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Database: UniProt
Entry: A6QRL0_AJECN
LinkDB: A6QRL0_AJECN
Original site: A6QRL0_AJECN 
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}.
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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
//
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