ID   CG12_CANAX              Reviewed;         465 AA.
AC   P43062;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=G1/S-specific cyclin CLN2;
GN   Name=CLN2;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SGY126;
RX   PubMed=7830719; DOI=10.1007/bf00297278;
RA   Sherlock G., Bahman A.M., Mahal A., Shieh J.C., Ferreira M., Rosamond J.;
RT   "Molecular cloning and analysis of CDC28 and cyclin homologues from the
RT   human fungal pathogen Candida albicans.";
RL   Mol. Gen. Genet. 245:716-723(1994).
CC   -!- FUNCTION: Essential for the control of the cell cycle at the G1/S
CC       (start) transition. Interacts with the CDC28 protein kinase to form MPF
CC       (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclin family. {ECO:0000305}.
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DR   EMBL; X80033; CAA56337.1; -; Genomic_DNA.
DR   PIR; S51613; S51613.
DR   AlphaFoldDB; P43062; -.
DR   SMR; P43062; -.
DR   VEuPathDB; FungiDB:C5_01100C_A; -.
DR   VEuPathDB; FungiDB:CAWG_04499; -.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:UniProt.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IEA:InterPro.
DR   CDD; cd00043; CYCLIN; 1.
DR   InterPro; IPR028857; CCNF_metazoan.
DR   InterPro; IPR039361; Cyclin.
DR   InterPro; IPR013763; Cyclin-like.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR014399; Cyclin_CLN.
DR   InterPro; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10177; PTHR10177; 1.
DR   PANTHER; PTHR10177:SF252; PTHR10177:SF252; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   PIRSF; PIRSF001770; Cyclin_CLN; 1.
DR   SMART; SM00385; CYCLIN; 1.
DR   SUPFAM; SSF47954; SSF47954; 1.
DR   PROSITE; PS00292; CYCLINS; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cyclin.
FT   CHAIN           1..465
FT                   /note="G1/S-specific cyclin CLN2"
FT                   /id="PRO_0000080415"
SQ   SEQUENCE   465 AA;  53177 MW;  97CC07FB3A07C230 CRC64;
     MFPNSPDAFH QVRMMQSSIK ASNFKLQSME FRCHSNNVCE YQMEMLHHLL SVEAKTLPSL
     SLIEQQPEIK LGMRPLLLDF LMEVITILNL SRSTFPLTVN LIDRYCSTRI VKKQHYQLLG
     LTSLWISCKN LDSKFKVPTL NDLRKICVDS YYKELFVEME KHILKSLEWV VNAPTFDAFI
     DLYSNLLISN SSNFEVANII KKSSHKIKLF SNYIGELFQF YPNIYYDYTS SQIALIAILI
     TVLTLKIPVD LISLLNFYNG LVKTEMFKSN VEQGAEDQFE EILSVDSFKS LFNKSFFKNL
     IKIIDNPPSS LKIKYFAENG KYSVLMKQLV TTASNTLKCI LDPVPTTPKA NSFVKHQQQQ
     HHYHPRPPMS INTSMIPLTP VSNSTSPNRF SPDQIFSENE STPGIAFGTM TPDSQSTSPG
     EKRSYECIDE LEIGTSTIAG YTLKNHDTLK RSKSANYGTL FYLQQ