ID   ATG5_SCHPO              Reviewed;         261 AA.
AC   O74971;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=Autophagy protein 5;
DE   AltName: Full=Meiotically up-regulated gene 77 protein;
GN   Name=atg5; Synonyms=mug77; ORFNames=SPBC4B4.10c;
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 IN MEIOSIS.
RX   PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA   Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA   Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA   Smith G.R., Moreno S.;
RT   "A large-scale screen in S. pombe identifies seven novel genes required for
RT   critical meiotic events.";
RL   Curr. Biol. 15:2056-2062(2005).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [4]
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   [5]
RP   DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, CONJUGATION TO ATG12, AND
RP   INTERACTION WITH ATG16 AND ATG18.
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).
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). Has a role in meiosis and
CC       sporulation. {ECO:0000250, ECO:0000269|PubMed:16303567,
CC       ECO:0000269|PubMed:19778961}.
CC   -!- SUBUNIT: Conjugated with atg12. Interacts with atg16 and atg18.
CC       {ECO:0000269|PubMed:23950735}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Preautophagosomal structure
CC       membrane; Peripheral membrane protein.
CC   -!- PTM: Conjugated to atg12; which is essential for autophagy.
CC   -!- DISRUPTION PHENOTYPE: Impairs atg8-processing.
CC       {ECO:0000269|PubMed:23950735}.
CC   -!- SIMILARITY: Belongs to the ATG5 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA19290.1; -; Genomic_DNA.
DR   PIR; T40482; T40482.
DR   RefSeq; NP_596427.1; NM_001022346.2.
DR   AlphaFoldDB; O74971; -.
DR   SMR; O74971; -.
DR   BioGRID; 277333; 14.
DR   STRING; 4896.SPBC4B4.10c.1; -.
DR   MaxQB; O74971; -.
DR   PaxDb; O74971; -.
DR   EnsemblFungi; SPBC4B4.10c.1; SPBC4B4.10c.1:pep; SPBC4B4.10c.
DR   GeneID; 2540814; -.
DR   KEGG; spo:SPBC4B4.10c; -.
DR   PomBase; SPBC4B4.10c; atg5.
DR   VEuPathDB; FungiDB:SPBC4B4.10c; -.
DR   eggNOG; KOG2976; Eukaryota.
DR   HOGENOM; CLU_051894_2_0_1; -.
DR   InParanoid; O74971; -.
DR   OMA; KWHYPLG; -.
DR   PhylomeDB; O74971; -.
DR   Reactome; R-SPO-1632852; Macroautophagy.
DR   Reactome; R-SPO-8934903; Receptor Mediated Mitophagy.
DR   PRO; PR:O74971; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0000407; C:phagophore assembly site; IDA:PomBase.
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:0006914; P:autophagy; IMP:PomBase.
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:0016236; P:macroautophagy; IMP:PomBase.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0000423; P:mitophagy; IMP:PomBase.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0061709; P:reticulophagy; IMP:PomBase.
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   1: Evidence at protein level;
KW   Autophagy; Cytoplasm; Isopeptide bond; Meiosis; Membrane; Nucleus;
KW   Protein transport; Reference proteome; Transport; Ubl conjugation.
FT   CHAIN           1..261
FT                   /note="Autophagy protein 5"
FT                   /id="PRO_0000219008"
FT   CROSSLNK        148
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ATG12)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   261 AA;  29827 MW;  E6202802E0EFF514 CRC64;
     MNVDNNKGNI PELLWNGTIS VRIDYEGNSL AYLANVPRQS YFAQILPNVQ RLLAPSIPLS
     ECWLDYNGVP LKWHWPVGLL FDLLTVFDPD TPRAPVLWRI QLRSGLFPTT KILQMETMDT
     FRTYFFNCLK ESDYVRNGSS SGIIALSKAE TDTYWNAILN HDYYDFRPIA IKILFSKSKF
     IPLKIYLGAN APIIQTSAPL GSSLGEFLNK RLPDLFPSCD KFLIVKPVIH GITIFLQSVL
     DELNRDFCYI DGFLHIVLMK V