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ATG8_ASPOR
ID   ATG8_ASPOR              Reviewed;         118 AA.
AC   Q2UBH5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Autophagy-related protein 8;
DE   AltName: Full=Autophagy-related ubiquitin-like modifier atg8;
DE   Flags: Precursor;
GN   Name=atg8; ORFNames=AO090012000997;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16896216; DOI=10.1128/ec.00024-06;
RA   Kikuma T., Ohneda M., Arioka M., Kitamoto K.;
RT   "Functional analysis of the ATG8 homologue Aoatg8 and role of autophagy in
RT   differentiation and germination in Aspergillus oryzae.";
RL   Eukaryot. Cell 5:1328-1336(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
CC   -!- FUNCTION: Ubiquitin-like modifier involved in autophagosomes formation.
CC       With atg4, mediates the delivery of the autophagosomes to the vacuole
CC       via the microtubule cytoskeleton. 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. Participates
CC       also in membrane fusion events that take place in the early secretory
CC       pathway. Also involved in endoplasmic reticulum-specific autophagic
CC       process and is essential for the survival of cells subjected to severe
CC       ER stress. The atg8-PE conjugate mediates tethering between adjacent
CC       membranes and stimulates membrane hemifusion, leading to expansion of
CC       the autophagosomal membrane during autophagy (By similarity). Required
CC       for both the differentiation of aerial hyphae and conidial germination
CC       (PubMed:16896216). {ECO:0000250|UniProtKB:P38182,
CC       ECO:0000269|PubMed:16896216}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane
CC       {ECO:0000269|PubMed:16896216}; Lipid-anchor
CC       {ECO:0000269|PubMed:16896216}. Vacuole membrane
CC       {ECO:0000250|UniProtKB:P38182}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P38182}. Lipid droplet
CC       {ECO:0000269|PubMed:16896216}.
CC   -!- PTM: The C-terminal 2 residues are removed by atg4 to expose Gly-116 at
CC       the C-terminus. The c-terminal Gly is then amidated with
CC       phosphatidylethanolamine by an activating system similar to that for
CC       ubiquitin. {ECO:0000250|UniProtKB:P38182}.
CC   -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
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DR   EMBL; AB246664; BAE93233.1; -; Genomic_DNA.
DR   EMBL; AP007161; BAE61090.1; -; Genomic_DNA.
DR   RefSeq; XP_001727929.1; XM_001727877.2.
DR   AlphaFoldDB; Q2UBH5; -.
DR   SMR; Q2UBH5; -.
DR   STRING; 510516.Q2UBH5; -.
DR   EnsemblFungi; BAE61090; BAE61090; AO090012000997.
DR   GeneID; 5988403; -.
DR   KEGG; aor:AO090012000997; -.
DR   VEuPathDB; FungiDB:AO090012000997; -.
DR   HOGENOM; CLU_119276_0_1_1; -.
DR   OMA; AVYQEHK; -.
DR   Proteomes; UP000006564; Chromosome 4.
DR   GO; GO:0005776; C:autophagosome; IDA:AspGD.
DR   GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IDA:AspGD.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0000324; C:fungal-type vacuole; IDA:AspGD.
DR   GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR   GO; GO:0000407; C:phagophore assembly site; IDA:AspGD.
DR   GO; GO:0043936; P:asexual sporulation resulting in formation of a cellular spore; IMP:AspGD.
DR   GO; GO:0006914; P:autophagy; IMP:AspGD.
DR   GO; GO:0009306; P:protein secretion; IMP:AspGD.
DR   InterPro; IPR004241; Atg8-like.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR10969; PTHR10969; 1.
DR   Pfam; PF02991; ATG8; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
PE   3: Inferred from homology;
KW   Autophagy; Cytoplasmic vesicle; Lipid droplet; Lipoprotein; Membrane;
KW   Protein transport; Reference proteome; Transport; Ubl conjugation pathway;
KW   Vacuole.
FT   CHAIN           1..116
FT                   /note="Autophagy-related protein 8"
FT                   /id="PRO_0000317878"
FT   PROPEP          117..118
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P38182"
FT                   /id="PRO_0000317879"
FT   SITE            116..117
FT                   /note="Cleavage; by atg4"
FT                   /evidence="ECO:0000250|UniProtKB:P38182"
FT   LIPID           116
FT                   /note="Phosphatidylethanolamine amidated glycine"
FT                   /evidence="ECO:0000250|UniProtKB:P38182"
SQ   SEQUENCE   118 AA;  13748 MW;  8C78807255E14793 CRC64;
     MRSKFKDEHP FEKRKAEAER IRQKYADRIP VICEKVEKSD IATIDKKKYL VPADLTVGQF
     VYVIRKRIKL SPEKAIFIFV DEVLPPTAAL MSSIYEEHKD EDGFLYITYS GENTFGDL
 
 
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