ID U4LJ69_PYROM Unreviewed; 1291 AA.
AC U4LJ69;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Autophagy-related protein 11 {ECO:0000256|RuleBase:RU367075};
GN ORFNames=PCON_04149 {ECO:0000313|EMBL:CCX17165.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX17165.1};
RN [1] {ECO:0000313|EMBL:CCX17165.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX17165.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX17165.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(2013).
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}.
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DR EMBL; HF936599; CCX17165.1; -; Genomic_DNA.
DR STRING; 1076935.U4LJ69; -.
DR eggNOG; ENOG502QUQE; Eukaryota.
DR OMA; GLRWYLI; -.
DR OrthoDB; 2727468at2759; -.
DR Proteomes; UP000018144; 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.
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 Transport {ECO:0000256|RuleBase:RU367075};
KW Vacuole {ECO:0000256|RuleBase:RU367075}.
FT DOMAIN 113..443
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT DOMAIN 1027..1179
FT /note="Autophagy-related protein 11 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10377"
FT REGION 586..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1135..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1208..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 547..574
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 641..817
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 852..893
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 605..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1291 AA; 144391 MW; E4BA407F0CFEE709 CRC64;
MSLSIYTAHN GGVLKADGNS FTTLEELKEW IERQIRLSRE CQILMTPLGG KAMLKSLSQE
VRELFLYNRE QITASAKPLL EPIPKEPHIT PFPDDLDNET DMASWRRLFT KRKQWAEDVQ
QRLVGLVDKI REVDSQTAIM QRAVVVAFTN LDNHTNTLKD RWAAVQQVTG NLIDDRHGWL
KGWETAVKQL LRIPVHEEFK KCGSNEKVNR KITVLADFFD IKEVQIAATT AEILMPRLLN
DMEMMKSSVR DIAARTAALK NSIDNQDTRI DVEGELGGLL QEVDILLGKI QTDHDYVRNL
QGPKAAAMAS KRAYAATAEY LPGLKSAAID IGKLYVAVCE RKNAASVTCQ EHLTNLAFIQ
VMFGPVNTVI NKVEKDTEGR EDANFELLHL VILLPISYGS LLIECVRRRE WSEKFNTNSS
KMAEDLSVLK EDEERRRKNW RKHTAMLLPF DVDNNSQTSR AEVSIRGDPT GGLPKISRQD
VEAYIAVLQQ VGGLDSAIKT ITQHYEDMDK PSKRVNKRLQ KAFKMGSIHE AGMMESSIMI
PRNDDEVKSL KADKEQLHER IRGYESRIRK LEDLLHRNRT AAAISGNYPA SMATSPPPGR
PSTPSAFSSS PSKPTMQAPS IPHRRSSSEA QNSETHYKAK SLALEAELRI MQEKMERLQA
QVSGNNESEK VMNARITQTE QTKRDLIENL QSTVKSNNEE RKQLTMEITM LKEKLEQAED
ELEKLEEERI KPLESEQDLM KTELSILRNQ HNAEVEEKTE LQQKLLIMEK EKDEEIARLR
AELQMQTSKA EQGFRRTSEA EAANNELSKQ LHEAKSALDS RTNIHTSMLD TMKAALGYLT
PDPAPEDMHV LMDQLEALVS KATARNKHLN ALLNTSKSLV ESLNKEKDFL QKRFDSRTMK
AKDLTQRLYT HNVRSIQLLE SLGFKIVRND GNMQIVKVSR SSSKTAAAGG VGESTDLSLT
LNAVPSSPED AARARKSPLS QDPETSSPAD DLALLYWMES PDSDIESEKY SLFLGTIGSF
DLDAFSDSII SRVKKTDHDF RSALKQARTY REKYYRARDE ASEKIAFKSF KTGDLALFLP
TRNQVTRPWA AFNVGAPHFF LREQDTHKLG ARDWLLARIT RVEEKVVDLS KRSTNSGLIT
NPASEAGSAK SVTGDEKEVD EDNPFELSDG LRWFMLDAVE EKAGAPTTPG LSSSTVAAAN
VDARGSIKKQ KPVTGAKKKL SEVAGEASRR SSTGSRGSFE VGSILPAGGV AQTHAAEGEI
QPPRTPVEKI AAGIRSRAGS IRSVSSFTGR A
//
