ID A6QRL0_AJECN Unreviewed; 1305 AA.
AC A6QRL0;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Autophagy-related protein 11 {ECO:0000256|RuleBase:RU367075};
GN ORFNames=HCAG_00016 {ECO:0000313|EMBL:EDN02152.1};
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN02152.1, ECO:0000313|Proteomes:UP000009297};
RN [1] {ECO:0000313|Proteomes:UP000009297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(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|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; CH476655; EDN02152.1; -; Genomic_DNA.
DR STRING; 339724.A6QRL0; -.
DR VEuPathDB; FungiDB:HCAG_00016; -.
DR HOGENOM; CLU_002803_1_0_1; -.
DR OMA; GLRWYLI; -.
DR OrthoDB; 2727468at2759; -.
DR Proteomes; UP000009297; 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.
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:UP000009297};
KW Transport {ECO:0000256|RuleBase:RU367075};
KW Vacuole {ECO:0000256|RuleBase:RU367075}.
FT DOMAIN 96..444
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT DOMAIN 1051..1196
FT /note="Autophagy-related protein 11 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10377"
FT REGION 580..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1220..1305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 529..570
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 620..768
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 818..943
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 592..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1224..1267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1287..1305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1305 AA; 146928 MW; C7CA4515F8538C1E CRC64;
MSLHIYIAHT GEQLLADPVS FASPDALRTW ISRKISMPAQ RQILMTASGR NVRPQTLATE
NEIFVYDRLY ISDGTVRDLP VITPPERFTP ETPADTLADQ NNLQAWRNLY MARRAWALNL
AAQCAPISRA IDDQIEHTHN INRAVDVALE NLKSHVGNLE HKFQEAQSWA NDLLKEQQLA
LDGWRSALTN IETIPAKKDF TFLRRPSTPK RATEPQTGTL KDYIDVDRIK SAASQVSSVS
QRFARRMDEV EKAVHEVVSD TESLVEASHP SPQENASGYM EEIETIAKKI GSDYEHVLAL
PNSQKTLASV SRMALNHTKD LLPSMLEMCL EIQTTLELSI KQRNLATKAA VKRMQKISNI
ESRLAGVQTE LTNLDVEGDA FETLYEASQL PMIYGSILIE AVRRREWNDK MKTDSLSIAE
ELAVFRNEEQ RRRKKWIKNM GNFLSFSEDT IPSIEINLQS GQLPGWPEVS RKDVDAYIEE
LKTKPDTNSA VRDLTQLLKD LDAPTRQQRR KAKAFKHGSV FDIGQSSFLN RGDDMVRNLK
DEKMKLEDRL KASESRIRKL EDLLHRQSQM SRPVSANFGF DIPISPASPR PDGLSRRSSV
SSRRMSSNQT PEDKALVQRI VGLEAELLAE KENVSRLQKE AHLERLSNND KIQEAQSTKK
DLMDNLEAQQ REFEGERRFL ESEVKSIKIK LEEAEEELDK VMDAREHDKL VADERAAALQ
TELETLRNAT TEEIADFTSE VQALRENSDK AKAHNTTLQE RLEEMARNQR DYVIGLQTAH
AHLSPGGSAP EDLTSLIRAI EVLSEGLAIH SKGVEEASAK SNEENKCLLE RIEQMEAESK
ELRARLAAEE SERSKLQATL NEEALRLSAV RTELEDEREQ LNILRSKFSA GETGSEALKE
RVAEEERKVA ALREKLVVAE SHAQGFEDEI RTWQMKVKTL EENGERNTKA IWAKELSEKL
FSHVGQFSRV LQQLGFTIIR QDNKMVIYRA SKVNNSSSLL GESVSSPSAT PMTHDPKLVE
WVNTNNREEE QSNYTAFITA INEFDVELFG EAVVKRVKDI ETLARKWQKE ARGYREKSHR
FQSESHEKIA YRSFKEGDLA LFLPTRNQAI RSWAAFNVGA PHYFLREQEV HKLHTRDWLL
ARISKIEEKV VDLSKSMNGA NPDRRSIGEA SDGASIDDDN PFELSDGLRW YLLDASEEKP
GAPSTPGLAK STVASAHVDA TGSIRLKRST NGGGATKTLT KSLDSRRNSS TSKIGTPVPT
LQSAESAGDN VLPAAGDAGG QQRRAEAPIF DEVRRDLLSG PSKGE
//