ID   MDE4_SCHPO              Reviewed;         421 AA.
AC   O43068;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Monopolin complex subunit mde4;
DE   AltName: Full=Mei4-dependent protein 4;
GN   Name=mde4; ORFNames=SPBC6B1.04;
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, INTERACTION WITH PCS1, AND SUBCELLULAR LOCATION.
RX   PubMed=17627824; DOI=10.1016/j.cub.2007.06.044;
RA   Gregan J., Riedel C.G., Pidoux A.L., Katou Y., Rumpf C., Schleiffer A.,
RA   Kearsey S.E., Shirahige K., Allshire R.C., Nasmyth K.;
RT   "The kinetochore proteins Pcs1 and Mde4 and heterochromatin are required to
RT   prevent merotelic orientation.";
RL   Curr. Biol. 17:1190-1200(2007).
CC   -!- FUNCTION: The monopolin-like pcs1/mde4 complex is essential for
CC       accurate chromosome segregation during mitosis and meiosis II. May
CC       clamp together microtubule binding sites on the same kinetochore,
CC       preventing merotelic attachment of microtubules.
CC       {ECO:0000269|PubMed:17627824}.
CC   -!- SUBUNIT: Component of a monopolin-like complex composed of pcs1 and
CC       mde4. The complex associates with the kinetochore.
CC   -!- INTERACTION:
CC       O43068; O13684: pcs1; NbExp=3; IntAct=EBI-2211118, EBI-2211100;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17627824}.
CC       Chromosome, centromere {ECO:0000269|PubMed:17627824}. Note=Localizes to
CC       the central core of the centromere.
CC   -!- MISCELLANEOUS: Transcription is induced by mei4 transcription factor.
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DR   EMBL; CU329671; CAA17047.1; -; Genomic_DNA.
DR   PIR; T40645; T40645.
DR   RefSeq; NP_596083.1; NM_001021997.2.
DR   AlphaFoldDB; O43068; -.
DR   SMR; O43068; -.
DR   BioGRID; 277670; 18.
DR   DIP; DIP-47342N; -.
DR   IntAct; O43068; 3.
DR   STRING; 4896.SPBC6B1.04.1; -.
DR   iPTMnet; O43068; -.
DR   MaxQB; O43068; -.
DR   PaxDb; O43068; -.
DR   PRIDE; O43068; -.
DR   EnsemblFungi; SPBC6B1.04.1; SPBC6B1.04.1:pep; SPBC6B1.04.
DR   GeneID; 2541155; -.
DR   KEGG; spo:SPBC6B1.04; -.
DR   PomBase; SPBC6B1.04; mde4.
DR   VEuPathDB; FungiDB:SPBC6B1.04; -.
DR   HOGENOM; CLU_669318_0_0_1; -.
DR   OMA; ETEESNW; -.
DR   PRO; PR:O43068; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0034506; C:chromosome, centromeric core domain; IDA:PomBase.
DR   GO; GO:0072686; C:mitotic spindle; HDA:PomBase.
DR   GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR   GO; GO:0033551; C:monopolin complex; IDA:PomBase.
DR   GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IMP:PomBase.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0045144; P:meiotic sister chromatid segregation; IMP:PomBase.
DR   GO; GO:1990893; P:mitotic chromosome centromere condensation; IMP:PomBase.
DR   InterPro; IPR018479; Lrs4/Mde4.
DR   Pfam; PF10422; LRS4; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Centromere; Chromosome; Meiosis; Mitosis;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..421
FT                   /note="Monopolin complex subunit mde4"
FT                   /id="PRO_0000096323"
FT   REGION          122..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          224..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..238
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   421 AA;  47664 MW;  9D26F6A1BAAC5601 CRC64;
     MSTISTSTDS KLDNLGLSVT SRRNQILFYL SKALNLAHLL RSDSLQKSFL DALKQSATDS
     ELLHKNLDEI KFLQNEKLNN EKLLEQEQNE ANDYRLKVER LEHKISDYVQ EINSLNSQLQ
     IQKSNPEKHE DAVSQNRLRG SLDTVSSPSK THKANKDEKA TRLHLIIANL KKALKEKDAE
     VLNLQSHVSS KESELDRFKI KLETEESNWK VRLQVLESKL ATQDRKLRMQ KKSTERKSLL
     VSPRVSSPKL FSPSKQAIMG TRQPNATSGS PLSVTPFLQK TSTSIGLSSS PPQSSPSAQS
     SQPFSRDKYP HSMTVSPSNA RYLKKHLDDT IPSNVSDINH NDHLKIPQSP SSLSPSKIPI
     RKKRKLKDTV SNCEFTEEDS ESSFLLETIQ PTKSTLRRSI SPLKKRNDEI NELKKGFTMK
     K