ID A0A177WR80_BATDL Unreviewed; 1198 AA.
AC A0A177WR80;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Autophagy-related protein 11 {ECO:0000256|RuleBase:RU367075};
GN ORFNames=BDEG_26061 {ECO:0000313|EMBL:OAJ42628.1};
OS Batrachochytrium dendrobatidis (strain JEL423).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC Rhizophydiales incertae sedis; Batrachochytrium.
OX NCBI_TaxID=403673 {ECO:0000313|EMBL:OAJ42628.1, ECO:0000313|Proteomes:UP000077115};
RN [1] {ECO:0000313|EMBL:OAJ42628.1, ECO:0000313|Proteomes:UP000077115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL423 {ECO:0000313|EMBL:OAJ42628.1,
RC ECO:0000313|Proteomes:UP000077115};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Cuomo C., Devon K., Jaffe D., Butler J.,
RA Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E., Brockman W.,
RA Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA O'Leary S., Kodira C., Zeng Q., Yandava C., Alvarado L., Longcore J.,
RA James T.;
RT "The Genome Sequence of Batrachochytrium dendrobatidis JEL423.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAJ42628.1, ECO:0000313|Proteomes:UP000077115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL423 {ECO:0000313|EMBL:OAJ42628.1,
RC ECO:0000313|Proteomes:UP000077115};
RA Cuomo C.A., Farrer R.A., James T., Longcore J., Birren B.;
RT "Lineage-specific infection strategies underlie the spectrum of fungal
RT disease in amphibians.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; DS022308; OAJ42628.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A177WR80; -.
DR STRING; 403673.A0A177WR80; -.
DR VEuPathDB; FungiDB:BDEG_26061; -.
DR eggNOG; ENOG502QVZE; Eukaryota.
DR Proteomes; UP000077115; 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:UP000077115};
KW Transport {ECO:0000256|RuleBase:RU367075};
KW Vacuole {ECO:0000256|RuleBase:RU367075}.
FT DOMAIN 137..469
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT DOMAIN 1097..1196
FT /note="Autophagy-related protein 11 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10377"
FT COILED 555..582
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 607..704
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 815..945
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1198 AA; 136138 MW; 9CC067C60567E121 CRC64;
MSLKVYQAET GILLPLQRLV PGDTVDMLRA DIEAVTFIPQ KFQVLLGSNA QIVKQSMLTT
LLSSQKDERI FIFNRLALMQ QTGNKPVHMS IDIEPPVPSD TVVGLKVISP LAPNLSSKER
VIAFKRAFSE HISYGQALRK IANKHAKTCE RLLEEQSIQV EGLTMALCNL FTHRKSVLDS
YDSFIAPAQI QISSHTELLH GIAADLDTLT MIPIHEAIVS ESKVLNDYIP RDKLLRWIND
CRVAHDELVD KVQSISVTMN DVRAGARIDQ LEPEDFDLSK LDPLLDIVRK LVGQIESRQN
ILERDFTRVE TILADISNGP DDQAGDRFEA LEHLYKIHFE EYIPEITRCD RQVRETVVQF
SDSKAHLTQA LMEKLLELAK QQSTIYIIPQ ALMALDKELR VQAEAFLQLL HVHRMPPAWG
AAFIEIVRRR EHSKVLGDKV NQIMGILTSF QNQEEARRDT FRTEIERYLP KGLLKGLESA
TPSIKLSISE DEILLPNLTK DDVTAFSQMV ASLRAIQDPS TVQTSGSLSK LHAMMVQMSP
QVDSPLLDFE ELISNSTFCD RIVKLEAENA KLRKEVVEMR AQAAPVSQTS TAFRHPSMND
VLSSSHSTKQ EEKIKAYEAR IKNLEQLLQQ SYSTSGAVEK THVTDRRLMQ EMESTIQTMT
LEKERILKEN QQFCDQLQQS TQRISELTTL YQNVRESHDK LRNEKQTTDV QLSNTLVELK
KLQDFLVEVR EYMEGCCLSL RRDTGSEQKS DIEEQTPVQL NHMRSKPASI DELRRCMRVL
KDDILWHAAM MESMKNSMQD SQDGSDVTQS VAAEMVTLIQ RLGETEERLR IAENDLTVAQ
AHEAVLEADL ESLKVLYERA EGHVAAAKVQ RNEHQAQQEK NALELKRLQD LQESQIEQHR
TSEVVLQKQI EQIKKELEQT QADSMADIES QKQAHTKAIE QMRLDMQQDL SQRELSRLAF
SQVQQMREQI EDWNIVCRLS LQHLTGCLDA LVRLVQHTLS EDVVYALIRN NGLTGSTENC
CLSKLSDTFS ISDAGAHYDD TKSLIEGFGN DDDALGGMSK FIEHYDLLLR ELYSKVVSAG
AYLDVSDSVD RIEKRWSDLT GQASFRVAFQ NFKINDLVLF LPTRNPAAWT AFNVNTPHFF
LDIQPNSVFA DRIQQRGWIL AYITGITDKT ATDISLSPTN PFGLAEETRY HICQATPY
//
