ID A0A371CJA2_9APHY Unreviewed; 1402 AA.
AC A0A371CJA2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Autophagy-related protein 11 {ECO:0000256|RuleBase:RU367075};
GN ORFNames=OH76DRAFT_1366354 {ECO:0000313|EMBL:RDX40353.1};
OS Polyporus brumalis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Polyporus.
OX NCBI_TaxID=139420 {ECO:0000313|EMBL:RDX40353.1, ECO:0000313|Proteomes:UP000256964};
RN [1] {ECO:0000313|EMBL:RDX40353.1, ECO:0000313|Proteomes:UP000256964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM 1820 {ECO:0000313|EMBL:RDX40353.1,
RC ECO:0000313|Proteomes:UP000256964};
RX PubMed=30061923; DOI=10.1186/s13068-018-1198-5;
RA Miyauchi S., Rancon A., Drula E., Hage H., Chaduli D., Favel A., Grisel S.,
RA Henrissat B., Herpoel-Gimbert I., Ruiz-Duenas F.J., Chevret D., Hainaut M.,
RA Lin J., Wang M., Pangilinan J., Lipzen A., Lesage-Meessen L., Navarro D.,
RA Riley R., Grigoriev I.V., Zhou S., Raouche S., Rosso M.N.;
RT "Integrative visual omics of the white-rot fungus Polyporus brumalis
RT exposes the biotechnological potential of its oxidative enzymes for
RT delignifying raw plant biomass.";
RL Biotechnol. Biofuels 11:201-201(2018).
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; KZ857562; RDX40353.1; -; Genomic_DNA.
DR STRING; 139420.A0A371CJA2; -.
DR Proteomes; UP000256964; 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:UP000256964};
KW Transport {ECO:0000256|RuleBase:RU367075};
KW Vacuole {ECO:0000256|RuleBase:RU367075}.
FT DOMAIN 111..426
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT DOMAIN 916..1024
FT /note="Autophagy-related protein 11 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10377"
FT REGION 1029..1351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1374..1402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 531..558
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 605..702
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 743..805
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1029..1043
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1184
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1240..1342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1402 AA; 153027 MW; DF3ACECF2669FE47 CRC64;
MIQLCRAEDG VIIQLDVSLW DLERLDSLEH FIYERTGVPP DAVWAYLSDG RPLKNDNVRE
LAGLEDQQTI YVFNKSYLSS DPEEVIYHLR CESELQPPVE DAIASTPPFR ISQLASSYVQ
TALTHVEYIN RTLTSLHYQQ RAVQISSSAL DHHILATTDT YEGIAAIAER ELDKQGKLLG
GLDADLEIAS RVKVHKEFLS VSVRRAMEAG DKGRTLGDYV SKVKMQQVAA SCVKTHEELK
SRFETVRAAM ERLSQGSDEV RHAVSNSSSI DDGENCGRRT QELWEQISSL NSTIDRPGVI
PEKALQEFRQ LDDGLRLEVE RITEVKNAYT EQCVYAIRRI SELNTDLVTL PSAMTSLQTS
FRAKTSFSHI ARLHSMLYAY GATVVEIVRR KEFARFFYQR AQSILEVMAK LSSNERKRRQ
AYKNEVQGEL PFEVKAMDDA VPNIDFSPSG SSDSPYTLER VDIDDFLRVL EDLEHFAKEA
NDSVAEASVH EARSKLHKLI GKMDTLESGF DRIAERSLLS TSRLLSHRRR ATEDDQAYAE
LQLQLKDLQQ QRAEEQAASK QSSSALEAEI VQLRDSLQMS ETARGQLERD LHAARAQLES
EAMSRRILEE RNAEMSQEAD AKRETLAIAL AEATEQTRSA EVLRQQLTQV QSEYEAMKSL
EARNAEKVST LLEEQAKTLR RLEEARARGE DLEAQIHAAR GESDDVKRAL LEAGKEKDRL
LRAQASEHDR LLRDHIAEAD GDRAVLEHQF SELRAALDDA ERRLKDALAQ AEMANADAVG
LREELQRVEH ELRDARRDER AVRDDLRATR ASQADFEHRL EQSERLVAQM LDVALAFRDA
HVKALSNVQA MITHPGNRAS AAANLADSAL SHSRHTIVAH SGEPAPIDPS DPVAALDALR
AFDHDHFLES IGKAGQTIRK WQKQCKDYRE RAKGKISFRN FAKGDLALFL PTRNSISKPW
AAFNVSFPHY FLQATGHLAE QLKTREWIVA RITSITERIV DAKDPSSNPY GLGDGVKYYM
LEVEDWTQPS YPSKRRESSK KVPTVEPPLE SAGQLLPAAD TGSIPTGPPE PEVEESFSAT
RPPTSHLFPR TRAGSSPTAG PSSLSRLLAQ AGPSEPPASS SLGLVSADVG DDAPHAHTAA
PPKGDSPRAS RSVSPTVPLP PPASVPSPPP SHSQSPPSPT TRPIPGPSTA SGSHPANIHA
PSLPSPLRPG SRASRGSTSS RFSTARIPFG GVPSAATAKA MPTTAISEQA ISTLSTTPTS
GTGSGSGSGS GSSDTVAVGM PDALSNSSIP SPEGSPTMGM SHLLSQTHRR RTTSYHLPTA
RSSTVGLSTP TTSASASSPL ATGTGAGAGI GATASSRLAS LASSWGVSFG RKKGKELAEA
EGGGRAPGTS SPIPESPTRS SD
//
