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DescriptionRecName: Full=Autophagy-related protein 21; AltName: Full=Meiotically up-regulated gene 179 protein;
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MyHits synonymsMG179_SCHPO , Q9P6N1 , BBACA9C3E4915705
match map segment
ismart:WD40 ismart:WD40  
Legends: 1, ismart:WD40 [T].
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   30-NOV-2016, entry version 104.
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;
OC   Schizosaccharomycetaceae; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., 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.,
RA   San-Segundo P., Smith G.R., Moreno S.;
RT   "A large-scale screen in S. pombe identifies seven novel genes
RT   required for 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
RT   fission 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.,
RA   He W.Z., 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)
CC       vesicles formation and autophagy (By similarity). Has a role in
CC       sporulation. {ECO:0000250, ECO:0000269|PubMed:16303567}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, Golgi stack
CC       membrane; Peripheral membrane protein. Vacuole membrane;
CC       Peripheral membrane protein. Preautophagosomal structure membrane;
CC       Peripheral membrane protein.
CC   -!- DISRUPTION PHENOTYPE: Impairs atg8-processing.
CC       {ECO:0000269|PubMed:23950735}.
CC   -!- SIMILARITY: Belongs to the WD repeat SVP1 family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 2 WD repeats. {ECO:0000305}.
DR   EMBL; CU329670; CAB90161.1; -; Genomic_DNA.
DR   RefSeq; NP_593843.1; NM_001019272.2.
DR   ProteinModelPortal; Q9P6N1; -.
DR   BioGrid; 279722; 1.
DR   MINT; MINT-4704393; -.
DR   PRIDE; Q9P6N1; -.
DR   EnsemblFungi; SPAC823.16c.1; SPAC823.16c.1:pep; SPAC823.16c.
DR   GeneID; 2543297; -.
DR   KEGG; spo:SPAC823.16c; -.
DR   EuPathDB; FungiDB:SPAC823.16c; -.
DR   PomBase; SPAC823.16c; -.
DR   InParanoid; Q9P6N1; -.
DR   OMA; NGASICE; -.
DR   OrthoDB; EOG092C3UKJ; -.
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; IDA:PomBase.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000407; C:pre-autophagosomal structure; IDA:PomBase.
DR   GO; GO:0034045; C:pre-autophagosomal structure membrane; IBA:GO_Central.
DR   GO; GO:0043234; C:protein complex; NAS:PomBase.
DR   GO; GO:0035091; F:phosphatidylinositol binding; ISO:PomBase.
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:0000045; P:autophagosome assembly; IBA:GO_Central.
DR   GO; GO:0006914; P:autophagy; IMP:PomBase.
DR   GO; GO:0016236; P:macroautophagy; IMP:PomBase.
DR   GO; GO:0000422; P:mitophagy; IBA:GO_Central.
DR   GO; GO:0044804; P:nucleophagy; IBA:GO_Central.
DR   GO; GO:0006497; P:protein lipidation; IBA:GO_Central.
DR   GO; GO:0034497; P:protein localization to pre-autophagosomal structure; 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; -; 2.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   SMART; SM00320; WD40; 2.
DR   SUPFAM; SSF50978; SSF50978; 2.
PE   1: Evidence at protein level;
KW   Autophagy; Complete proteome; Cytoplasm; Golgi apparatus; Membrane;
KW   Protein transport; Reference proteome; Repeat; Sporulation; Transport;
KW   Vacuole; WD repeat.
FT   CHAIN         1    335       Autophagy-related protein 21.
FT                                /FTId=PRO_0000050881.
FT   REPEAT      165    205       WD 1.
FT   REPEAT      210    249       WD 2.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       156    196       ismart:WD40 [T]
FT   MYHIT       199    240       ismart:WD40 [T]
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
//