ID   ATG5_EMENI              Reviewed;         334 AA.
AC   Q5B2Q6; C8VF45;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 2.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Autophagy protein 5;
GN   Name=atg5; ORFNames=AN5174;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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=EAA62355.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AACD01000089; EAA62355.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001305; CBF81013.1; -; Genomic_DNA.
DR   RefSeq; XP_662778.1; XM_657686.1.
DR   AlphaFoldDB; Q5B2Q6; -.
DR   SMR; Q5B2Q6; -.
DR   STRING; 162425.CADANIAP00003167; -.
DR   EnsemblFungi; CBF81013; CBF81013; ANIA_05174.
DR   EnsemblFungi; EAA62355; EAA62355; AN5174.2.
DR   GeneID; 2871463; -.
DR   KEGG; ani:AN5174.2; -.
DR   VEuPathDB; FungiDB:AN5174; -.
DR   eggNOG; KOG2976; Eukaryota.
DR   HOGENOM; CLU_566231_0_0_1; -.
DR   InParanoid; Q5B2Q6; -.
DR   OMA; KWHYPLG; -.
DR   OrthoDB; 457861at2759; -.
DR   Proteomes; UP000000560; Chromosome V.
DR   Proteomes; UP000005890; 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..334
FT                   /note="Autophagy protein 5"
FT                   /id="PRO_0000219004"
FT   REGION          237..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        151
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ATG12)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   334 AA;  36711 MW;  594CB52A2A360ED8 CRC64;
     MEKATLNSIQ KSVWEGQIPL KIVLAPSESR TYDQTDPYLI SYPRISYLPS LLPRLKAFFS
     SSLIDPTASQ PHDGWFSFEG VPLKWHYPVG LLYDLYAGAE PATKSSETEA LDDEQLPWRL
     VVHFGDWPDA ELVRLDAQGT VMHDAFINSV KEADFVRNGT AKGIMTLSKD DSSGLWKAVQ
     DVDLPSFQRI MNILLPPNPH QPLRNLPVRL FLPLPPKPDS NSDSPFLKVV QSPIPPTIST
     TPSQLQRQMA QSTLSSSGVS GSSPGAAQPQ PQTQTIGTAL HSILPNLFPS RRTPVIAKPV
     LHGAQVPMSA PVEEVVRAAA YGDGWVYIVI RMMG