ID   ATG5_PHANO              Reviewed;         311 AA.
AC   Q0UXN8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Autophagy protein 5;
GN   Name=ATG5; ORFNames=SNOG_03476;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAT88681.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH445329; EAT88681.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001794039.1; XM_001793987.1.
DR   AlphaFoldDB; Q0UXN8; -.
DR   SMR; Q0UXN8; -.
DR   STRING; 13684.SNOT_03476; -.
DR   GeneID; 5970902; -.
DR   KEGG; pno:SNOG_03476; -.
DR   eggNOG; KOG2976; Eukaryota.
DR   InParanoid; Q0UXN8; -.
DR   OMA; KWHYPLG; -.
DR   OrthoDB; 457861at2759; -.
DR   Proteomes; UP000001055; 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..311
FT                   /note="Autophagy protein 5"
FT                   /id="PRO_0000317858"
FT   REGION          102..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        159
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ATG12)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   311 AA;  34951 MW;  2A233816F2C34C7D CRC64;
     MSSREVTSRL REKVWNGSVP LEIRLHKGDC RTYDDSDAYL IQFPRLSYLA LLIHKLHAFF
     APSLIYPDIH PSDLWFSYEG VPLKWHYPLG LLYDLYSGAE PYHPSDSPPP SPTTPSKQDS
     KQPLPWRLTL HTSAYPTTQL IPLDNNNLQI HDLFIHSVKE ADYLRTGTGK TVMFLSQADS
     TQLWDAVVKH DFALFNPINQ KLLNPQGVNL RHLPVRLYLP HAGVDEEDRG MGSVRVVQSL
     VKVEVGSRQP QTIGTALNQI LPTLFPSRRS ALLAQAVLHG AVVPLGASVE ELIRSVAYLD
     GWLHIAIVMM G