium kuroshium.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=2010991 {ECO:0000313|EMBL:RMJ15540.1, ECO:0000313|Proteomes:UP000277212};
RN [1] {ECO:0000313|EMBL:RMJ15540.1, ECO:0000313|Proteomes:UP000277212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR3666 {ECO:0000313|EMBL:RMJ15540.1};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:RMJ15540.1}.
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DR EMBL; NKUJ01000063; RMJ15540.1; -; Genomic_DNA.
DR STRING; 2010991.A0A3M2SD90; -.
DR Proteomes; UP000277212; 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 Gene3D; 1.10.287.1490; -; 2.
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:UP000277212};
KW Transport {ECO:0000256|RuleBase:RU367075};
KW Vacuole {ECO:0000256|RuleBase:RU367075}.
FT DOMAIN 119..463
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT DOMAIN 1118..1256
FT /note="Autophagy-related protein 11 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10377"
FT REGION 589..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1220..1242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 870..981
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1124..1151
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 621..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1441 AA; 162924 MW; 02D6228B2088C92F CRC64;
MALQVLIAHT GQRLEVDIAQ FSVLDDLKAW VSRNTSIPPQ HIVALTPHGR TVKFANLHAE
VCNTSKDKSS LTRHKKEVFI YDIRISASGA ANLIVPISAP KPYAITSAPN SIDDVQAISS
WQTLYQDRRN WAMRLAEDCG HMNAATHARY DEIDVIIKCL DAAVTNLEIS IKQIEPKYTD
LKKWVTPTLE EHGNLVSTWE RCLELARNTP ISPLMVRFMT RREVKKSRPT LEDLIELDTA
KKAGKLAPTA HRRFSDKAKE LDNAASRMYK GLEALIGDFE KLMSRSALTH SADSGQLLED
IEAVVKQMDS DYRTALSYGN SQRDLAQASK TASIHTEHMV PTLKMRAQEM DDMLHYATDA
RNSIASESAK FMRYVTEITS LHSNVKTQIN VLNQSEDDMT TFDYLRLIHQ LPYMYAAFVA
EAVRRREWVD KVKTDSSTLA NEMALFQDEE SKRRRKWQKM IGSMYGPDLD TNVMGLEVNL
LGEDIPWPSV TKEDLTDFIQ VLQEQDIDQA VLGDVVKLVQ DLDHPTKQQS KRLKAFKNGS
VHEAALGRSG LMIRGDDDLL RSLQDDKGKL ENKLKTAESR VRRLEDLLHR QSQATRPGNL
FHPSGPPQQR ERGNSGSSVR SSRFDDRRRS SDGLDPLLRR VTQLENELRE EKQRSTRLQQ
ELATQATHHE DMKGQNEDLK RRHDDLNGQI EEVNTTKKDL LGNMEAFKRE FLEERKSLES
EIKNLKARLE DTEDEIENFD QSRQHEKAGY VVRVEELEAE IEQINKQRQD DTLKAQGQVE
FLRKETRIQR EQQEALERQV QSAQEEARNA SKMLATAEET LENQWQALTK LFAELSPDST
IPDNLVDLSD SLIAIATELV AKLRNSDADI DLLKTDVEHL TATAKELREQ IAEKDSKLSE
DELTTVHLRE SLSKEEAKVS ALEAELADGR EQLTELRAKL SDGETGSEAL QKRVEEEEKK
VMTLTEEVAS KQSQVGSLEE ELHLFQEKVE ALHGKLTSLG TQYEQRDEKT KDLTQRLYSQ
NDRMCRLLER VGFAITRKDG EVTVTKIPRA ERNVQNPNDS SDPGSSLRRS GTLSRAMADS
TDLELLYWLS NSDMQAEGEK YEAFMNKLGN FDMDLFSETI YRRIKEVEHM ARKWQREARA
YREKAHHLQK DSHEKIAFKH FKEGDLALFL PTRNQQAGAW AAFNVGFPHY FLREQDAHRL
RHREWLVARI SRIQERVVDL SKSLQPSNET DSINDEENDN PFQLSDGLRW YLIDAFEDKP
GAPSTPGMGK STVAANTVEA TANIHTHATG ARGKSRDSVA SIEGINKTLS KSLESRRSST
GSRKALPFQL GGTTLLKNSA LASETNSLRA HPTDTPSGAS PTQGGPLTTT NASTAQRAAA
DGQDAQRNEQ ADPSESSAKG AAAEPRIAVQ REDSIESQTK KSVVWDSLWS VDYNYEGGGR
K
//
