ID   ATG5_SCLS1              Reviewed;         266 AA.
AC   A7EJG6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Autophagy protein 5;
GN   Name=atg5; ORFNames=SS1G_05459;
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
CC   -!- FUNCTION: Involved in cytoplasm to vacuole transport (Cvt) and
CC       autophagic vesicle formation. Autophagy is essential for maintenance of
CC       amino acid levels and protein synthesis under nitrogen starvation.
CC       Required for selective autophagic degradation of the nucleus
CC       (nucleophagy). Also required for mitophagy, which eliminates defective
CC       or superfluous mitochondria in order to fulfill cellular energy
CC       requirements and prevent excess ROS production. Conjugation with atg12,
CC       through a ubiquitin-like conjugating system involving atg7 as an E1-
CC       like activating enzyme and atg10 as an E2-like conjugating enzyme, is
CC       essential for its function. The atg12-atg5 conjugate acts as an E3-like
CC       enzyme which is required for lipidation of atg8 and atg8 association to
CC       the vesicle membranes (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Conjugated with atg12. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- PTM: Conjugated to atg12; which is essential for autophagy.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATG5 family. {ECO:0000305}.
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DR   EMBL; CH476626; EDO02982.1; -; Genomic_DNA.
DR   RefSeq; XP_001594031.1; XM_001593981.1.
DR   AlphaFoldDB; A7EJG6; -.
DR   SMR; A7EJG6; -.
DR   STRING; 665079.A7EJG6; -.
DR   EnsemblFungi; EDO02982; EDO02982; SS1G_05459.
DR   GeneID; 5489984; -.
DR   KEGG; ssl:SS1G_05459; -.
DR   VEuPathDB; FungiDB:sscle_08g066910; -.
DR   eggNOG; KOG2976; Eukaryota.
DR   HOGENOM; CLU_051894_2_0_1; -.
DR   InParanoid; A7EJG6; -.
DR   OMA; KWHYPLG; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
DR   GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IBA:GO_Central.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR   GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR   GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR   GO; GO:0006501; P:C-terminal protein lipidation; IBA:GO_Central.
DR   GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.246.190; -; 1.
DR   Gene3D; 3.10.20.620; -; 1.
DR   InterPro; IPR007239; Atg5.
DR   InterPro; IPR042526; Atg5_HR.
DR   InterPro; IPR042527; Atg5_UblA_dom.
DR   PANTHER; PTHR13040; PTHR13040; 1.
DR   Pfam; PF04106; APG5; 1.
PE   3: Inferred from homology;
KW   Autophagy; Isopeptide bond; Membrane; Protein transport;
KW   Reference proteome; Transport; Ubl conjugation.
FT   CHAIN           1..266
FT                   /note="Autophagy protein 5"
FT                   /id="PRO_0000317862"
FT   REGION          158..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        97
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in atg12)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   266 AA;  29236 MW;  E35C0908D231F66C CRC64;
     MQSLIWASAI PLYITHSSST IPYLINVPRV SYLALLFPRL TSFFGENVSS FSYEGILLKN
     LPVGLLCDLY QPELPWRIEL GDGPLFDIHD TFINSVKEAD FMRNGNAKGI MSMSKEHSTQ
     LWNSVQDNDF STYHKISTIL LNPATALKHI PLRIYLPSSS TPSSTPHPGS SGSSKAPSTA
     SPPSPLFTFK TIQTLIQPQT TSREPQTLGG ALNSVLPTLF PSKRDAILAE VILHGATVPF
     KAVLEDLMRE ASYADGWLNV CVVMLN