ID A0A0P7AT02_9HYPO Unreviewed; 1426 AA.
AC A0A0P7AT02;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Autophagy-related protein 11 {ECO:0000256|RuleBase:RU367075};
GN ORFNames=AK830_g5589 {ECO:0000313|EMBL:KPM40978.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM40978.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM40978.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM40978.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-2015) 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:KPM40978.1}.
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DR EMBL; LKCW01000073; KPM40978.1; -; Genomic_DNA.
DR STRING; 78410.A0A0P7AT02; -.
DR OrthoDB; 2727468at2759; -.
DR Proteomes; UP000050424; 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; -; 1.
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:UP000050424};
KW Transport {ECO:0000256|RuleBase:RU367075};
KW Vacuole {ECO:0000256|RuleBase:RU367075}.
FT DOMAIN 115..452
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT DOMAIN 1093..1231
FT /note="Autophagy-related protein 11 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10377"
FT REGION 581..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1325..1407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 837..969
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1099..1126
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 581..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..644
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1325..1343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1390..1404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1426 AA; 160671 MW; BEDE6FAC9C5223F9 CRC64;
MATQVLIAHT GQRLDVDTAQ FSILDDLKAW VSRSTSIPPQ HIVALTPQGR SVKFASLHAE
KEIFVYDIRI SQPALSKNTS IPISDAPLPK KYTTTNAPNS IDDVKAIASW QNLYKDRRSW
AMRLLEDCTH MNAATLARYD EIDVIVKCLD AAVTNLEISI KQIEPKYTEL KKWVTPALAE
HDQLVKKWEH YLLLATNTPI SASMVKFMTG RESIKTAPSL EDLIEFDTAK KAGKLAPAAH
RRFSDKAKDL DGTATRMYQG LEGLIGDFDK LMSRSALGHS MDSSQLLEDI EAVVKQIDSD
YRATLGYGNS QRDLALASKT ASIHTEHIVP TIKKRAQEMD EMLRYATEAR NSIASESANF
MRAITDITSL HSSVKGQINV LNQSEEDMST FDYLRLIHQV PYMYASFVVE AIRRREWVEK
VRTDSSTLAN EMALFQDEEA KRRRKWQKMI GSMYGPGLDT NVVGLEVNLL GEDSPWPTVT
KEDLDDFTQN LQDQGIDPEI LDDILKLVQE LIVPTKQQSK RLKAFKNGSV HEAALGRSGL
LIRGDDDLLR SLQDDKGKLE NKLRTAESRV RRLEDLLHRQ SQAARSGNLF QPQSPQPRER
QNSISSIKSS RFDDRRRSSD NGDHLLRRIT QMENELRQEK QRSTRLQQEL NSQATQHDDM
KGQIDEANST KKDLLGNMEA LEREFVEERK ALESEIKTLK SRLEDTEDDL EHFDESRQHE
KATYVEKVVA LQTELDELNK NRQDDVLKAQ GQVEFLRKET RIQREHQETL ERQVQDAQEE
ARTATKKLSA VEETAEAQSQ TLKKLHLQIL PDQSMPDDLV DMADAILSHA TSLISKLQNA
ESDTALLRSD LEQANNSVKE LRADISETAS KLSEEEMSAM HLRENLLEEK AKVAALEGEL
ADGREQLAEL RAKLTDGETG PGALQKRLEE EETKVMKLTE EVASRQSQVG SLEEELHLFR
EKVETAQSKL TGLTSQYESR DERTKDLTER VYTQNDRMCR LLERVGFAVT RNNGEMTINK
IPRAERASLI LNGSSDPAAS VRRSGTLSRI LVDNSTDLEP LYWLNSSDMK AEGEKYEAFM
KTLGNFDMDL FSETIYRRIK EVEHMARKWQ REARTYRERA HALQKDSHEK IAFKHFKEGD
LALFLPTRNQ QAGAWAAFNV GFPHFFLREQ DAHRLHHREW LVARISRIQE RVVDLSKSLQ
PSNETDSMND SENDNPFQLS DGLRWYLIDA FEDKPGAPST PGMGKSTVAA NTVEATANIH
THTTAGKGKN RDSVASIEGI NKTLSKSLES RRSSSGSKKA ALPFQLGGTA LLKNSALASE
TNSLRAIPTD TPSGTSPTQP GPLAASNVGL APRTQAEEQD GPKRVQPEDL GKSPPGESSK
KGGSASLDEP RTSVRREDSV QSESKKSVVW DSLWSVDYNY ESSTKK
//
