ID   PUC1_SCHPO              Reviewed;         359 AA.
AC   P25009;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   27-MAR-2024, entry version 154.
DE   RecName: Full=Cyclin puc1;
GN   Name=puc1; ORFNames=SPBC19F5.01c, SPBP8B7.32c;
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=1828291; DOI=10.1038/351245a0;
RA   Forsburg S.L., Nurse P.;
RT   "Identification of a G1-type cyclin puc1+ in the fission yeast
RT   Schizosaccharomyces pombe.";
RL   Nature 351:245-247(1991).
RN   [2]
RP   ERRATUM OF PUBMED:1828291.
RA   Forsburg S.L., Nurse P.;
RL   Nature 352:648-648(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8006074;
RA   Forsburg S.L., Nurse P.;
RT   "Analysis of the Schizosaccharomyces pombe cyclin puc1: evidence for a role
RT   in cell cycle exit.";
RL   J. Cell Sci. 107:601-613(1994).
RN   [4]
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: Function in exit from the mitotic cycle. Contributes to
CC       negative regulation of the timing of sexual development in fission
CC       yeast, and functions at the transition between cycling and non-cycling
CC       cells. Interacts with protein kinase A.
CC   -!- SIMILARITY: Belongs to the cyclin family. {ECO:0000305}.
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DR   EMBL; X59154; CAA41868.1; -; Genomic_DNA.
DR   EMBL; X74451; CAA52460.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAA21817.1; -; Genomic_DNA.
DR   PIR; S15406; S15406.
DR   PIR; S36408; S36408.
DR   RefSeq; NP_596539.1; NM_001022460.2.
DR   AlphaFoldDB; P25009; -.
DR   SMR; P25009; -.
DR   BioGRID; 277179; 23.
DR   DIP; DIP-659N; -.
DR   STRING; 284812.P25009; -.
DR   iPTMnet; P25009; -.
DR   PaxDb; 4896-SPBC19F5-01c-1; -.
DR   EnsemblFungi; SPBC19F5.01c.1; SPBC19F5.01c.1:pep; SPBC19F5.01c.
DR   PomBase; SPBC19F5.01c; puc1.
DR   VEuPathDB; FungiDB:SPBC19F5.01c; -.
DR   eggNOG; KOG0653; Eukaryota.
DR   HOGENOM; CLU_771972_0_0_1; -.
DR   InParanoid; P25009; -.
DR   PhylomeDB; P25009; -.
DR   Reactome; R-SPO-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-SPO-69202; Cyclin E associated events during G1/S transition.
DR   PRO; PR:P25009; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005816; C:spindle pole body; IBA:GO_Central.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IGI:PomBase.
DR   GO; GO:0044843; P:cell cycle G1/S phase transition; IMP:PomBase.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR   GO; GO:0110045; P:negative regulation of cell cycle switching, mitotic to meiotic cell cycle; IGI:PomBase.
DR   GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; EXP:PomBase.
DR   GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IGI:PomBase.
DR   GO; GO:0023052; P:signaling; NAS:PomBase.
DR   CDD; cd20559; CYCLIN_ScCLN_like; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 2.
DR   InterPro; IPR039361; Cyclin.
DR   InterPro; IPR013763; Cyclin-like_dom.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR014399; Cyclin_CLN.
DR   InterPro; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10177; CYCLINS; 1.
DR   PANTHER; PTHR10177:SF523; G1_S-SPECIFIC CYCLIN CLN1-RELATED; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   PIRSF; PIRSF001770; Cyclin_CLN; 1.
DR   SMART; SM00385; CYCLIN; 1.
DR   SUPFAM; SSF47954; Cyclin-like; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cyclin; Reference proteome.
FT   CHAIN           1..359
FT                   /note="Cyclin puc1"
FT                   /id="PRO_0000080418"
SQ   SEQUENCE   359 AA;  40430 MW;  72DB0BB149041B4B CRC64;
     MLVSSNEEQL TAHTPTSSSS IEPKILAACS YSLSVGPCSL AVSPKGVNSK SPSLKNETAF
     VVDSVSTLSA ESSALLYNTQ SSLLTGLSMN GYLGEYQEDI IHHLITREKN FLLNVHLSNQ
     QPELRWSMRP ALVNFIVEIH NGFDLSIDTL PLSISLMDSY VSRRVVYCKH IQLVACVCLW
     IASKFHETED RVPLLQELKL ACKNIYAEDL FIRMERHILD TLDWDISIPT PASYIPVLDP
     IFFLVLDASM FVPNLFKFPA SKIACSVMNI VNEHVGSFLL THPSMESYRK DDNFLWPEDL
     DTVTSYMENM SKRYANEECT DLLFSSLGRI SSILAKKYPE QCAMAAWCNM TEKDTERTL
//