ATG11_PICGU
ID ATG11_PICGU Reviewed; 1083 AA.
AC A5DPN3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Autophagy-related protein 11;
GN Name=ATG11; ORFNames=PGUG_05234;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Vacuole
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Note=During pexophagy, accumulates in the vacuolar membrane region,
CC where the peroxisomes contact the vacuole. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATG11 family. {ECO:0000305}.
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DR EMBL; CH408161; EDK41136.2; -; Genomic_DNA.
DR RefSeq; XP_001482214.1; XM_001482164.1.
DR AlphaFoldDB; A5DPN3; -.
DR SMR; A5DPN3; -.
DR STRING; 4929.XP_001482214.1; -.
DR EnsemblFungi; EDK41136; EDK41136; PGUG_05234.
DR GeneID; 5124187; -.
DR KEGG; pgu:PGUG_05234; -.
DR VEuPathDB; FungiDB:PGUG_05234; -.
DR eggNOG; ENOG502QVZE; Eukaryota.
DR HOGENOM; CLU_002803_1_0_1; -.
DR InParanoid; A5DPN3; -.
DR OMA; EIDVHYF; -.
DR OrthoDB; 287492at2759; -.
DR Proteomes; UP000001997; 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:InterPro.
DR GO; GO:0000422; P:autophagy of mitochondrion; IEA:InterPro.
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; PTHR13222; 1.
DR Pfam; PF10377; ATG11; 1.
DR Pfam; PF04108; ATG17_like; 1.
PE 3: Inferred from homology;
KW Autophagy; Coiled coil; Membrane; Protein transport; Reference proteome;
KW Transport; Vacuole.
FT CHAIN 1..1083
FT /note="Autophagy-related protein 11"
FT /id="PRO_0000317924"
FT COILED 562..591
FT /evidence="ECO:0000255"
FT COILED 648..812
FT /evidence="ECO:0000255"
FT COILED 953..988
FT /evidence="ECO:0000255"
SQ SEQUENCE 1083 AA; 124171 MW; 2EEC1D25E4D5DC5B CRC64;
MHLTIHNAHN GLTTSIQKPI RYHSYQSFKE YIVESFTNYI LDDANNVFLL TQFGMRVDFN
IINELNDIYF FDKRLFVNEN PASILKDYAT QTMRDIPPPK HPSLAPYSRG LNIRQMSSSL
RSNAGWSMSV KVDAALADEQ VRAYKRQISV MFRCLSIMFE FIASFTSDIE NSFTKFYNHI
NQLSLKTLHE HWKSHYKTLA SRPQFTFKNG KSVRLADMLN YDALVEASQF VERNLSTVID
QFNQLSATIN EVNKSKIDID GEIQVLRDES IAEFASLKAS ESLVEDIKSI GTAISTEIDS
IASSESRVLG DIYTKHVESS KKLDEKYVQL YNDLTKLDQF KDKLAEKGTA LFRHCARLQM
QMVNVKLALN EFDSRKQEGK QRSAMQKVQE IKKKEEYLSL TIDLPLLFGF AIIEMRRQYE
WYDFFASGAV SNVTEQLQVI INQERVFRKI WAKKIGSFLS ILDSLPSDLS QTLPSLDVTV
VKGREDFFGK FWIHDIQRED IDKYIKWVGS IDAGKHANFS MLLERNFEDL IKSTNAMKSV
TKAIGTLSSY TSPENIDAVQ PNDKKEDQDL IQGYKNRIRK LENLLHQQQF KDLSTWPVIK
GATQDQSIIF NPKRNSGVGS DNVLVHSQHD AKILLQNHRS SIKDESSSRT DHLKLAKENE
DLRKRLQELQ IGGERRVEAK VPFEASLSGT KILAQQNTEI LAQKKALEMK VDSQLQVIEK
IQKESSEKDN EIFALKKQIQ DLTGEANEFY ARNEELKKNA EVKYDHLVQE LNEEKDKSSS
LSSELDAMKR GANDRKDAEK AIAELTSVAS DLYGKLVDHS HITFDYVLTL SYILEKMGLM
LTNEEGKNNV FKIRRVKGLR SRKQDGENSQ TDVGSPVPGA IKNMMVWSHT DINVNPADMI
ESAKEIINVC RNKMDETFDK YNQVVAFRSN VSIEQVSEHD IRTIEFFSNA VVKRFKDVEG
LAKKLAKEKK TYETQLQKLT RKMSAKVTLS NFQTNDLVLF LPTRLETKEP QEVIQPWTAF
NIGTPHYFLK SQPSVEREWI VARIVSIVEH TVTATNKNDT SLNPYRLSEG ITWFSVEAKE
VSQ