ID A0A0D1XZ80_9PEZI Unreviewed; 1448 AA.
AC A0A0D1XZ80;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Autophagy-related protein 11 {ECO:0000256|RuleBase:RU367075};
GN ORFNames=PV09_01044 {ECO:0000313|EMBL:KIW08106.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW08106.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW08106.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW08106.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-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}.
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DR EMBL; KN847531; KIW08106.1; -; Genomic_DNA.
DR RefSeq; XP_016217975.1; XM_016353880.1.
DR STRING; 253628.A0A0D1XZ80; -.
DR GeneID; 27309017; -.
DR VEuPathDB; FungiDB:PV09_01044; -.
DR InParanoid; A0A0D1XZ80; -.
DR OrthoDB; 2727468at2759; -.
DR Proteomes; UP000053259; 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:UP000053259};
KW Transport {ECO:0000256|RuleBase:RU367075};
KW Vacuole {ECO:0000256|RuleBase:RU367075}.
FT DOMAIN 114..459
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT DOMAIN 1078..1226
FT /note="Autophagy-related protein 11 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10377"
FT REGION 596..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1188..1210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 556..583
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 810..977
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1077..1111
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 625..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1269..1294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1399..1413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1448 AA; 162075 MW; 3B718BE1FB8E6643 CRC64;
MAFTVHVVPT GDSIQLSTGQ PPTTLDALYA WAASETGIRE TDQIILTKKG KHVQQQALLT
EDEFFLYDRG LFTSGPAGRK PIPLDPVPES WVPEDFPTDL QAPDSLKAWQ TLFRQRRQWA
SNILQECKSL CEEAQSYLAK RRAIENGLRV ATSKHETYLQ RLGQQHREVK AWFEEVRKDA
GANIQLLEED LEKMSNVPVK TAFGKFFGRA NLSSGRKNSG TEDTTNLAAF IDRASTEKAA
DEARSALDKC DSVLQELGAR LESITAEYDG LIRDLGNSQT RSLRDDPDEP RKQLQEVQAI
ANKVASDYEH VMGLKNDQSA LRAASKMALL HTKNFLPNLR DCAVEMNELL RYLVEQKNNL
TQRALDHLQT IARVETSIPT LRKAFDSFEI SESGLAALDR VAAASQLPIT YGSLLLEGAR
RKEWADKMKH DSAVLAEEIA GYQEEEQRRR RKWMRGVANM ISDASVEGKV LSVEVNLQGE
DRTWPPVTRA DVEEYIRNLQ AIPGFEAVVE SLTQTLKSMD QPTRQQVKRA KAFKMGSVHE
AGFGKGSLML RGDDEAKVLR EANLKLEEEV KGYKSRIRKL EDLLHRQSMF NRLSIGNASQ
STPFGEHAMT PVDGERAAPL SPRQGDLSRR SSTSSRRVSF NNQNQDEKTL ARRIVQLEAD
LVAAREARAR QEKAHQNALE EANSTKKDLL ENMEAQQREF ATERRSLEEE LTRLKLRVEE
LDDEFDRLTS SRENDRTSAE ARFQVLIAER DEARRDAAEK VKQAERRSRS LERNLRERSE
RDAERMDLLK GLYSVLDTEN PAPEDPAALC AALEELVQRS QDQAREVAQA VALARSENGN
LQAMLDVQKA ETTRLEEKLE EKEHEIKKLR DELHAERSKA ASVSAELESE RGHLKDLREK
FAEGETGSES LRQRLEEEQG KVSDLSTKLA ETRSHINSLD VELLSLQSKY RKLQDLYEAA
EKRLQERSQR AKAVSQRLYS HNDRLMRLLQ ALGFVVTFED NKMKLERASK AGGSTMMADG
STTIQRTVSG STTTRWIEDL ADVSLLLWPE KDVAEEEEAK FAEYMERIGR FNLDTFSEAI
TKRMRDMEHT ARKWQREARN YRDKAHKYQS EAHDKIAFRS FKEGDLALFL PTRNQAMKPW
AAFNIGAPHY FLREQEGHRL VNRDWLVARI SKVEERIVDL SKTLNSPGAV DTRSLTEASD
AGTPYEDDNP FDLSDGLRWY LLDAQEEKIG APSTPGLGKA VVSTSTVSAT RDATTTKTTS
TAAAIRIKRK PTDAVEEASK ALSRSLDSRR SSHSSKKSVP VSTPGLGIST KNTSSNDALS
PDAAAGATPP DAQHRNGPGP SHLRTTSDVA SMLKSDEDEA ATRDTAALQE EHPHPPSSVL
LTKSKPVSSP LKAGSSLDAL RRNTPQGSNL ASPAASPAKP KPSPAKAGVW DSLFQYEISL
QGGGKRKG
//
