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ATG3_PHANO
ID   ATG3_PHANO              Reviewed;         350 AA.
AC   Q0U388;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Autophagy-related protein 3;
DE   AltName: Full=Autophagy-related E2-like conjugation enzyme ATG3;
GN   Name=ATG3; ORFNames=SNOG_13776;
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: E2 conjugating enzyme required for the cytoplasm to vacuole
CC       transport (Cvt) and autophagy. Required for selective autophagic
CC       degradation of the nucleus (nucleophagy) as well as for 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. Responsible
CC       for the E2-like covalent binding of phosphatidylethanolamine to the C-
CC       terminal Gly of ATG8. The ATG12-ATG5 conjugate plays a role of an E3
CC       and promotes the transfer of ATG8 from ATG3 to phosphatidylethanolamine
CC       (PE). This step is required for the membrane association of ATG8. The
CC       formation of the ATG8-phosphatidylethanolamine conjugate is essential
CC       for autophagy and for the cytoplasm to vacuole transport (Cvt). The
CC       ATG8-PE conjugate mediates tethering between adjacent membranes and
CC       stimulates membrane hemifusion, leading to expansion of the
CC       autophagosomal membrane during autophagy (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. Interacts with ATG8 through an intermediate thioester
CC       bond through the C-terminal Gly of ATG8. Also interacts with the 40
CC       amino acid C-terminal region of the E1-like ATG7 enzyme. Interacts also
CC       with the ATG12-ATG5 conjugate. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: The N-terminal region is involved in phosphatidylethanolamine-
CC       binding and is required for ATG8-PE conjugation. {ECO:0000250}.
CC   -!- DOMAIN: The flexible region (FR) is required for ATG7-binding.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The handle region (HR) contains the ATG8 interaction motif
CC       (AIM) and mediates binding to ATG8. It is crucial for the cytoplasm-to-
CC       vacuole targeting pathway (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATG3 family. {ECO:0000305}.
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DR   EMBL; CH445352; EAT78800.1; -; Genomic_DNA.
DR   RefSeq; XP_001803981.1; XM_001803929.1.
DR   AlphaFoldDB; Q0U388; -.
DR   SMR; Q0U388; -.
DR   STRING; 13684.SNOT_13776; -.
DR   EnsemblFungi; SNOT_13776; SNOT_13776; SNOG_13776.
DR   GeneID; 5980903; -.
DR   KEGG; pno:SNOG_13776; -.
DR   eggNOG; KOG2981; Eukaryota.
DR   HOGENOM; CLU_027518_2_0_1; -.
DR   InParanoid; Q0U388; -.
DR   OMA; YDKYYQV; -.
DR   OrthoDB; 1432328at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0000153; C:cytoplasmic ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0061908; C:phagophore; IEA:EnsemblFungi.
DR   GO; GO:0000407; C:phagophore assembly site; IEA:EnsemblFungi.
DR   GO; GO:0019776; F:Atg8 ligase activity; 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; IEA:EnsemblFungi.
DR   GO; GO:0044805; P:late nucleophagy; IEA:EnsemblFungi.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR   GO; GO:0006612; P:protein targeting to membrane; IEA:EnsemblFungi.
DR   InterPro; IPR007135; Atg3/Atg10.
DR   PANTHER; PTHR12866; PTHR12866; 1.
DR   Pfam; PF03987; Autophagy_act_C; 1.
PE   3: Inferred from homology;
KW   Autophagy; Cytoplasm; Protein transport; Reference proteome; Transport;
KW   Ubl conjugation pathway.
FT   CHAIN           1..350
FT                   /note="Autophagy-related protein 3"
FT                   /id="PRO_0000317825"
FT   REGION          87..165
FT                   /note="Flexible region"
FT                   /evidence="ECO:0000250"
FT   REGION          126..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          248..326
FT                   /note="Handle region"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        244
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   350 AA;  38716 MW;  6822A2FA921B6500 CRC64;
     MAYNFVRSYI DTFRERTAAI SHTSTFRETG QITPEEFVLA GDFLVFKFPS WQWGDASSAG
     KRVPYLPEGK QYLMTRGVPC HRRLDDNFAG EAGQDETIVG DGFAGSEGAD DDGWLRTGGM
     AASQEAKVRD VRTVDESGNL GAAEEEDEIP DMEDMDDDEE AIIRDPQGGS SSTAPLRTYT
     LYICYSAHYR TPRLYLSGYG ATSVPLKPQE MMEDIVGDYK DKTVTIEDFP FFEHALKTAS
     VHPCKHASVM KVLLDRADAA LKLRLAKLKA GKDIGKLDTG MEGLVDDTRL LKLSEQAKGK
     EGDEAKDDWE VLSEGGDDEV AIRVDQYLVV FLKFMASVTP GIEHDFTMGV
 
 
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