ID A0A0D1E2D4_USTMA Unreviewed; 1828 AA.
AC A0A0D1E2D4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Autophagy-related protein 11 {ECO:0000256|RuleBase:RU367075};
GN ORFNames=UMAG_03341 {ECO:0000313|EMBL:KIS68775.1};
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS68775.1, ECO:0000313|Proteomes:UP000000561};
RN [1] {ECO:0000313|EMBL:KIS68775.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=521 {ECO:0000313|EMBL:KIS68775.1};
RA Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., Ait-zahra M.,
RA Allen N., Allen T., An P., Anderson M., Anderson S., Arachchi H.,
RA Armbruster J., Bachantsang P., Baldwin J., Barry A., Bayul T.,
RA Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., Borowsky M.,
RA Boukhgalter B., Brunache A., Butler J., Calixte N., Calvo S., Camarata J.,
RA Campo K., Chang J., Cheshatsang Y., Citroen M., Collymore A., Considine T.,
RA Cook A., Cooke P., Corum B., Cuomo C., David R., Dawoe T., Degray S.,
RA Dodge S., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A.,
RA Elkins T., Engels R., Erickson J., Farina A., Faro S., Ferreira P.,
RA Fischer H., Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G.,
RA Gnerre S., Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K.,
RA Hafez N., Hagopian D., Hagos B., Hall J., Hatcher B., Heller A.,
RA Higgins H., Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E.,
RA Iliev I., Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M.,
RA Karlsson E., Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E.,
RA Labutti K., Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T.,
RA Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., Lui A.,
RA Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., Manning J.,
RA Marabella R., Maru K., Matthews C., Mauceli E., Mccarthy M., Mcdonough S.,
RA Mcghee T., Meldrim J., Meneus L., Mesirov J., Mihalev A., Mihova T.,
RA Mikkelsen T., Mlenga V., Moru K., Mozes J., Mulrain L., Munson G.,
RA Naylor J., Newes C., Nguyen C., Nguyen N., Nguyen T., Nicol R., Nielsen C.,
RA Nizzari M., Norbu C., Norbu N., O'donnell P., Okoawo O., O'leary S.,
RA Omotosho B., O'neill K., Osman S., Parker S., Perrin D., Phunkhang P.,
RA Piqani B., Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V.,
RA Raymond C., Retta R., Richardson S., Rise C., Rodriguez J., Rogers J.,
RA Rogov P., Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T.,
RA Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C.,
RA Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., Stetson K.,
RA Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., Tenzing P.,
RA Tesfaye S., Theodore J., Thoulutsang Y., Topham K., Towey S., Tsamla T.,
RA Tsomo N., Vallee D., Vassiliev H., Venkataraman V., Vinson J., Vo A.,
RA Wade C., Wang S., Wangchuk T., Wangdi T., Whittaker C., Wilkinson J.,
RA Wu Y., Wyman D., Yadav S., Yang S., Yang X., Yeager S., Yee E., Young G.,
RA Zainoun J., Zembeck L., Zimmer A., Zody M., Lander E.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KIS68775.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 {ECO:0000313|EMBL:KIS68775.1};
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [3] {ECO:0000313|EMBL:KIS68775.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=521 {ECO:0000313|EMBL:KIS68775.1};
RA Guldener U., Munsterkotter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) 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; CM003147; KIS68775.1; -; Genomic_DNA.
DR RefSeq; XP_011389733.1; XM_011391431.1.
DR STRING; 237631.A0A0D1E2D4; -.
DR EnsemblFungi; KIS68775; KIS68775; UMAG_03341.
DR GeneID; 23563821; -.
DR KEGG; uma:UMAG_03341; -.
DR VEuPathDB; FungiDB:UMAG_03341; -.
DR eggNOG; ENOG502QVZE; Eukaryota.
DR InParanoid; A0A0D1E2D4; -.
DR OMA; AWKSANE; -.
DR OrthoDB; 2727468at2759; -.
DR Proteomes; UP000000561; Chromosome 8.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IBA:GO_Central.
DR GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR GO; GO:1903599; P:positive regulation of autophagy of mitochondrion; IEA:UniProtKB-UniRule.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
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:UP000000561};
KW Transport {ECO:0000256|RuleBase:RU367075};
KW Vacuole {ECO:0000256|RuleBase:RU367075}.
