ID A0A3D8SJN8_9EURO Unreviewed; 1360 AA.
AC A0A3D8SJN8;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Autophagy-related protein 11 {ECO:0000256|RuleBase:RU367075};
GN ORFNames=DSM5745_03201 {ECO:0000313|EMBL:RDW86559.1};
OS Aspergillus mulundensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1810919 {ECO:0000313|EMBL:RDW86559.1, ECO:0000313|Proteomes:UP000256690};
RN [1] {ECO:0000313|EMBL:RDW86559.1, ECO:0000313|Proteomes:UP000256690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5745 {ECO:0000313|EMBL:RDW86559.1,
RC ECO:0000313|Proteomes:UP000256690};
RX PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA Xiong C., Yue Q., Zhang X.;
RT "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT and Morchella septimelata.";
RL IMA Fungus 9:199-223(2018).
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:RDW86559.1}.
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DR EMBL; PVWQ01000003; RDW86559.1; -; Genomic_DNA.
DR STRING; 1810919.A0A3D8SJN8; -.
DR OrthoDB; 2727468at2759; -.
DR Proteomes; UP000256690; 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:UP000256690};
KW Transport {ECO:0000256|RuleBase:RU367075};
KW Vacuole {ECO:0000256|RuleBase:RU367075}.
FT DOMAIN 52..399
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT DOMAIN 1012..1157
FT /note="Autophagy-related protein 11 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10377"
FT REGION 522..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1311..1336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 490..517
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 574..725
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 524..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1360 AA; 153468 MW; A3BB93E609E4F148 CRC64;
MTARGKNVKI QTLATEREVF VYDRRYVSEQ DNAELPKLPS PQPLVLDNPP DTLSDQNDLQ
AWRNLYSARK SWASKLTARC EVAYKTIREL NERTEIVNRA AGVALENLKT HVATLENRFQ
EAQVWANDLS KEQQSALGEW KRALSNLENI PARKEFPFLG RPSTPKRDSD RTGTLLDYVD
AVEVHKAGPE ASAASSRFNR QFQDIEQAVG EITADTQQLL DEVPSSSSDS VDGLLQEMET
LSRKIQSDYE HVLALPNNQK TLANISRLAF NHTQDFLPSM LEIGTEIREG LGGAARLYDA
AAKAALGRTK LISSTQSRLA DVQAHIANLT FQSDAFDLLY SVFHMPLVYG SVLVESVRRR
EFNEKMKSDS LTLAEELSVF QDEEQRRRKK WVKNMEDFLS VTDTTTPGIE VNLRGHEFDW
PTVTRKDVET YIEDLKSKPG TANAAQELAQ AFKELDAPTR VQRRRAKAFK QGSIFDLSRS
SLLLHSDEMV RSLKDEKLKL EEKLRGSESR IRKLEDLLHR HSQLGRPSSG NFSVDFPTSP
ASPHPDAMSR RSSVSSRRMS SNQTSEEKNL VNRIVHLEAD LATERETVQR LQREAHAERQ
TNTDKMQEAQ STKNDLIGNL EARQREFGDE RRYLEGEVKR FKIRVEELEE ELDRVIDSRD
HEKQDADERM HQLELELQDA HVRADEEMRK ANSLLEQMQS HKIAADRFRT RADELEKREV
EQNRKDQEMY HALQAALMNL SPGGSIPDEV ADIIKAIDVL SEGLAIHAKT AEDNATKAAA
ANKTLTEELE RMKSDYENTK NILEQRKSQL TQARGELEQE QSKRKSTESE LNDERARLLE
LESKLAAGET GAGALREHVA EEEQKLTDIN NQLVEVEARA RRSEEEALQW KKRAEALSDS
DKLVTAKVDV HRSRLEELSR QLFAQVEKLE RMLEQLGFTV IRQDGEIVVQ RSSKVNALSA
TADTLSQSGV VSVKPDVSLL TWMKAETPEQ ETNRFKAFLE SLHQFSVDIF GDAVVKRVKD
IEVLARKWQK EARGYRDKYH RMQSEAHDKI AYRSFKEGDL ALFLPTRNQA IRSWAAFNVG
APHYFLREQD VHKLQSRDWL LARITKIEER VVDLSKSMNG GNPDRRSIGE TSDGASIDDE
NPFELSDGLR WYLLDATEEK PGAPTTPGLG KSTVAPAHVD ARGSIRLKRT PAGANVTKTL
TKSLDSRRNS STSNKRGPTL SSRANDSTAD LVRAGQAEGE NSAAAIDSKS VSQSRERGQE
PGSIAISDEV LDRHRSQTLE HSGMLNGYAR HLHLDRERDA SAKSLSLSAN GAEMASSMAS
TQASTSTSVS GPSHRQLTRY RPWEKLWSVD LNYRLEGGDS
//
