ID H6BPN7_EXODN Unreviewed; 1454 AA.
AC H6BPN7;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Autophagy-related protein 11 {ECO:0000256|RuleBase:RU367075};
GN ORFNames=HMPREF1120_01827 {ECO:0000313|EMBL:EHY53639.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY53639.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY53639.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY53639.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) 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; JH226131; EHY53639.1; -; Genomic_DNA.
DR RefSeq; XP_009154100.1; XM_009155852.1.
DR STRING; 858893.H6BPN7; -.
DR GeneID; 20306466; -.
DR VEuPathDB; FungiDB:HMPREF1120_01827; -.
DR eggNOG; ENOG502QVZE; Eukaryota.
DR HOGENOM; CLU_002803_1_0_1; -.
DR InParanoid; H6BPN7; -.
DR OMA; GLRWYLI; -.
DR OrthoDB; 2727468at2759; -.
DR Proteomes; UP000007304; 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 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:UP000007304};
KW Transport {ECO:0000256|RuleBase:RU367075};
KW Vacuole {ECO:0000256|RuleBase:RU367075}.
FT DOMAIN 131..482
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT DOMAIN 1127..1275
FT /note="Autophagy-related protein 11 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10377"
FT REGION 544..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 991..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1234..1258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1303..1439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 270..304
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 570..597
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 653..825
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 875..944
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1125..1152
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 554..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1234..1249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1342..1359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1390..1406
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1454 AA; 162633 MW; 320A880243282784 CRC64;
MGQIISLPVA GNDVSISRQF DNQHALIQNY HAVRGARVMA LKVYISHTGQ SLTYTNADPN
TRVETLRTWI ESTAGIPTGR QILMTSRGKN VKNLSNEVEV YVYDKQVLSS DAQPPTRNDL
ELSRLSAPPS SLADENSLKA WQDLFMSRRA WALEAFEIAR TGVENIELCA DEAIIIARSK
QVALDNLRTH VTSLQQRFEE TRQWAENYIQ DHRDVLENWK ARVGALGELP VREDVAKVLR
RQVEQESDRI AAPIGTLLDL VDQDALHVAA ESVQQSSAEF EGKLQKLQAA MDKLKIDTNE
VGRRSTAIPE IDTNALLDEA ETLAKRITLD YEDVLQMQDN PKSVAAVSRK AAVHTRELLP
ALEAVVEEII HASKSASEVR NTVSNEWYSA LRNISSLQSR LAEAQSATSN LDFHDDENFQ
LLSRIFHLPL VYGATLIEAT RRSEWTERMR AEIDVLHEDL SVQTEEEQRR RKKWTAAHND
YLDQDLNAKD ALVDLKASAP RNSWPFVIRD EIFAWVDDLT ALRIDDAVEA LSQRLKDLDA
PIRKQKPKPF KNGSIHDLSQ STALRSGTDV KNLQDEKSRL EEKLRASDSR VRKLEDLLHR
QSQMSRPPSG IFVPGGAAEF ERQTPSPGPV ARQSDLSRRS SVSLRRLSNT QDEKSLVQKI
VALEGQVHKL QEEALAERRS STESRDKMHE AELVKRDLMA NFEAQKQEFE EERQLLDDEV
HRLKVKLDEA EDELDRLNES RDHLRTEQDQ AIANLREELE QVKRTAAEDV AKSERKLENA
QKETNIQREK VANLERQLHQ VRDERAAAQA QNMTLAKQLR IMEDQQQEYI TVLQGAHSNL
SPAGSPPDNL QRLVNALEIL SEGAAIHTRG LDDSLQLALA ENKALEEKVL QTESQVKALV
AQLSMAETQS AELRESLDQE RSKMSGLRTE LASERAEIHS LREKFAAGET GSDALRQQLQ
SEAQKVVELL DLKAEDEAKI QHLKHEIEEL RRESSTAAEK QDTLKRHLDS RGEKAKQLSE
RLFHHHDRIV RMLEQFGYMV SKQDDTLIIL RASKVNASAI LSGGEGSGAS TMKRTISGSA
PVQHYSDPSD LETLYWMSDN DLDSESSKYT SFLGALQRLD VDSTIDLVTK RYKDVESLAK
KYQKESRAYR ERTHRSQAEA HDKIAYRSFK EGDLALFLPT RNQATRPWAA FNVGAPHYFL
REQDAHKLQA RDWLLARITK IEERVVDLSR SLSTGMQGNA STSASVDDGG SMRSVEDENP
FELSDGLRWY MIDATEEKLG APGTPSVGKS TVTASNVEVK GHMGTGRKEH KSGMSIGGGM
GGASATTNMV TKTLTKSLDS RRSSSGSKKS VDLKGKHDTI GASRGGSNVK DMTSKAPLAP
IKSDTDAEQA QPECDEAGAD ADAETERDEG EAARPDNQAG PVASMVRQPT AASATDREDA
QVFEVVRRDL LLGP
//