FT DOMAIN 142..507
FT /note="Autophagy protein ATG17-like"
FT /evidence="ECO:0000259|Pfam:PF04108"
FT DOMAIN 1052..1191
FT /note="Autophagy-related protein 11 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10377"
FT REGION 63..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1400..1620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1666..1723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1773..1828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 644..869
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 905..939
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 241..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1265..1287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1431..1446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1529..1544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1561..1575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1595..1620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1666..1701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1708..1723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1783..1828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1828 AA; 197272 MW; C7250E23B1E5EAB6 CRC64;
MRVIRAYDGR SIVVNQPLSQ FASLDDLLDC LSLATEIPSD SIICMTSDGS QLKQELLDRI
IQQTATSPSE SSSAAVVEPN PSSSTHQDAH HQSQNYEFFV YNREFLYTDP TELAAELAEH
TVLEPVPPML DVELTFPPTP KSLEALVSWS AEIATLVATY EQSCHDLLER ITLIARSLQV
ALANLRDHAD NIEKGANALI DDVAQKELKR MHSLLQGYER DLCILAMVSI HPRLQSTSAQ
MANAAATSST TSAQNGNGPA NGQSGLTKPK HRTLGDYISK SKMSAVADAC HRVYTELRER
IERIQTELSL VRNDTQGLSE EVQSTTPEVA DETYQRAVEA QLRTQQLYAF ICSTCSPDPQ
GWPVADKIDQ ETFDEIVRSS NELLLLDEVV REAVQRLTQD RNDILERSLH LLIDISAIQS
EFTETGSLLA AVDADLHSNK LDGFKHLHRL KNMLWAYGAT VVEVVRRREF AKHFLGKSQS
LAELMAKVSA SEWKRRQFYR SDVSSLLPWE VKGMDDKPPS LEITTPRVSS EGMADLGLAD
LQALYELLDH IDYQLREDGI DGVDSPIPEV KAALQALAAA LQDLDDEFIH LVNHQLLNRQ
EQEDEASDDQ GDESGSDTSI RARQRLRRRQ RLSAPLAAAN AQELTQLRSE LAAAKAAQEQ
AEHGLKAETE TRLVRLKTEI ETLRRQVQTG KADVAKLEAE KREAEARIDT LAADLELERE
RRLNMVDEVN QLRRDLEQSH RIEAQAKQEV IEEADRVAEL EAQAHELHVE LEEAKRARID
ASSRIEALLS EGSSFEGELR TAQARIEELT EQLSNAHAEA AKAREAATEV ETAKERQIRS
YRAEADGDRA ILEEKVRALK ADLDAKTKLL EKQTSIATRA EQSRIPDREA IDLLRGQLRA
ADVAHEEIVK EMDHAKELAN EAEASRREVE ASRQLLLERS RGLLAKTSLL RKAVRDMPKH
TSSRQALSSE AAQATDKNNA NAASTPALAA SSGAVVAAQR AIAASTGSLS VSELSESQRQ
AALDAFDAEA EGATLETTLE ALRALDVSEM YDEIKGKLDS LNIVVRKWQK AWKSANEKAN
KANHAAREKI AFKNFQVGDL ALFLPTRSSN LAYKPWAAFN ISFPHFFLNA KGALAEQLRT
KEWVVARITS INNKVVPTAS QVKSLIQGES DADANPFRLP EGVRFFMLDV ETYGGHSSAP
PALRSRKSSS ATVDGGNGAA NDPSSHLKDA SSHPRSRSEG TLTGLKGLVE EHKNAPGGGA
EPSVAKPSQL QSIAAEASKS TTPKAVDDQQ IVPDDEAAGR TSGFSLHSDK IEAPEQSTPP
MQTPDTSPRL GSTAVLSAPS LAEKGRSKAQ QDDNTAETRS AISTSALTRV MRSASSASSF
RTEGGISAGG VGRWRAGSSA SANAAHWPSR SITGIAEEPT ARHRDGNDAD TSSSTDSTSH
RSTLIEHATM TPAFGRAPNK RRFEAAGRTH NESRSGRAAA AADAAARRHG ESQSPETGLL
DGCNARSAPA SQSRSEGITI RAPQPLHSDL SDTAVSNPFS QSPGPASLPA DREGMGTLLR
GQTRRKSSLH ITSSASVDDE VGKREAPKVQ RWPSDAVSKA SQRTTSSAST ASAPSQASGG
IRINGRSIVV DAAVLTGAHR SEASSSSVAT TAVTAAHAIP GAFPSSFSSS GSLASPASPS
VGQGQTEEAG LSSSTVRQAW RSPRFSGAAS PSRPTLSGTQ KPSFLSQTLG RFTGAAAQAV
QAPPFAPIAS ESETARKRRV SRPSLLQAIA PMQDAGGAEA EAASGTWQQT HRGTPESTAS
GVSGFSSMSG NGAQGMLKRL QGQQGSLR
//
