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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}.
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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
 
 
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