ID   WOS2_SCHPO              Reviewed;         186 AA.
AC   Q11118;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Protein wos2;
DE   AltName: Full=p21;
GN   Name=wos2; ORFNames=SPAC9E9.13;
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 [MRNA].
RC   STRAIN=972 / ATCC 24843;
RA   Munoz M., Bejarano E.R., Jimenez J.;
RT   "The identification of p21wos2, a novel cell cycle regulatory protein which
RT   closely interacts with p34cdc2 in the control of the M/G1 transition.";
RL   Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
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).
CC   -!- FUNCTION: Cell cycle regulatory protein that interacts with cdc2 in the
CC       control of the M-G1 transition.
CC   -!- SIMILARITY: Belongs to the p23/wos2 family. {ECO:0000305}.
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DR   EMBL; L41166; AAA64891.1; -; mRNA.
DR   EMBL; CU329670; CAB16411.1; -; Genomic_DNA.
DR   PIR; T39220; T39220.
DR   RefSeq; NP_594586.1; NM_001020015.2.
DR   AlphaFoldDB; Q11118; -.
DR   SMR; Q11118; -.
DR   BioGRID; 278933; 20.
DR   STRING; 4896.SPAC9E9.13.1; -.
DR   iPTMnet; Q11118; -.
DR   MaxQB; Q11118; -.
DR   PaxDb; Q11118; -.
DR   PRIDE; Q11118; -.
DR   EnsemblFungi; SPAC9E9.13.1; SPAC9E9.13.1:pep; SPAC9E9.13.
DR   GeneID; 2542472; -.
DR   KEGG; spo:SPAC9E9.13; -.
DR   PomBase; SPAC9E9.13; wos2.
DR   VEuPathDB; FungiDB:SPAC9E9.13; -.
DR   eggNOG; KOG3158; Eukaryota.
DR   HOGENOM; CLU_078883_0_1_1; -.
DR   InParanoid; Q11118; -.
DR   OMA; DDYANNF; -.
DR   PhylomeDB; Q11118; -.
DR   Reactome; R-SPO-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR   Reactome; R-SPO-3371511; HSF1 activation.
DR   PRO; PR:Q11118; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0051087; F:chaperone binding; ISO:PomBase.
DR   GO; GO:0051879; F:Hsp90 protein binding; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   Gene3D; 2.60.40.790; -; 1.
DR   InterPro; IPR007052; CS_dom.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   InterPro; IPR045250; p23-like.
DR   PANTHER; PTHR22932; PTHR22932; 1.
DR   Pfam; PF04969; CS; 1.
DR   SUPFAM; SSF49764; SSF49764; 1.
DR   PROSITE; PS51203; CS; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Reference proteome.
FT   CHAIN           1..186
FT                   /note="Protein wos2"
FT                   /id="PRO_0000218958"
FT   DOMAIN          5..101
FT                   /note="CS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT   REGION          121..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   186 AA;  20951 MW;  77A3CEE60C266265 CRC64;
     MSLNTQIPEV LWAQRSNKDD AEKNVIYLTV LIPDAVDPKI NLTPEKLVID SKSGANAHYA
     VQIDFFKDID VEKSKYSVTG RYIFFVLYKK ELQEEFWPRL TKEKLRLHWL RTDFDRWVDE
     DEQEAQPEVS PFGAGGMPDL SALGGMGGMD FSQFGNLGGA GAGEDASDSE PELEEEEEVG
     SNEKKE