ID   ATG8_USTMA              Reviewed;         118 AA.
AC   Q4P2U6; A0A0D1DQB5;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Autophagy-related protein 8;
DE   AltName: Full=Autophagy-related ubiquitin-like modifier atg8;
DE   Flags: Precursor;
GN   Name=ATG8; ORFNames=UMAG_05567;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20618705; DOI=10.1111/j.1364-3703.2010.00620.x;
RA   Nadal M., Gold S.E.;
RT   "The autophagy genes ATG8 and ATG1 affect morphogenesis and pathogenicity
RT   in Ustilago maydis.";
RL   Mol. Plant Pathol. 11:463-478(2010).
RN   [4]
RP   FUNCTION.
RX   PubMed=22843561; DOI=10.1128/ec.00115-12;
RA   Nieto-Jacobo F., Pasch D., Basse C.W.;
RT   "The mitochondrial Dnm1-like fission component is required for lgA2-induced
RT   mitophagy but dispensable for starvation-induced mitophagy in Ustilago
RT   maydis.";
RL   Eukaryot. Cell 11:1154-1166(2012).
CC   -!- FUNCTION: Ubiquitin-like modifier involved in autophagosomes formation.
CC       With ATG4, mediates the delivery of the autophagosomes to the vacuole
CC       via the microtubule cytoskeleton. Participates also in membrane fusion
CC       events that take place in the early secretory pathway. Also involved in
CC       endoplasmic reticulum-specific autophagic process and is essential for
CC       the survival of cells subjected to severe ER stress. The ATG8-PE
CC       conjugate mediates tethering between adjacent membranes and stimulates
CC       membrane hemifusion, leading to expansion of the autophagosomal
CC       membrane during autophagy (By similarity). Required for selective
CC       autophagic degradation of the mitochondria (mitophagy) which
CC       contributes to regulate mitochondrial quantity and quality by
CC       eliminating the mitochondria to a basal level to fulfill cellular
CC       energy requirements and preventing excess ROS production. Required for
CC       wild-type budding of haploid sporidia and for complete symptom
CC       development during pathogenic growth such as gall formation and
CC       teliospore production in ears of mature maize (PubMed:20618705,
CC       PubMed:22843561). {ECO:0000250|UniProtKB:P38182,
CC       ECO:0000269|PubMed:20618705, ECO:0000269|PubMed:22843561}.
CC   -!- SUBUNIT: Conjugation to phosphatidylethanolamine (PE) leads to
CC       homodimerization. Interacts with ATG1, ATG3, ATG4, ATG7, ATG12, ATG32,
CC       ATG34 and the C-terminal 10 residues domain of ATG19. Interacts also
CC       with the endoplasmic reticulum to Golgi v-SNARE protein BET1 and the
CC       vacuolar v-SNARE protein NYV1. Interacts with the UBX domain-containing
CC       protein SHP1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane
CC       {ECO:0000250|UniProtKB:P38182}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P38182}. Vacuole membrane
CC       {ECO:0000250|UniProtKB:P38182}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P38182}.
CC   -!- INDUCTION: Transcripts accumulate during carbon stress conditions.
CC       {ECO:0000269|PubMed:20618705}.
CC   -!- PTM: The C-terminal 2 residues are removed by ATG4 to expose Gly-116 at
CC       the C-terminus. The C-terminal Gly is then amidated with
CC       phosphatidylethanolamine by an activating system similar to that for
CC       ubiquitin. {ECO:0000250|UniProtKB:P38182}.
CC   -!- DISRUPTION PHENOTYPE: Prevents vacuolar accumulation of autophagosomes
CC       and affects survival during carbon starvation.
CC       {ECO:0000269|PubMed:20618705}.
CC   -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
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DR   EMBL; CM003157; KIS66579.1; -; Genomic_DNA.
DR   RefSeq; XP_011391873.1; XM_011393571.1.
DR   AlphaFoldDB; Q4P2U6; -.
DR   SMR; Q4P2U6; -.
DR   STRING; 5270.UM05567P0; -.
DR   EnsemblFungi; KIS66579; KIS66579; UMAG_05567.
DR   GeneID; 23565422; -.
DR   KEGG; uma:UMAG_05567; -.
DR   VEuPathDB; FungiDB:UMAG_05567; -.
DR   eggNOG; KOG1654; Eukaryota.
DR   HOGENOM; CLU_119276_0_1_1; -.
DR   InParanoid; Q4P2U6; -.
DR   OMA; AVYQEHK; -.
DR   OrthoDB; 1508198at2759; -.
DR   PHI-base; PHI:2497; -.
DR   Proteomes; UP000000561; Chromosome 18.
DR   GO; GO:0005776; C:autophagosome; IBA:GO_Central.
DR   GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR   GO; GO:0008429; F:phosphatidylethanolamine binding; IBA:GO_Central.
DR   GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR   GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR004241; Atg8-like.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR10969; PTHR10969; 1.
DR   Pfam; PF02991; ATG8; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
PE   2: Evidence at transcript level;
KW   Autophagy; Cytoplasmic vesicle; Lipoprotein; Membrane; Protein transport;
KW   Reference proteome; Transport; Ubl conjugation pathway; Vacuole; Virulence.
FT   CHAIN           1..116
FT                   /note="Autophagy-related protein 8"
FT                   /id="PRO_0000017238"
FT   PROPEP          117..118
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P38182"
FT                   /id="PRO_0000017239"
FT   SITE            116..117
FT                   /note="Cleavage; by ATG4"
FT                   /evidence="ECO:0000250|UniProtKB:P38182"
FT   LIPID           116
FT                   /note="Phosphatidylethanolamine amidated glycine"
FT                   /evidence="ECO:0000250|UniProtKB:P38182"
SQ   SEQUENCE   118 AA;  13675 MW;  8756A51F7BE05C3C CRC64;
     MRSAFKNEHS FEKRKAEAER IRQKYPDRIP VICEKADRTD IPTIDKKKYL VPSDLTVGQF
     VYVIRKRIKL APEKAIFIFV DEVLPATAAL MSAIYEEHKD EDGFLYVSYS GENTFGQL