ID A1CKQ9_ASPCL Unreviewed; 1263 AA.
AC A1CKQ9;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Autophagy-related protein 11 {ECO:0000256|RuleBase:RU367075};
GN ORFNames=ACLA_039480 {ECO:0000313|EMBL:EAW09733.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW09733.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW09733.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027056; EAW09733.1; -; Genomic_DNA.
DR RefSeq; XP_001271159.1; XM_001271158.1.
DR AlphaFoldDB; A1CKQ9; -.
DR STRING; 344612.A1CKQ9; -.
DR EnsemblFungi; EAW09733; EAW09733; ACLA_039480.
DR GeneID; 4703492; -.
DR KEGG; act:ACLA_039480; -.
DR VEuPathDB; FungiDB:ACLA_039480; -.
DR eggNOG; ENOG502QUQE; Eukaryota.
DR HOGENOM; CLU_002803_1_0_1; -.
DR OMA; GLRWYLI; -.
DR OrthoDB; 2727468at2759; -.
DR Proteomes; UP000006701; 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.
DR SUPFAM; SSF57997; Tropomyosin; 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:UP000006701};
KW Transport {ECO:0000256|RuleBase:RU367075};
KW Vacuole {ECO:0000256|RuleBase:RU367075}.
FT DOMAIN 52..399
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT DOMAIN 1012..1158
FT /note="Autophagy-related protein 11 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10377"
FT REGION 520..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 490..517
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 574..725
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 768..893
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 522..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1263 AA; 142932 MW; 9A771D8A54049515 CRC64;
MTARGKNVRI QTLATEDEIF VYDRRYVSEP DNVELVELPS PESFTPDNPP DTLANQNDLQ
SWRNLYMARR SWALTLSEQC EEMDKKIHEH NERTDIINRA AGVALENLKT HVGNLEHRLQ
EAQAWANDLL KEQKAALDGW QRALSTLESI PVLTDFPFLG RPSTPTKHKD RSSGTLRDFV
DIEEVHKAGA GASTESSRFA RQIEDVSEAV GGIAADTQQL IENAIPSSPA VIDGLQEVIT
IAKKISSDYE HVLALPNNQK TLANISRLAL THTQDLLPSI LDISAEIHAG LEEAIRRYNG
AMKEALEHMR TISAIELRLA DVQSQIINLN VQSDAFDIVF SVYHMPMVYG SVLVESVRRR
EFNEKMKADS LTLAEEMAVF RDEEQRRRKR WLKSMGDFIS ITDATTPGVE INLQGMDYQW
PEVTRKDIES YINELKARPN LAGLADELTQ QYKELDAPTR HQRRRAKAFK QGSIFDLSRS
SLLLRSDDML RSLRDEKSKI EEKLKGSESR IRKLEDLLHR QSQMSRPVSG NFSLEFPSSP
ASPHPDPLSR RSSVSSRRMS ANQSSEERAQ AQRIVTLEAE LAAERETVQR LQKDAHAERL
SNTDKIQEAQ STKKDLIGNL EARQREFDEE RRYLEGELKK YRLRTEELEE ELDRMTGSRD
HEKQDADERI NQLENELQNI HAHAEEEMHR ANSLFEEVQR QKKAEEDFQL RINELEKQQS
ESRAKEQENL LSLQAAFMSL SPGGAVPAEI PSIIKAIEVL SEGLSIHAKN AEENMAEAVA
ENRTLEERVN QIESELDQTK KILNERTSEL SRMREDLAQE KEKLSAVQSE LQEERTQLST
LQSQHTTGDA GADALRERVV EEEQKLARLS QRLNEVEAQA RQSEHEVSAW KDKVDAISEA
EQHATARIEI RGARSKELSR QLFGQVEKME HMLEQLGFTV IRQDGEIVVQ RASKVNAASG
IGDTLSQSAV VSVKPDPSLL DWMEADSAEE ETDRYMAFLE SLYQFDVEVF GDTVVKRVKD
IELLARKWQK EARGYRDKYH RTQSEAHEKI AYRTFKEGDL ALFLPTRNQA IRSWAAFNVG
APHYFLREQD AHKLQTRDWL LARITKIEER VVDLSKSLNG ANPDRQSLGG TSDATSFDDE
NPFELSDGLR WYLLDAAEEK PGAPATPGLG KSTVAPAHVD ARGSIRLKRS TNGGNVAKTL
TRSLDSRRNS SSSKKGPLGT PQRANESTTE LTRPPESGTP GSQQAREAAS TPEEVRRDQL
QGP
//
