ID   CCN1_ANTMA              Reviewed;         473 AA.
AC   P34800;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=G2/mitotic-specific cyclin-1;
OS   Antirrhinum majus (Garden snapdragon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Plantaginaceae; Antirrhineae; Antirrhinum.
OX   NCBI_TaxID=4151;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8313906; DOI=10.1002/j.1460-2075.1994.tb06299.x;
RA   Fobert P.R., Coen E.S., Murphy G.J.P., Doonan J.H.;
RT   "Patterns of cell division revealed by transcriptional regulation of genes
RT   during the cell cycle in plants.";
RL   EMBO J. 13:616-624(1994).
CC   -!- FUNCTION: Essential for the control of the cell cycle at the G2/M
CC       (mitosis) transition. G2/M cyclins accumulate steadily during G2 and
CC       are abruptly destroyed at mitosis.
CC   -!- SUBUNIT: Interacts with the CDC2 and CDK2 protein kinases to form a
CC       serine/threonine kinase holoenzyme complex. The cyclin subunit imparts
CC       substrate specificity to the complex.
CC   -!- DEVELOPMENTAL STAGE: Accumulates steadily during G2 and is abruptly
CC       destroyed at mitosis.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X76122; CAA53728.1; -; mRNA.
DR   PIR; S41709; S41709.
DR   AlphaFoldDB; P34800; -.
DR   SMR; P34800; -.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   CDD; cd00043; CYCLIN; 2.
DR   InterPro; IPR039361; Cyclin.
DR   InterPro; IPR013763; Cyclin-like.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10177; PTHR10177; 1.
DR   Pfam; PF02984; Cyclin_C; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   PIRSF; PIRSF001771; Cyclin_A_B_D_E; 1.
DR   SMART; SM00385; CYCLIN; 2.
DR   SMART; SM01332; Cyclin_C; 1.
DR   SUPFAM; SSF47954; SSF47954; 2.
DR   PROSITE; PS00292; CYCLINS; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cyclin; Mitosis.
FT   CHAIN           1..473
FT                   /note="G2/mitotic-specific cyclin-1"
FT                   /id="PRO_0000080389"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          134..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   473 AA;  52704 MW;  502CF1735587638A CRC64;
     MGSRNIVQQQ NRAEAAVPGA MKQKNIAGEK KNRRALGDIG NLVTVRGVDG KAKAIPQVSR
     PVTRSFCAQL LANAQTAAAD NNKINAKGAI VVDGVLPDRR VAAARVPAQK KAAVVKPRPE
     EIIVISPDSV AEKKEKPIEK EKAAEKSAKK KAPTLTSTLT ARSKAASGVK TKTKEQIVDI
     DAADVNNDLA VVEYVEDMYK FYKSVENESR PHDYMGSQPE INEKMRAILI DWLVQVHHKF
     ELSPETLYLT INIVDRYLAS ETTIRRELQL VGIGAMLIAS KYEEIWAPEV HELVCISDNT
     YSDKQILVME KKILGALEWY LTVPTPYVFL VRFIKASMTD SDVENMVYFL AELGMMNYAT
     LIYCPSMIAA ASVYAARCTL NKAPFWNETL QLHTGFSEPQ LMDCAKLLVA FPKMAGDQKL
     KSIYRKYSNL ERGAVALLSP AKSVFVFLIE LLMNAIEKIQ CSLFFTSEIW CRF