ID A0A1J9QIQ2_9EURO Unreviewed; 1310 AA.
AC A0A1J9QIQ2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Autophagy-related protein 11 {ECO:0000256|RuleBase:RU367075};
GN ORFNames=AJ78_03990 {ECO:0000313|EMBL:OJD15772.1};
OS Emergomyces pasteurianus Ep9510.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX NCBI_TaxID=1447872 {ECO:0000313|EMBL:OJD15772.1, ECO:0000313|Proteomes:UP000182235};
RN [1] {ECO:0000313|EMBL:OJD15772.1, ECO:0000313|Proteomes:UP000182235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 9510 {ECO:0000313|EMBL:OJD15772.1,
RC ECO:0000313|Proteomes:UP000182235};
RG The Broad Institute Genomics Platform;
RA Cuomo C.A., Munoz J.F., Imamovic A., Priest M.E., Young S., Clay O.K.,
RA McEwen J.G.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (JUL-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:OJD15772.1}.
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DR EMBL; LGRN01000138; OJD15772.1; -; Genomic_DNA.
DR STRING; 1447872.A0A1J9QIQ2; -.
DR VEuPathDB; FungiDB:AJ78_03990; -.
DR OrthoDB; 2727468at2759; -.
DR Proteomes; UP000182235; 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.
DR SUPFAM; SSF57997; Tropomyosin; 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:UP000182235};
KW Transport {ECO:0000256|RuleBase:RU367075};
KW Vacuole {ECO:0000256|RuleBase:RU367075}.
FT DOMAIN 96..444
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT DOMAIN 1056..1201
FT /note="Autophagy-related protein 11 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10377"
FT REGION 566..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1229..1310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 536..563
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 620..754
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 568..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..832
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1310 AA; 147492 MW; 79EAB2946A9EE301 CRC64;
MSLHIYVAHT GEQLLADPVS FASPDALRTW ISRKASIPAH RQILMTARGR NVRPQTLATE
NEIFVYDRLY IGDGTVRDLQ EIALPERFAP ASPPDTLADQ NNLQAWRNLY MERRAWALNL
AAQCAPITKD IDNQIERTHV INRAVDVALE NLKSHVGNLE HKFQEAQSWA NDLLKEQQLA
LDSWRRVSTN IQTIPAKKDF TFLRRPSTPK KAKERPTGTL QDYIDVDRVK DAASQVSAVS
QRFARRMDEV EKSVHEVASE TESLVEASHP SPQENANSLL EEVETIAKKI ASDYEHVLAL
PNTQKTLSSV SRMALNHTKD LLPSMLEMGL EIQTTLEQSI KQRNLAMKSA VSRMQKISGI
ESRLARVQTE LSNLDVEGDV FETLYEASQL PTVYGSILIE AVRRLEWSNK MKTDSLSIAE
ELAVFRDEEQ RRRKKWIKNM GTLLSLPDDS TPGVEINLQS SQLPEWPEVS RKEVEAYIEE
LKTKPDTNSA VQELTQQLKD LDAPTRQQRR KSKAFKHGSV FEMSRSSIFN RGDDMVRSLK
DEKSKLEDRL KGSESRVRKL EDLLHRQSQM SRPVSANFGS EVAISPASPR PDALSRRSSV
SSRRMSSNQS PEDKALVQRI VSLEAELLAE KEAVLRLQKE AHLERQSTND KIQEAQSTKR
DLMENLEAQQ REFEDERRFL DSEAKTIKIK LEEVEEELDK VMDAREHERL DADGRLAALQ
TELDTQQKKT AGEIADLTSQ VQALRENIET TNAHNTTLQG QLEEVDRNQR DYVNALQTAH
AHLSPDGSAP DDLPSLVRAI EVLSEGLAIH SKGADEASAK ANEENKSLSE RADQMETEIE
DLRTRLAKAE TERSRLQTML SEETLKLSVV RTELEDERKQ LRTLRSKFSA GETGSEVLKE
RVAEEERKVT GLTEKLAIVE SRAQGFEAEI RIWQRKVEGL EAIGERNNSL LNTKAIWAKE
LSEKLFSHVE QLNRVLQQLG FTIIRQDNNL VIHRASKVNN NSSLLGESVN SPSATPIIFD
PKLLEWVNAS DPEEEQTNYA SFMTAVNEFS VELVGEAVVK RVKDIETLAR KWQKEARGYR
EKSHRFQGEA HEKIAYRSFK EGDLALFLPT RNQTIRSWAA FNVGAPHYFL REQEVHKLHT
RDWLLARISK IEERVVDLSK SMNGTNPDRR SIGETSDGAS IDDDNPFELS DGLRWYLLDA
SEEKPGAPST PGLAKSTVAS AHVDAKGSIR LKRASNGGGA TKTLTKSLDS RRNSSTSKLG
TPVPALQSVE SAGDNVLPAE GDSGAQQRRA EAPIFDEVRR DLLSGPSNGE
//
