ATG5_ASPFU
ID ATG5_ASPFU Reviewed; 326 AA.
AC Q4WNA5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Autophagy protein 5;
GN Name=atg5; ORFNames=AFUA_6G07040;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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; AAHF01000006; EAL88559.1; -; Genomic_DNA.
DR RefSeq; XP_750597.1; XM_745504.1.
DR AlphaFoldDB; Q4WNA5; -.
DR SMR; Q4WNA5; -.
DR STRING; 746128.CADAFUBP00007104; -.
DR EnsemblFungi; EAL88559; EAL88559; AFUA_6G07040.
DR GeneID; 3508752; -.
DR KEGG; afm:AFUA_6G07040; -.
DR VEuPathDB; FungiDB:Afu6g07040; -.
DR eggNOG; KOG2976; Eukaryota.
DR HOGENOM; CLU_051894_2_0_1; -.
DR InParanoid; Q4WNA5; -.
DR OMA; KWHYPLG; -.
DR OrthoDB; 457861at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
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..326
FT /note="Autophagy protein 5"
FT /id="PRO_0000317850"
FT CROSSLNK 163
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in atg12)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 326 AA; 36079 MW; 263D78C700809F16 CRC64;
MRTSSMMENQ VSLSSIQRAV WDGKLPLQIT LASSESRTYD QTDPYLIACP RISYLPSLLP
RLRAFFSPSL IEPNSQPHEG WFSFEGVPLK WHLPVGLLYD LYAGADPASK GTRVDETDHP
TSSLNDTLPW RLTVHFSDWP DEELVRLDAD GMVMHDAFIN SVKEADFLRN GTAKGIMTLS
KEDSAGLWQA VQDVDLLSFQ RISNILLPPP NQPFRNVPIR FFLPLSPDSG SPSLKVVQSP
LPPNIPATTN TSQSTNLRHS PATQVQTLGS ALHSLLPNLF PSRRTPVLAK PVLHGAAVPM
SAPIEELVRS CAYGDGWVYI VIRMMG