ATG11_MAGO7
ID ATG11_MAGO7 Reviewed; 1395 AA.
AC Q51UJ9; A4QVJ9; G4MSA0;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 3.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Autophagy-related protein 11;
GN Name=ATG11; ORFNames=MGG_04486;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Vacuole
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Note=During pexophagy, accumulates in the vacuolar membrane region,
CC where the peroxisomes contact the vacuole. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATG11 family. {ECO:0000305}.
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DR EMBL; CM001231; EHA58358.1; -; Genomic_DNA.
DR RefSeq; XP_003710970.1; XM_003710922.1.
DR AlphaFoldDB; Q51UJ9; -.
DR SMR; Q51UJ9; -.
DR STRING; 318829.MGG_04486T0; -.
DR PRIDE; Q51UJ9; -.
DR EnsemblFungi; MGG_04486T0; MGG_04486T0; MGG_04486.
DR GeneID; 2678072; -.
DR KEGG; mgr:MGG_04486; -.
DR VEuPathDB; FungiDB:MGG_04486; -.
DR eggNOG; ENOG502QVZE; Eukaryota.
DR HOGENOM; CLU_002803_1_0_1; -.
DR InParanoid; Q51UJ9; -.
DR OMA; GLRWYLI; -.
DR OrthoDB; 287492at2759; -.
DR PHI-base; PHI:2085; -.
DR Proteomes; UP000009058; Chromosome 1.
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:InterPro.
DR GO; GO:0000422; P:autophagy of mitochondrion; IEA:InterPro.
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; PTHR13222; 1.
DR Pfam; PF10377; ATG11; 1.
DR Pfam; PF04108; ATG17_like; 1.
PE 3: Inferred from homology;
KW Autophagy; Coiled coil; Membrane; Protein transport; Reference proteome;
KW Transport; Vacuole.
FT CHAIN 1..1395
FT /note="Autophagy-related protein 11"
FT /id="PRO_0000124549"
FT REGION 586..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1260..1395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 123..172
FT /evidence="ECO:0000255"
FT COILED 246..277
FT /evidence="ECO:0000255"
FT COILED 555..591
FT /evidence="ECO:0000255"
FT COILED 629..818
FT /evidence="ECO:0000255"
FT COILED 862..986
FT /evidence="ECO:0000255"
FT COMPBIAS 592..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1395 AA; 156360 MW; A56425534D96C411 CRC64;
MATQVLIAHS GQRLQIDTSR LTTLDEFRSA VSRSTSIPQN CIIALVPPGK ALRPQAIQME
KEIFVYDSRM TQTGAPGSPF PVKLEIDLPK PYAITNPPND IIDTRSLESW QDLFRERRVW
AHRLSEDCEG MEKEAHDQYE AMDNMLSCLD AAVANLESVV RATENKYEDL KKWAATEQTG
YNDLVTRWEQ NLGLARSIPI SAAMVRLMTG KDVTGAKGRP SKQATLEDLV DLDCARKEGR
RAPTVLRKFN ARIADLEKAE GRLMQNFEEL EAEFRRVISR SVMGHSQDAT QLLQDIQALA
GKVENDYRTT MDYSTSTRDL LQASKIAQTH TEKHLPSLHK RALEMDGMLR YAIKARNALA
LEQAEFMRSI ADVSKLDMQV KSLINAIAED EELATFDYLR LIHQVPYMYA AFTAEAIRRK
EWFDKVKTDS TTLANEMALF QDEEAKRRRK WYKTIGDTSY GPESLSTDNN VPGLEVNLLG
EDELWPSTSR KDLEEFLDLL QRQRADASII GDVGKIIAEL SNPTKQQFKR LKAFKNGSVH
DSALGRSGLM IRGDDELLRS LQDDKTKLET KLRTAESRVR RLEDLLHRQG QASRPTLGNL
FQNPSQQLPE RSGSAQSVGS PGPIGDRRQS DEVGNQLVQR VAQLEKELQE EKERNAALER
DAADRTTHTN DIKAQMDDVN ATKKDLLENM EAQKREFLVE RKALDEEIRN LKARLEETED
EFHNIDESRE HEKTSYDEKV QLLEAQLESL TKEKSDDALK AQGQVDFLRN ETRLQRESNE
ALQAQIQASQ DELGLLNKKL KTTNEAADVQ LRALRELYTT FVKSAGIPED VNDLADTVLN
NAAETLAKVQ NLDADISIMR SNLALAQDVA KDLRAQQANA LEKLAKEETT SMHLREQCDE
HKAKVNALEG ELADGRKQLD ELRTQIAQGE TGSESLRTRL EEEEKKIVRL TEDLASKQSQ
VGSLEEELRL FQERLQDSQS KLTTLTLRTE TRNERTKDIS QRLYSQNERL VRLLERLGFS
VSRENGVMTI QKIPRAERST MNLAASSTAD AKSRIASEPA DVELLYWMNA TDVQGETEKY
DKFMSTLGSF DVDAFADTVY RRVKDVEHIA RKLQRDVRGY REKTHALHKD AHDKIAFRNF
KEGDLALFLP TRNQTNGAWA AFNIGFPHYF LREQEHHRLS NREWLVARIT RVQEKVVDLS
KSLDTTESIN GTSGGAEDDN DNPFDLSDGL RWYLIDAQED KPGAPSTPGL GKTTVASTKV
EAKGDMQTQP RSTPGGLAVL GGAKPSAVDG ASKSLSKSLE SRRSSTSSTR RPLPFAGALS
RNAPGSETNS LRAVATTAPG DGAGSPSGPT SPKPHLAHGE DQDVRLAALP EPQQQRVEVR
NDSGGGAIDS LLGPT
