ID   MG179_SCHPO             Reviewed;         335 AA.
AC   Q9P6N1;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 129.
DE   RecName: Full=Autophagy-related protein 21;
DE   AltName: Full=Meiotically up-regulated gene 179 protein;
GN   Name=mug179; Synonyms=atg18b; ORFNames=SPAC823.16c;
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 SPORULATION.
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   DISRUPTION PHENOTYPE, AND 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).
CC   -!- FUNCTION: Required for cytoplasm to vacuole transport (Cvt) vesicles
CC       formation and autophagy (By similarity). Has a role in sporulation.
CC       {ECO:0000250, ECO:0000269|PubMed:16303567}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, Golgi stack membrane;
CC       Peripheral membrane protein. Vacuole membrane; Peripheral membrane
CC       protein. Preautophagosomal structure membrane; Peripheral membrane
CC       protein.
CC   -!- DISRUPTION PHENOTYPE: Impairs atg8-processing.
CC       {ECO:0000269|PubMed:23950735}.
CC   -!- SIMILARITY: Belongs to the WD repeat PROPPIN family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB90161.1; -; Genomic_DNA.
DR   RefSeq; NP_593843.1; NM_001019272.2.
DR   AlphaFoldDB; Q9P6N1; -.
DR   SMR; Q9P6N1; -.
DR   BioGRID; 279722; 3.
DR   STRING; 4896.SPAC823.16c.1; -.
DR   PaxDb; Q9P6N1; -.
DR   EnsemblFungi; SPAC823.16c.1; SPAC823.16c.1:pep; SPAC823.16c.
DR   GeneID; 2543297; -.
DR   KEGG; spo:SPAC823.16c; -.
DR   PomBase; SPAC823.16c; -.
DR   VEuPathDB; FungiDB:SPAC823.16c; -.
DR   eggNOG; KOG2110; Eukaryota.
DR   HOGENOM; CLU_826814_0_0_1; -.
DR   InParanoid; Q9P6N1; -.
DR   OMA; DDFYMEY; -.
DR   PhylomeDB; Q9P6N1; -.
DR   Reactome; R-SPO-1632852; Macroautophagy.
DR   PRO; PR:Q9P6N1; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; ISO:PomBase.
DR   GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; ISO:PomBase.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
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:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IBA:GO_Central.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; 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:0016236; P:macroautophagy; IMP:PomBase.
DR   GO; GO:0006497; P:protein lipidation; IBA:GO_Central.
DR   GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
DR   GO; GO:0006623; P:protein targeting to vacuole; ISO:PomBase.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   SMART; SM00320; WD40; 2.
DR   SUPFAM; SSF50978; SSF50978; 2.
PE   1: Evidence at protein level;
KW   Autophagy; Cytoplasm; Golgi apparatus; Membrane; Protein transport;
KW   Reference proteome; Repeat; Sporulation; Transport; Vacuole; WD repeat.
FT   CHAIN           1..335
FT                   /note="Autophagy-related protein 21"
FT                   /id="PRO_0000050881"
FT   REPEAT          165..205
FT                   /note="WD 1"
FT   REPEAT          210..249
FT                   /note="WD 2"
SQ   SEQUENCE   335 AA;  37108 MW;  BBACA9C3E4915705 CRC64;
     MPSIILYCSW NQDRGFLSIG SENGYQVYRS NPFTLCFSKK ANGASICEML YESSLLAFVN
     ISPESTRLLK LVDIKRDIVL CRIFYPSPVL SVRFTWNRLV VLIKGSIYVY NLKNMELINT
     LNTSKGNVIA FAVHENYVAY NSPTNPGDIY LASLDTAIPV TLIHCHSSAV QVVDFHPRGH
     LIATASAKGT VIRVITTSDG ELVTELRRGY IPASIVSISF HPVEPFLACA SENGTIHVFK
     ISKQPSDPNS SPTSSVTVSS SWSKYLTSNV AKVWDTRKEF ATAKIPEASF YGKIIFSSSG
     PHIQVASYSG HYYRFAVNLK NGGNCALLER YIFDD