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ATG8_CRYNJ
ID   ATG8_CRYNJ              Reviewed;         126 AA.
AC   P0CO54; Q55YQ9; Q5KN30;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Autophagy-related protein 8;
DE   AltName: Full=Autophagy-related ubiquitin-like modifier ATG8;
DE   Flags: Precursor;
GN   Name=ATG8; OrderedLocusNames=CNA07930;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(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.
CC       {ECO:0000250|UniProtKB:P38182}.
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 9 residues are removed to expose Gly-117 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; AE017341; AAW41320.1; -; Genomic_DNA.
DR   RefSeq; XP_567139.1; XM_567139.1.
DR   AlphaFoldDB; P0CO54; -.
DR   SMR; P0CO54; -.
DR   STRING; 5207.AAW41320; -.
DR   PaxDb; P0CO54; -.
DR   EnsemblFungi; AAW41320; AAW41320; CNA07930.
DR   GeneID; 3253893; -.
DR   KEGG; cne:CNA07930; -.
DR   VEuPathDB; FungiDB:CNA07930; -.
DR   eggNOG; KOG1654; Eukaryota.
DR   HOGENOM; CLU_119276_0_1_1; -.
DR   InParanoid; P0CO54; -.
DR   OMA; AVYQEHK; -.
DR   OrthoDB; 1508198at2759; -.
DR   Proteomes; UP000002149; Chromosome 1.
DR   GO; GO:0005776; C:autophagosome; IBA:GO_Central.
DR   GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR   GO; GO:0008429; F:phosphatidylethanolamine binding; IBA:GO_Central.
DR   GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR   GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; Lipoprotein; Membrane; Protein transport;
KW   Reference proteome; Transport; Ubl conjugation pathway; Vacuole.
FT   CHAIN           1..117
FT                   /note="Autophagy-related protein 8"
FT                   /id="PRO_0000017214"
FT   PROPEP          118..126
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P38182"
FT                   /id="PRO_0000017215"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            117..118
FT                   /note="Cleavage; by ATG4"
FT                   /evidence="ECO:0000250|UniProtKB:P38182"
FT   LIPID           117
FT                   /note="Phosphatidylethanolamine amidated glycine"
FT                   /evidence="ECO:0000250|UniProtKB:P38182"
SQ   SEQUENCE   126 AA;  14691 MW;  93AA67B3F8884CC9 CRC64;
     MVRSKFKDEH PFDKRKAEAE RIRQKYQDRI PVICEKAEKS DIPTIDKKKY LVPADLTVGQ
     FVYVIRKRIK LAPEKAIFIF VDDILPPTAA LMSSIYDEHK DEDGFLYVLY ASENTFGDLE
     QYAISE
 
 
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