ID C5DIS4_LACTC Unreviewed; 1082 AA.
AC C5DIS4;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Autophagy-related protein 11 {ECO:0000256|ARBA:ARBA00013804, ECO:0000256|RuleBase:RU367075};
GN OrderedLocusNames=KLTH0E14784g {ECO:0000313|EMBL:CAR23685.1};
OS Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS (Yeast) (Kluyveromyces thermotolerans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR23685.1, ECO:0000313|Proteomes:UP000002036};
RN [1] {ECO:0000313|EMBL:CAR23685.1, ECO:0000313|Proteomes:UP000002036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC {ECO:0000313|Proteomes:UP000002036};
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
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|ARBA:ARBA00004148,
CC ECO:0000256|RuleBase:RU367075}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004148, ECO:0000256|RuleBase:RU367075}.
CC Note=During pexophagy, accumulates in the vacuolar membrane region,
CC where the peroxisomes contact the vacuole.
CC {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; CU928169; CAR23685.1; -; Genomic_DNA.
DR RefSeq; XP_002554122.1; XM_002554076.1.
DR AlphaFoldDB; C5DIS4; -.
DR STRING; 559295.C5DIS4; -.
DR GeneID; 8292292; -.
DR KEGG; lth:KLTH0E14784g; -.
DR eggNOG; ENOG502QVZE; Eukaryota.
DR HOGENOM; CLU_272501_0_0_1; -.
DR InParanoid; C5DIS4; -.
DR OMA; EIDVHYF; -.
DR OrthoDB; 2727468at2759; -.
DR Proteomes; UP000002036; Chromosome E.
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:UP000002036};
KW Transport {ECO:0000256|RuleBase:RU367075};
KW Vacuole {ECO:0000256|ARBA:ARBA00022554, ECO:0000256|RuleBase:RU367075}.
FT DOMAIN 138..473
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT DOMAIN 910..1075
FT /note="Autophagy-related protein 11 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10377"
FT COILED 355..418
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 634..703
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 754..788
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1082 AA; 123970 MW; D13C6707188DA0D7 CRC64;
MAGDNAVIYN AITGACVSAN IRLFLGVEDL QRFTSQQFMI PIDQCFILLP YGVKLKKASF
LNCRRQPERA EFYVFDRRLF SFAQDPSSGE GRVDSQELET LLDSVTRSCN VTLIKPITSP
LLEVANMTNN LDHRKITSLL TTNMGWLSAL EIDAHYFYSM IHSTISEMRN IFQCMTICTQ
YLKLYCYDIE KLHDSNVEFL NQLTKDSSVY RWRRVFEEVL KKLNTVNSEK EERLSDFLSI
EDLESHSNNF LATNKVISSK LQQLKGQINE SLDKRQHISL KLQSLKSQFE EPASNYEMES
HMMERFDEMI YDLKKSTRET LEMGSDEISP ELLVTISQKI LEDKNSVIPK LFTVAQSLYL
QAEELLAKKR QLQEQVMFVL SQTAFVQFHI LGVKRALLKE CNQQLESLQE LELRLSQVED
FPIFYGLRLI EQLRRNNWLG QLEKLERNMR QEFQVISEAE EKYRQKWDET FGQLAHISNM
TNADLVGFKD FPTPNPKRWS SSELASTIVT TEKIEKYLAQ LSQRDISADS ITLLKKNFVN
ANRVSVTSNQ FSSLTSFDWN VSKPAESDVI KGYQIRIRKL EALLHDAKFS NINAWPSGVI
NNTILTAFEN NVPPVNVKMN MLLSGEKEGG CYVQEEAGKE ISRLKRELGN QKEETTLFRE
ESRKMQTQLV DLEDERNAYQ ETLKTLNQEI SKLTLEREQK KLAQDELLIK IKGDIETVNK
LNTSLVNEFD SWKDKCNRLS ELNDDLHSRI AHQEDTFREE KLNLEGDLSD LRKEVASLKT
ANEALVSEQA SLKSSNIVNL SKALNDRMQS KLFEIFSSDV YILENIGLLL SQLDESHFQI
TRVKGLRKGQ VQGELDESTL ESKVSPSIKS NVFQAVKSFY EASVHSGDFE SQKDFLASID
KLFENGLYEA SVIKRFKDIE ALAKKLTKEN KFKRGLLETY QREKITIKNF QVGDMALFLP
TQDVPDSVAS SVSSLTSSFS SVDLSTPPPL GANSSHAVNS HNKGKKIHDG SRPWAAFTAF
DDSTRYLLRD NEKFTLDRDW FVGKITSVER STSSETSSTT YKLPKGTNWV QVTAEFITAK
NF
//
