ID MUG72_SCHPO Reviewed; 574 AA.
AC Q9Y7P6; Q9UTU8;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE RecName: Full=Meiotically up-regulated gene 72 protein;
GN Name=mug72; ORFNames=SPCC1902.02, SPCC663.16c;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 357-536, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
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 [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-343 AND SER-392, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Has a role in meiosis. {ECO:0000269|PubMed:16303567}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:16823372}. Note=Localizes at the cell tip and
CC barrier septum.
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DR EMBL; CU329672; CAB40004.1; -; Genomic_DNA.
DR EMBL; AB027984; BAA87288.1; -; Genomic_DNA.
DR PIR; T41207; T41207.
DR RefSeq; NP_588277.1; NM_001023267.3.
DR AlphaFoldDB; Q9Y7P6; -.
DR SMR; Q9Y7P6; -.
DR BioGRID; 275899; 8.
DR STRING; 284812.Q9Y7P6; -.
DR iPTMnet; Q9Y7P6; -.
DR MaxQB; Q9Y7P6; -.
DR PaxDb; 4896-SPCC1902-02-1; -.
DR EnsemblFungi; SPCC1902.02.1; SPCC1902.02.1:pep; SPCC1902.02.
DR GeneID; 2539333; -.
DR KEGG; spo:SPCC1902.02; -.
DR PomBase; SPCC1902.02; mug72.
DR VEuPathDB; FungiDB:SPCC1902.02; -.
DR eggNOG; ENOG502QT3Z; Eukaryota.
DR HOGENOM; CLU_471855_0_0_1; -.
DR InParanoid; Q9Y7P6; -.
DR OMA; STKWKPD; -.
DR PhylomeDB; Q9Y7P6; -.
DR PRO; PR:Q9Y7P6; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
DR PANTHER; PTHR21708:SF44; MEIOTICALLY UP-REGULATED GENE 72 PROTEIN; 1.
DR PANTHER; PTHR21708; PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR Pfam; PF02558; ApbA; 1.
DR Pfam; PF08546; ApbA_C; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Meiosis; Phosphoprotein; Reference proteome.
FT CHAIN 1..574
FT /note="Meiotically up-regulated gene 72 protein"
FT /id="PRO_0000116550"
FT REGION 339..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 343
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 358..364
FT /note="PVGAASR -> SGCLPHG (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 574 AA; 62847 MW; 6A4D8DF5F4858F92 CRC64;
MSEEDTSKLR ILSVGSNAIS AFISWRLSES KACHTTLIWR NRCESVLSEG IRIRSSVFGS
TKWKPDVVAP TVEQLAMNSE PFDYIFVCLK ILPSVYNLDT AIKEVVTPGH TCIVLNTTGI
VGAEKELQHA FPNNPVLSFV LPDQFAQRGP LQFEHTTFAA DSAKSVIYVG LTEEEDDVPD
SVQDAMIETL TLTLEAGGVS CDFLSKIQKK QWETGVGHMC FYPLSIINDE PNLALMYRLK
SFAKVIDGLM DEAFSIAQAQ GCEFEPEKLD VLKRHIVNRM LATPRPSYPY QDYIAHRPLE
VAVLLGYPVE IAKELGVSVP RMETLLALFD AKNKRNLTVR AGTPQSSPNF NPAMRRSPVG
AASRSPSRST IGISNRIGSV DDLLNTRQFT SSPIGGSMPK GPNSIYKIPS ASMVNLSSPL
VTSPSGLNPT GRPSRFGGRV RGNPLTMNKA GSVSDLLSTS TNMASSDALE TASMIGVPSA
MPPNSFDMLT LTQRRNRRNN QSSSPPAPSD RRYTMGARRP VQTRGMTDSV IPILEDPMST
LYDTSRYPTR NSKPATPKAS RPPSIASTVH RRMD
//
