ID L8FW76_PSED2 Unreviewed; 1381 AA.
AC L8FW76;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Autophagy-related protein 11 {ECO:0000256|RuleBase:RU367075};
GN ORFNames=GMDG_06952 {ECO:0000313|EMBL:ELR04723.1};
OS Pseudogymnoascus destructans (strain ATCC MYA-4855 / 20631-21) (Bat
OS white-nose syndrome fungus) (Geomyces destructans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=658429 {ECO:0000313|EMBL:ELR04723.1, ECO:0000313|Proteomes:UP000011064};
RN [1] {ECO:0000313|Proteomes:UP000011064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4855 / 20631-21 {ECO:0000313|Proteomes:UP000011064};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C.A., Blehert D.S., Lorch J.M., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Geomyces destructans 20631-21.";
RL Submitted (SEP-2010) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL573358; ELR04723.1; -; Genomic_DNA.
DR RefSeq; XP_012745398.1; XM_012889944.1.
DR STRING; 658429.L8FW76; -.
DR VEuPathDB; FungiDB:GMDG_06952; -.
DR HOGENOM; CLU_002803_1_0_1; -.
DR InParanoid; L8FW76; -.
DR OrthoDB; 2727468at2759; -.
DR Proteomes; UP000011064; 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:UP000011064};
KW Transport {ECO:0000256|RuleBase:RU367075};
KW Vacuole {ECO:0000256|RuleBase:RU367075}.
FT DOMAIN 102..455
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT DOMAIN 1103..1251
FT /note="Autophagy-related protein 11 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10377"
FT REGION 580..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1298..1381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 552..579
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 857..933
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 960..987
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1102..1129
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 582..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1298..1317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1339..1367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1381 AA; 153934 MW; E19A5F1FDF887338 CRC64;
MALQVYIAHT GARLQTEPGA FASLDGFKAW VADKGGVSVQ NQICLTGSGK SARTQSLFTE
HEIFVYNRLI LNVSSSNSAM EQVSQLPMPA TYEIENPPDT IADQNDLGAW KDLFHARREW
ASKVVNDSER ISREAQKRFG EIDVIARSVY AAVVNLGGHV AGLEQKFPQT QKWAQDIVDE
YGIRISELEQ SAKLLRTLPV TTTMFRFISG KNPKGGNHQP SLADLIDIND IQQAGAEASD
VIAALRTNLD DMTRNLKRID SGMDKITKKE KDSVGASAMA KSEEPAGLLA DIKAILNKIG
KDYENLLAYA DTPKSISQAS KTALLHTRSF LPSLSKRCME MSEVLADATN MRNSAAVEAV
ETMQGIATLN TLCTEMNRRT DGLEISDDGQ KSLELILLVA RLPIVYASFV AEAICRREWS
DKMKSDSSTL GNEMASFQDE EGRRRKKWQK NTGFYFWAEK PERKVLGLEV NLLGEEDQLP
LVSRQDLEDL INKLNSANVH PDIIAEVSQI VTDLSTPTKQ QARRAKAFKN GSFHEASMGR
STLLVRGNDD IIRTLQSEKA KTETKLKGAE SRVRKLESLL HQQSHASRTS SANIFPLPSD
EHDPGNMASS PQFRDEIYRP SSVSSRRYSA NKTQDDRAAT QRYIHLEADL IAERERAAGL
EKEAAAKSAM LTHLRTQFEE ATSTKHDLMQ NLEAQLREFG TERKSLEDDN RRLKSQLEDY
EDSIDRSREN ERLTLDEQLH TLRTELNKVQ ADAEAESQKA QGQVDFLRGD AQLQRESNDS
LQKQLNKARE ENKELKDRLD SAEDGRREAT ASLRGVHSVL FPASDEQAQA QSTVLAENLL
SRIKDLITHA GVHERDLALA HADRDEAQEK LSEVKKELAD IKDKLSSDES ESVRLQEEIV
GERAKYAALE SNMAEHQQEL TSLRTKFAEG ETEVLRSRIK EEEQKVTSLI AKLTSSKTQV
GSLQEQLKSV EGRLQESQAK LEKVNGRFEG RTMRTKDLTQ RLYAQNDRIW RLLDRLSYSV
TREADSMTIT RIPRQERANL TDSSDPSSAM RRSISGQAKK PMIDSGDLEL LYWMNNDDSE
VEGEKYEAYL SAMGSLDIEV FCDTILKRIK ETEHQARKAT RDARTYRDKS HAAQKEAHEK
IAYRHFKDGD LALFLPTRNQ ANGAWAAFNV GAPHYFLREQ DTHKLRSRDW LLARIQRVES
RVVDLSKSMT GQLSTAGDNG SFGDVSVDDS FEDDNPFDLS DGLRWYLIDA VEEKPGAPPL
TLSLGKSTVA AANVDATGSI RHSKKISGSA VDNISKTLSR SLDSRRSSNN SRKAAPFAST
PVKQPDSAAA VEGEDSLHPS SATEITPRPN HPPQLQAGGS SGLEVRDSDT TPAVLDRPLG
P
//
