ID   DIMI_SCHPO              Reviewed;         142 AA.
AC   P87215;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 144.
DE   RecName: Full=Mitosis protein dim1;
GN   Name=dim1; ORFNames=SPCC16A11.05c;
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 [GENOMIC DNA].
RX   PubMed=9182666; DOI=10.1083/jcb.137.6.1337;
RA   Berry L.D., Gould K.L.;
RT   "Fission yeast dim1(+) encodes a functionally conserved polypeptide
RT   essential for mitosis.";
RL   J. Cell Biol. 137:1337-1354(1997).
RN   [2]
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   [3]
RP   INTERACTION WITH CUT20.
RX   PubMed=10082519; DOI=10.1128/mcb.19.4.2535;
RA   Berry L.D., Feoktistova A., Wright M.D., Gould K.L.;
RT   "The Schizosaccharomyces pombe dim1(+) gene interacts with the anaphase-
RT   promoting complex or cyclosome (APC/C) component lid1(+) and is required
RT   for APC/C function.";
RL   Mol. Cell. Biol. 19:2535-2546(1999).
CC   -!- FUNCTION: Plays a fundamental role as a protein essential for entry
CC       into mitosis (G2/M progression) as well as for chromosome segregation
CC       during mitosis. May play a role in mitotic spindle formation and/or
CC       function. May have a role in the maintenance or establishment of the
CC       steady-state level of the APC complex.
CC   -!- SUBUNIT: Interacts with cut20. {ECO:0000269|PubMed:10082519}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DIM1 family. {ECO:0000305}.
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DR   EMBL; AF001214; AAC49744.1; -; Genomic_DNA.
DR   EMBL; CU329672; CAB53077.1; -; Genomic_DNA.
DR   PIR; T41078; T41078.
DR   RefSeq; NP_587992.1; NM_001022983.2.
DR   AlphaFoldDB; P87215; -.
DR   SMR; P87215; -.
DR   BioGRID; 275935; 34.
DR   STRING; 4896.SPCC16A11.05c.1; -.
DR   MaxQB; P87215; -.
DR   PaxDb; P87215; -.
DR   EnsemblFungi; SPCC16A11.05c.1; SPCC16A11.05c.1:pep; SPCC16A11.05c.
DR   GeneID; 2539369; -.
DR   KEGG; spo:SPCC16A11.05c; -.
DR   PomBase; SPCC16A11.05c; dim1.
DR   VEuPathDB; FungiDB:SPCC16A11.05c; -.
DR   eggNOG; KOG3414; Eukaryota.
DR   HOGENOM; CLU_117348_0_0_1; -.
DR   OMA; DFNEMYE; -.
DR   PhylomeDB; P87215; -.
DR   Reactome; R-SPO-72165; mRNA Splicing - Minor Pathway.
DR   PRO; PR:P87215; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR   GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISS:PomBase.
DR   GO; GO:0005682; C:U5 snRNP; IBA:GO_Central.
DR   GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISS:PomBase.
DR   CDD; cd02954; DIM1; 1.
DR   InterPro; IPR004123; Dim1.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR12052; PTHR12052; 1.
DR   Pfam; PF02966; DIM1; 1.
DR   PIRSF; PIRSF017199; mRNA_splic_U5; 1.
DR   SMART; SM01410; DIM1; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   1: Evidence at protein level;
KW   mRNA processing; mRNA splicing; Nucleus; Reference proteome.
FT   CHAIN           1..142
FT                   /note="Mitosis protein dim1"
FT                   /id="PRO_0000218285"
SQ   SEQUENCE   142 AA;  16971 MW;  2F1A393FBCBBCEBF CRC64;
     MSYFLPHLHS GWHVDQAILS EQERLVVIRF GRDHDEECIK QDEVLYRIAE KVVNMAVIYL
     VDIDEVPDFN KMYELYDRTT IMFFYRNKHM MIDLGTGNNN KINWPLEDKQ EMIDIIETIF
     RGARKGKGLV ISPKDYSTRH RY