ID A0A2S5B4T9_9BASI Unreviewed; 1401 AA.
AC A0A2S5B4T9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Autophagy-related protein 11 {ECO:0000256|RuleBase:RU367075};
GN ORFNames=BMF94_5116 {ECO:0000313|EMBL:POY71755.1};
OS Rhodotorula taiwanensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=741276 {ECO:0000313|EMBL:POY71755.1, ECO:0000313|Proteomes:UP000237144};
RN [1] {ECO:0000313|EMBL:POY71755.1, ECO:0000313|Proteomes:UP000237144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD1149 {ECO:0000313|EMBL:POY71755.1,
RC ECO:0000313|Proteomes:UP000237144};
RX PubMed=29375494;
RA Tkavc R., Matrosova V.Y., Grichenko O.E., Gostincar C., Volpe R.P.,
RA Klimenkova P., Gaidamakova E.K., Zhou C.E., Stewart B.J., Lyman M.G.,
RA Malfatti S.A., Rubinfeld B., Courtot M., Singh J., Dalgard C.L.,
RA Hamilton T., Frey K.G., Gunde-Cimerman N., Dugan L., Daly M.J.;
RT "Prospects for Fungal Bioremediation of Acidic Radioactive Waste Sites:
RT Characterization and Genome Sequence of Rhodotorula taiwanensis MD1149.";
RL Front. Microbiol. 8:2528-2528(2018).
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:POY71755.1}.
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DR EMBL; PJQD01000072; POY71755.1; -; Genomic_DNA.
DR STRING; 741276.A0A2S5B4T9; -.
DR OrthoDB; 2727468at2759; -.
DR Proteomes; UP000237144; 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};
KW Membrane {ECO:0000256|RuleBase:RU367075};
KW Protein transport {ECO:0000256|RuleBase:RU367075};
KW Reference proteome {ECO:0000313|Proteomes:UP000237144};
KW Transport {ECO:0000256|RuleBase:RU367075};
KW Vacuole {ECO:0000256|RuleBase:RU367075}.
FT DOMAIN 182..504
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT DOMAIN 882..1007
FT /note="Autophagy-related protein 11 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10377"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1194..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1287..1306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1325..1401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1035
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1236..1277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1340..1385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1401 AA; 150696 MW; C7DA836A9C75EE55 CRC64;
MAAWAHYSLE GSSPEPVEAP RPSLFVVRSS DGAEFPLHRD DFRNITTLDE LRYNLLSPLL
SIPPEFLILM NEEGAPIARD DAVQHLLLLA STPSSSLQLQ EAAGSSGDPS PDGSVVLRNS
GSGSSGPAKA PRQRSSVKRI FVFDRDHLDS DPDEVADALA VTEDLVLGEP PLNPQDPLPS
HLSLSQHNLA TLHALVDSIH LQIASLALAL ANLRRVNTNT VNSFVQFFDS AQPSLERYER
LLGGWEGAME AVGKVAVISG LLTRSGAGAG TAASSVGGAP TPHDKQRYLG DYVSREKMLA
VRDGCAKVLA ELKIRSEGLQ ATLDAVTSAT DAVQSELDIT SSDLSDLEAC THDAEQGHLR
IVELVQAGSE MTDPELLDEC FGELSHADAE HRDRIRFLIE RKNAMTRYFL LEMQKISALQ
SDIASVPSEL AALDRDITTR TDNFKHLARL EGLIPAYVAT VAEVVRRREY ARLLSEQSDD
LSSSFRPLAE FERSRRSHYR QTHSGKLPWE VRGLAGSANE RVPEMALEIL DKDEGLPEVG
PDALDQLEEH IRHLEASNEH LSRELQAERS SWEERAAKLE TRASTAEDAL ARAEQEAAAA
RDKLYRLDHS RADAESARRE AEDRASGESK KREVAERDLA SATAAEAELR KQWSALNDSH
ALMQSEYAAL RAEHEQRQTA ISEHEANLKA IQQAQQVLTV ALAEKDKLLR DHRADAELDR
AVLEKEADEL RRLLVERDDA VEQATSATRQ LRDDLTSLRD KSAAVERESL NTAVQASTVE
SALNDARRAA AEAKQERSRL RAIAYEALRE LASFWQHNAL VSSDVSGLTV LKTDLSPTTP
PAYTPAAATI PAGPDAQGLD TEALSTLLTD LSAYDHEAFH RAVLEKAEGL AGGVKKWIKE
AKAYRERAHR ATAASVDKIA FRNFTKGDLA LFLPTRNSAV PVWAAFNVSF PHHFLSASGV
IAEQMRTREW IVARVTEMTE KVVDPKDPST NPYLLPAGTK YFMLEVEPWS SKESSRRRRI
STDKTSGDRR TSSKGTRLEG PTIAAPSTGS AEGSADATPP PGSRAVASSP PTFRRTVSEG
SPLPPNAIEF GRSDFSIPEA EEDEPRGMSR TPSPSLDAAH AAKSEGVRPI VRPSELSKAI
ALSTPSTPAL DDPFAASVRS PFGTPDVAAY SSSPHAPTIL TDFRHGETSS EALPAFLPAS
SARRPSRASA DGSVLSVARG PRYAGPAERS RHATSIARAG SVSNPATALL SSSPASTSAS
SIHVVSQPRS VSSASGILSA SIHRRGSSSA LGAGTPASSV KAAPTQAAQL VGSGWRAISQ
NVIDESSTLR ADPKVSKGWP SASSPGNGQA SSFSPPTTVA SKKSTSSILD ALRGNKGTSS
RGAESASAEG EMRKLLGQPP F
//
