ID   ATG11_ACRCH             Reviewed;        1423 AA.
AC   A0A286M9N3;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2017, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=Autophagy-related protein 11 {ECO:0000303|PubMed:28830792};
GN   Name=ATG11 {ECO:0000303|PubMed:28830792}; ORFNames=FG00382;
OS   Acremonium chrysogenum (Cephalosporium acremonium).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreales incertae sedis; Acremonium.
OX   NCBI_TaxID=5044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=28830792; DOI=10.1016/j.fgb.2017.08.006;
RA   Liu J., Hao T., Hu P., Pan Y., Jiang X., Liu G.;
RT   "Functional analysis of the selective autophagy related gene Acatg11 in
RT   Acremonium chrysogenum.";
RL   Fungal Genet. Biol. 107:67-76(2017).
CC   -!- FUNCTION: Involved in cytoplasm to vacuole transport (Cvt), pexophagy,
CC       mitophagy and nucleophagy (PubMed:28830792). Recruits mitochondria for
CC       their selective degradation via autophagy (mitophagy) during
CC       starvation, through its interaction with ATG32 (By similarity). Works
CC       as scaffold proteins that recruit ATG proteins to the pre-autophagosome
CC       (PAS), the site of vesicle/autophagosome formation (By similarity).
CC       Required for ATG9 anterograde transport from the mitochondria to the
CC       PAS (By similarity). Recruits also the ATG19-prAPE1 complex to the PAS
CC       (By similarity). Required for the Cvt vesicles completion
CC       (PubMed:28830792). Plays a role in morphological differentiation and
CC       cephalosporin production (PubMed:28830792).
CC       {ECO:0000250|UniProtKB:Q12527, ECO:0000269|PubMed:28830792}.
CC   -!- SUBUNIT: Homodimer and potential homooligomers (By similarity).
CC       Interacts with ATG1 kinase and the ATG19 and ATG34 cargo protein
CC       transporters (By similarity). Interacts with ATG9, ATG17 and ATG20 (By
CC       similarity). {ECO:0000250|UniProtKB:Q12527}.
CC   -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC       {ECO:0000250|UniProtKB:Q12527}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q12527}. Vacuole membrane
CC       {ECO:0000250|UniProtKB:Q12527}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q12527}. Note=During pexophagy, accumulates in
CC       the vacuolar membrane region, where the peroxisomes contact the vacuole
CC       (By similarity). {ECO:0000250|UniProtKB:Q12527}.
CC   -!- DISRUPTION PHENOTYPE: Impairs the cytoplasm to vacuole transport (Cvt)
CC       pathway, pexophagy, mitophagy and non-selective autophagy
CC       (PubMed:28830792). Enhances conidiation and significantly reduces
CC       cephalosporin production (PubMed:28830792).
CC       {ECO:0000269|PubMed:28830792}.
CC   -!- SIMILARITY: Belongs to the ATG11 family. {ECO:0000305}.
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DR   EMBL; MF374633; ASV72107.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A286M9N3; -.
DR   SMR; A0A286M9N3; -.
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   InterPro; IPR011628; Cleaved_adhesin.
DR   PANTHER; PTHR13222; PTHR13222; 1.
DR   Pfam; PF10377; ATG11; 1.
DR   Pfam; PF04108; ATG17_like; 1.
DR   Pfam; PF07675; Cleaved_Adhesin; 1.
PE   3: Inferred from homology;
KW   Autophagy; Coiled coil; Membrane; Protein transport; Transport; Vacuole.
FT   CHAIN           1..1423
FT                   /note="Autophagy-related protein 11"
FT                   /id="PRO_0000443902"
FT   REGION          583..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1028..1048
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1327..1423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          551..589
FT                   /evidence="ECO:0000255"
FT   COILED          625..978
FT                   /evidence="ECO:0000255"
FT   COILED          1102..1130
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        587..631
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..660
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1423 AA;  159908 MW;  EABECE4BA4883832 CRC64;
     MATQVLIAHT GQRLEVDTAQ FSHLDDFKAW VGRNTPVAPK HFVALTPQGR TVKHASLYAE
     ACCPSQKEIY IYDIRMSQAP SSDGSPSVVS QVPPPKRYSI PNAPNSIENV QAIASWQELY
     KQRRAWAVHL LEDCSAMDAT ARARFEEMDV MIKCVDAAVA NLELSIKQIE PKYTELKKWV
     EPALEEHARL STSWQQYLAL ARNTPVSPSM VKFMTRGQAS KSNATLEDLI EPDTAKKAGT
     LAPTAHRRFN DKATELDRAA KKMYQTLDAL IADFDKLMSR SVLGRSDEST QLLQDIEAVV
     KQIDSDYRTA LSYSGSQKDV AQASKTASNH TERLVPNLKK RAKEMDDLLQ YVTTSRNTVA
     SDAVEFMRAI TEITSLRGKL KDNIGILNQS EDDMTTFDYL RLIQQLPYMY ASFLVEAIRR
     QEWNEKIKAD SSTLANEMAL FQDEEAKRRR RWQKMVGSTY GPGLDTNVIG LEVSVLGDDN
     SWPSVNKDEL VAFLAALKDQ ETEEAILEDV GRLIQELNSP TKQQSKRLKA FKNGSVHEAA
     LGRSGLMIRG DDELLRSLQD DKSKLESKLK TAESRVRRLE DLLHRQSQAS RPGNLFQPQT
     NSIHERNDSA SSVKAAPTDR QRASSEGTDT LLRRISELEN ELREEKQRSS RIQNDLSNRA
     TQHDDMKNQI REVNSTKKDL LENMEALKRE FVLERKSLED EIKTLKARLE DTEDEMEHFG
     ESREKERTSY EERAQQLEAE LERIDKERRD EMLKAQGQVD FLRNENRIQR EQRDTLEREL
     QNTKDAGHAT SKRLEALQEA ADAHLQSLKE LHSQLTGNDP VPDDGDLADV IQTKAADLLA
     RLQNMESDTS LIRGDLDRTR DQVKELREEL ASTKDKLATE EAASIHVREC VSEEKAKVKA
     LEHELAETRE QLSRARARLA DGETGSETLQ KRVEEEEKKV ASLSEELASR QSQVGSLEEE
     LHLYKEKQEA ACARASELTQ RHETRDERSK ELTQRLYSQN DRLCHLLERL GYAVSRKEGT
     MTITKVPRAE RAAQNPNDSS DPGTSLRKSG MLGAKALHES ADLDLLYWWN SADAATETEK
     YAAFMSKLGD FDADLFADTI YHRIKEVEHK ARKWQKEARS YRDRAHIAQK DAHDKIAFRH
     FKEGDLALFL PTRNQQAGAW AAFNVGFPHY FLREQDSHRL RHREWLVARI NRIQERVVDL
     SKSLQANDSA SINDEENDNP FQLSDGLRWY LIDAQEDKPG APATPGMGKS TVAANNVEAT
     ANIHTHMAGA KGKNRDSVHS IEGINKTLSK SLESRRSSSS SKRALPFAGA GAQALLKSNP
     IASETNSLRA AAPETPVATS PVQGGLLSTG EGGRPQPGAA GSSSARRPND GPGEASGNGD
     AAKTAEPRRM LDRQESTGSP TKKSVVWDPL WSVDYTYESP GKK