MUG66_SCHPO
ID MUG66_SCHPO Reviewed; 184 AA.
AC O13978;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Meiotically up-regulated gene 66 protein;
DE AltName: Full=Autophagy-related protein 101;
GN Name=mug66; Synonyms=atg101; ORFNames=SPAC25H1.03;
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/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: Autophagy factor required for autophagosome formation (By
CC similarity). Has a role in meiosis and sporulation. {ECO:0000250,
CC ECO:0000269|PubMed:16303567}.
CC -!- INTERACTION:
CC O13978; O36019: atg13; NbExp=6; IntAct=EBI-16158557, EBI-16158534;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Preautophagosomal structure
CC membrane; Peripheral membrane protein.
CC -!- DISRUPTION PHENOTYPE: Impairs atg8-processing.
CC {ECO:0000269|PubMed:23950735}.
CC -!- SIMILARITY: Belongs to the ATG101 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAB11600.1; -; Genomic_DNA.
DR PIR; T38383; T38383.
DR RefSeq; NP_593807.1; NM_001019236.2.
DR PDB; 4YK8; X-ray; 3.00 A; A=1-184.
DR PDBsum; 4YK8; -.
DR AlphaFoldDB; O13978; -.
DR SMR; O13978; -.
DR BioGRID; 279174; 19.
DR DIP; DIP-61610N; -.
DR IntAct; O13978; 1.
DR STRING; 4896.SPAC25H1.03.1; -.
DR PaxDb; O13978; -.
DR EnsemblFungi; SPAC25H1.03.1; SPAC25H1.03.1:pep; SPAC25H1.03.
DR GeneID; 2542723; -.
DR KEGG; spo:SPAC25H1.03; -.
DR PomBase; SPAC25H1.03; -.
DR VEuPathDB; FungiDB:SPAC25H1.03; -.
DR eggNOG; KOG4493; Eukaryota.
DR HOGENOM; CLU_069661_1_1_1; -.
DR InParanoid; O13978; -.
DR OMA; VCWEIWT; -.
DR PhylomeDB; O13978; -.
DR Reactome; R-SPO-1632852; Macroautophagy.
DR PRO; PR:O13978; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IDA:PomBase.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0000045; P:autophagosome assembly; IMP:PomBase.
DR GO; GO:0016236; P:macroautophagy; IMP:PomBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR012445; ATG101.
DR PANTHER; PTHR13292; PTHR13292; 1.
DR Pfam; PF07855; ATG101; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Cytoplasm; Meiosis; Membrane; Nucleus;
KW Protein transport; Reference proteome; Sporulation; Transport.
FT CHAIN 1..184
FT /note="Meiotically up-regulated gene 66 protein"
FT /id="PRO_0000278502"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:4YK8"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:4YK8"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:4YK8"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:4YK8"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:4YK8"
FT HELIX 54..73
FT /evidence="ECO:0007829|PDB:4YK8"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:4YK8"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:4YK8"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:4YK8"
FT STRAND 103..113
FT /evidence="ECO:0007829|PDB:4YK8"
FT HELIX 119..137
FT /evidence="ECO:0007829|PDB:4YK8"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:4YK8"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:4YK8"
SQ SEQUENCE 184 AA; 20318 MW; 9F08647CBF182A6B CRC64;
MTNTVTIELK IGYKYAAEVV KAVLGVILFH RQFSTVPART IDVLDITVPT LVGAELNEQL
ATKAAEFIDT IRNEAGANGQ MILLLYERSP KKSWFGKGNT IPWEQWILHT TILEEGDSYQ
ESSLSLEAAV EQIVQAVNLR SLSYLPPVAM DSGNYPYEIV TPTSTEGWGS LLKRMIIENV
SGGD