ID M2UML2_COCH5 Unreviewed; 1347 AA.
AC M2UML2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Autophagy-related protein 11 {ECO:0000256|RuleBase:RU367075};
GN ORFNames=COCHEDRAFT_1205377 {ECO:0000313|EMBL:EMD89193.1};
OS Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) (Southern
OS corn leaf blight fungus) (Bipolaris maydis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=701091 {ECO:0000313|EMBL:EMD89193.1, ECO:0000313|Proteomes:UP000016936};
RN [1] {ECO:0000313|EMBL:EMD89193.1, ECO:0000313|Proteomes:UP000016936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2] {ECO:0000313|Proteomes:UP000016936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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; KB445579; EMD89193.1; -; Genomic_DNA.
DR STRING; 701091.M2UML2; -.
DR eggNOG; ENOG502QVZE; Eukaryota.
DR HOGENOM; CLU_002803_1_0_1; -.
DR OMA; GLRWYLI; -.
DR Proteomes; UP000016936; 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:UP000016936};
KW Transport {ECO:0000256|RuleBase:RU367075};
KW Vacuole {ECO:0000256|RuleBase:RU367075}.
FT DOMAIN 101..446
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT DOMAIN 1068..1215
FT /note="Autophagy-related protein 11 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10377"
FT REGION 579..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1173..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1239..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 544..571
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 637..767
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 824..946
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1074..1101
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 612..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1288..1306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1347 AA; 151483 MW; 56B10B024B9EABC1 CRC64;
MSLQIAVAHT GQRLDADPVA FTSVDALKYW ISRTTEIPPE QQVLLTTQGK HKEIFVFSRE
ISNNPQAAIS STPLPDPFAP DDAPNHLANN TDLGAWQALF QARRNWAFAL LEKSHSMSRI
ASKHFAEQAT IERATQVAVG NHDAHIKGLE QKYKAAKEWY DGVEKEAGDN LRRLDRDFAQ
LGTVSAILNF KRFLAKEMRS AKNVPSNVIV RETLQDFLDV EAVKMATATS QRVREAFGKR
MDKTNMQLEK IAADYNDLLR AVGQSQSRSV VDDTEEPVRL YNEIDAVAKK VESDLEHVMG
LEASSKSVAQ VSKMALLHTR NFLPAIQEYS VEMSDLVRRA VEQKNAAIRN SVESMQGIAN
IESFIASMGA DLEQISIPQE GVAAFELISL VGRLPYVYGT LLVEAVRRRE WMERMERDTS
SLAEEMATFQ EEEERRRKRW LKPIADVVNL EAVQGGTLGF EMNVQPEKTV WPTVTREELR
DYLKDLQRLD GQQSEAEAFA QAIKDLDRPT KQQIKRAKNF KMGSVHEPAF GRGSHLMMRG
DDELRVLKEG NAKLEEELRG YKSRVRRLED LVHRQNTVSR LSIGGAPPSF SIPDAAEPST
PTARVASPRP MEENSRRSSI SSRRLSANTG QEDKRRILRL EQELAAEKEA RVKLENEAQS
RRDEDADQQR RFEEAMSTTN NIMENMRAQQ KEFAEERKSL EDEIRVYKAR IEEAEDELDR
LLGSRDNERI GIDTRVQELV AELEQTRKEA AEQKTRTDEQ TEALQAEIIK LKATRAQERD
SLATVFNHLS PGTSVPDDHS ALIAQLEDVA VRSLNYQKEL QQAVAVAKSD NDNAHARIEE
QENNFNAKVA EHEKAIALVR EDLDAEKAKA ASITAQLEEE KSHLHDLRSK FAEGETGSEA
LRKRVEEEEA KVGRLQTELA EKNSHANSLD VELMRAEKRL RKLEEVDSSR THQRMTRAKD
LSQRLYTQHE RLVRLLEALG FVITHENGEM VLQRASKLGN STVMADTSAG ISRSTTAPSP
TPLKRFLEDV GDLHFLQWTE AMSPEEEDQR YQELISKLDL FNIETFSDAV AKRMRDMEHT
ARKWQKEARA YRDKAHRFQA DSHDKIAYRS FKEGDLALFL PTRNNAHRPW AAFNVGAPHY
FLREQDTHRL GGKEWLVARI SKVEERVVDL SKTLDGPPRA SLDDRSVASS NAVSFEDDNP
FELSDGLRWY LLEATEEKAM APGTPGIKGA VTVKSSLETG QGEMQKSKKK SLMDPATQLG
KSLDSRRSSG TSKKSAPLAG KNNSAEALSP GERANSTPNS ATATRGGSPA GAHGPSHLRE
TETNGTEPDK TAYDGNGTNV RDLLWGP
//
