ID A0A0J0XPY9_9TREE Unreviewed; 1356 AA.
AC A0A0J0XPY9;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Autophagy-related protein 11 {ECO:0000256|RuleBase:RU367075};
GN ORFNames=CC85DRAFT_284896 {ECO:0000313|EMBL:KLT43142.1};
OS Cutaneotrichosporon oleaginosum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT43142.1, ECO:0000313|Proteomes:UP000053611};
RN [1] {ECO:0000313|EMBL:KLT43142.1, ECO:0000313|Proteomes:UP000053611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBC0246 {ECO:0000313|EMBL:KLT43142.1,
RC ECO:0000313|Proteomes:UP000053611};
RG DOE Joint Genome Institute;
RA Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT T. oleaginosus allow insights into substrate utilization and the diverse
RT evolutionary trajectories of mating systems in fungi.";
RL Submitted (MAR-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; KQ087198; KLT43142.1; -; Genomic_DNA.
DR RefSeq; XP_018279633.1; XM_018422908.1.
DR STRING; 879819.A0A0J0XPY9; -.
DR GeneID; 28983511; -.
DR OrthoDB; 2727468at2759; -.
DR Proteomes; UP000053611; 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 Reference proteome {ECO:0000313|Proteomes:UP000053611};
KW Transport {ECO:0000256|RuleBase:RU367075};
KW Vacuole {ECO:0000256|RuleBase:RU367075}.
FT DOMAIN 137..417
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT DOMAIN 893..998
FT /note="Autophagy-related protein 11 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10377"
FT REGION 1007..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1236..1356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 520..621
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 671..705
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 736..781
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1010..1053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1075
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1178
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1356 AA; 148528 MW; 866B855248289692 CRC64;
MDVYLASDGG FVQIPHALSD YDSLEGVIAD VSAATGLISG NVLLFTEDGR ELKQEVLEEL
WERGGHGGGS SPQREVVYLF NRETFFSDPE RWANELREEV VYPPVLEASG QLGVSQAQAP
FAVAYDHLCH LQSLFKAQAH ALRIAYANLA YHLDPIVQAF REFSSRAEDQ LYNQEKLLAG
YHVDMAMLPK VIVHEAVYRR RDKDSVEKRK ALVDWIHTKK MEEVRNHCQV AHTDWVNRYN
TVLGEMDELA IQSDADRQQA EHRILGVEHE FTAALERVDL AIQQVEALLR SGDVEADNSL
RDLDQAMRED LAGMTAVKND FTLDLHVHLR GIANYQVRMT KLTRPMTELD LDLRQKNAFP
HLERLHNMPF AYAANIIEIV HRKNFASTLT EWASRLSRTL NTVLAEEARR RQQHKSDNLL
PWEIAALEES QVARVDVSFP STDILSATGL SRKDIDALLA SLEHIRSDAE FQNLQDTENP
IPPLLEQIKV LMTSLESSTL TTTAQLDQAA ASSAAAPNEL QELRDENAAY KDRLAEMEKH
IRDMEERHER KVNMLQNRQG EMQEEQVRLR TDLSEEVQAR QHIATELDDK SRECEELALA
LEEQKELVAA LKVDSQQEKD RINDLGVRLQ EALLDVDGLR SAEQTLIFQI REMQEERTRI
ITDLGEAQLL ATNYESELAG TRAELEATSN QLTEAQRERD LALKNQSAEA ERMMRDHIAE
ADGDRAVLEH QNLTLTKELE TVRASLTEKL NAAKNAHVRR EDGLKAELSF TKAQLREVQR
RETVLSDELA MAKDASASAE KKGTHNSEIA RDAVILAGKY HEACQRLMLA ISSSTTISGS
LSLPSRPKPA VPLRSGSPTS SIDMNNSSVL TRCLESASGF ELDAFADAVL RTINLARKLS
KSCKTYRELS RSKITISNFG KGDLVLFLPT RNAAVNAWAA FNISAPHHFL KVTEPIRQQL
VGKDYYLARI TATDEAVVNG DSPETNPYGL AEGLRYYSHY VEEWQPGQPR LSRRSMSSSA
PATQKPSQPK RQVSQPVPRQ RSLSPSKEES ASPSAGPSPP PRISQTQPSP TAPLSPQPQS
AGHSAIHSAV HSPLASSPAP QDSSPQDQSS AGDSPRRSLD VRSPPPREST PRRSLDARSP
PPPVETSPLR SLEARSPPAP SRRAMVSPPP PPSSPTTPFS PSAAFVRRSH RASLTSNASP
PARDFAASLV RPSSVASSIG SGARAGTLPI PIAAAKGAPA APVATSMEGS PSPSSFGDHG
PGGVGALVPA SRRLSTKGSA ASLRGAAASA SPKSAGPKGK AEDPFRPSPL GNSDAPTPTS
AGGFLSGLSM SRKRNMSSGG GATALDILNK YKGPTA
//
