ATG8_SCHPO
ID ATG8_SCHPO Reviewed; 121 AA.
AC O94272;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Autophagy-related protein 8;
DE AltName: Full=Autophagy-related ubiquitin-like modifier atg8;
DE Flags: Precursor;
GN Name=atg8; ORFNames=SPBP8B7.24c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17295836; DOI=10.1111/j.1365-2443.2007.01041.x;
RA Kohda T.A., Tanaka K., Konomi M., Sato M., Osumi M., Yamamoto M.;
RT "Fission yeast autophagy induced by nitrogen starvation generates a
RT nitrogen source that drives adaptation processes.";
RL Genes Cells 12:155-170(2007).
RN [3]
RP FUNCTION.
RX PubMed=19778961; DOI=10.1099/mic.0.034389-0;
RA Mukaiyama H., Kajiwara S., Hosomi A., Giga-Hama Y., Tanaka N., Nakamura T.,
RA Takegawa K.;
RT "Autophagy-deficient Schizosaccharomyces pombe mutants undergo partial
RT sporulation during nitrogen starvation.";
RL Microbiology 155:3816-3826(2009).
RN [4]
RP FUNCTION.
RX PubMed=20070859; DOI=10.1111/j.1365-2443.2009.01376.x;
RA Mikawa T., Kanoh J., Ishikawa F.;
RT "Fission yeast Vps1 and Atg8 contribute to oxidative stress resistance.";
RL Genes Cells 15:229-242(2010).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=23950735; DOI=10.1371/journal.pgen.1003715;
RA Sun L.L., Li M., Suo F., Liu X.M., Shen E.Z., Yang B., Dong M.Q., He W.Z.,
RA Du L.L.;
RT "Global analysis of fission yeast mating genes reveals new autophagy
RT factors.";
RL PLoS Genet. 9:E1003715-E1003715(2013).
RN [6]
RP INTERACTION WITH ATG43.
RX PubMed=33138913; DOI=10.7554/elife.61245;
RA Fukuda T., Ebi Y., Saigusa T., Furukawa K., Yamashita S.I., Inoue K.,
RA Kobayashi D., Yoshida Y., Kanki T.;
RT "Atg43 tethers isolation membranes to mitochondria to promote starvation-
RT induced mitophagy in fission yeast.";
RL Elife 9:61245-61245(2020).
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).
CC Contributes to the maintenance of cell viability under conditions of
CC nitrogen-depletion. Plays a role in meiosis and sporulation and
CC contributes to oxidative stress resistance (PubMed:17295836,
CC PubMed:19778961, PubMed:20070859). {ECO:0000250|UniProtKB:P38182,
CC ECO:0000269|PubMed:17295836, ECO:0000269|PubMed:19778961,
CC ECO:0000269|PubMed:20070859}.
CC -!- SUBUNIT: Interacts with atg43 (via N-terminal atg8 interacting motif);
CC the interaction is direct. {ECO:0000269|PubMed:33138913}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000250|UniProtKB:P38182}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P38182}. Vacuole membrane
CC {ECO:0000250|UniProtKB:P38182}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P38182}.
CC -!- PTM: The C-terminal 5 residues are removed to expose Gly-116 at the C-
CC 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; CU329671; CAA21809.1; -; Genomic_DNA.
DR PIR; T40818; T40818.
DR RefSeq; NP_596531.1; NM_001022452.2.
DR PDB; 6AAF; X-ray; 2.20 A; A=1-116.
DR PDBsum; 6AAF; -.
DR AlphaFoldDB; O94272; -.
DR SMR; O94272; -.
DR BioGRID; 277897; 26.
DR STRING; 4896.SPBP8B7.24c.1; -.
DR MaxQB; O94272; -.
DR PaxDb; O94272; -.
DR EnsemblFungi; SPBP8B7.24c.1; SPBP8B7.24c.1:pep; SPBP8B7.24c.
DR GeneID; 2541386; -.
DR KEGG; spo:SPBP8B7.24c; -.
DR PomBase; SPBP8B7.24c; atg8.
DR VEuPathDB; FungiDB:SPBP8B7.24c; -.
DR eggNOG; KOG1654; Eukaryota.
DR HOGENOM; CLU_119276_0_1_1; -.
DR InParanoid; O94272; -.
DR OMA; AVYQEHK; -.
DR PhylomeDB; O94272; -.
DR Reactome; R-SPO-1632852; Macroautophagy.
DR Reactome; R-SPO-8854214; TBC/RABGAPs.
DR Reactome; R-SPO-8934903; Receptor Mediated Mitophagy.
DR Reactome; R-SPO-9664873; Pexophagy.
DR PRO; PR:O94272; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005776; C:autophagosome; IBA:GO_Central.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:PomBase.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:PomBase.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000407; C:phagophore assembly site; IDA:PomBase.
DR GO; GO:0008429; F:phosphatidylethanolamine binding; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IMP:PomBase.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; IMP:PomBase.
DR GO; GO:0061025; P:membrane fusion; ISO:PomBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007033; P:vacuole organization; IMP:PomBase.
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 1: Evidence at protein level;
KW 3D-structure; Autophagy; Cytoplasmic vesicle; 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_0000017236"
FT PROPEP 117..121
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P38182"
FT /id="PRO_0000017237"
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"
FT HELIX 4..8
FT /evidence="ECO:0007829|PDB:6AAF"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:6AAF"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:6AAF"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:6AAF"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:6AAF"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:6AAF"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:6AAF"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:6AAF"
SQ SEQUENCE 121 AA; 14155 MW; 964BC3EFE5FAE983 CRC64;
MRSQFKDDFS FEKRKTESQR IREKYPDRIP VICEKVDKSD IAAIDKKKYL VPSDLTVGQF
VYVIRKRIKL SPEKAIFIFI DEILPPTAAL MSTIYEEHKS EDGFLYITYS GENTFGTVFP
F
