ID   CAL_BRARP               Reviewed;         254 AA.
AC   Q9SBK9;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Transcription factor CAULIFLOWER;
DE            Short=BcpCAL;
DE   AltName: Full=Agamous-like MADS-box protein CAL;
GN   Name=CAL;
OS   Brassica rapa subsp. pekinensis (Chinese cabbage) (Brassica pekinensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=51351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=cv. TT505; TISSUE=Leaf;
RX   PubMed=10765981; DOI=10.1038/sj.cr.7290033;
RA   Li X.F., Shen R.J., Liu P.L., Tang Z.C., He Y.K.;
RT   "Molecular characters and morphological genetics of CAL gene in Chinese
RT   cabbage.";
RL   Cell Res. 10:29-38(2000).
RN   [2]
RP   REVIEW, AND GENE FAMILY.
RX   PubMed=10835404; DOI=10.1093/genetics/155.2.855;
RA   Purugganan M.D., Boyles A.L., Suddith J.I.;
RT   "Variation and selection at the CAULIFLOWER floral homeotic gene
RT   accompanying the evolution of domesticated Brassica oleracea.";
RL   Genetics 155:855-862(2000).
CC   -!- FUNCTION: Probable transcription factor that promotes early floral
CC       meristem identity in synergy with APETALA1, FRUITFULL and LEAFY. Is
CC       required subsequently for the transition of an inflorescence meristem
CC       into a floral meristem. Seems to be partially redundant to the function
CC       of APETALA1. {ECO:0000269|PubMed:10765981}.
CC   -!- SUBUNIT: Homodimer capable of binding to CArG-box sequences.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
CC   -!- MISCELLANEOUS: CAULIFLOWER may contribute to the shape of the floral
CC       meristem. This trait has likely been selected by early farmers during
CC       the domestication of modified inflorescence structures.
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DR   EMBL; AJ251300; CAB61825.1; -; mRNA.
DR   AlphaFoldDB; Q9SBK9; -.
DR   SMR; Q9SBK9; -.
DR   STRING; 51351.Q9SBK9; -.
DR   eggNOG; KOG0014; Eukaryota.
DR   InParanoid; Q9SBK9; -.
DR   Proteomes; UP000011750; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0010582; P:floral meristem determinacy; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd00265; MADS_MEF2_like; 1.
DR   Gene3D; 3.40.1810.10; -; 1.
DR   InterPro; IPR033896; MADS_MEF2-like.
DR   InterPro; IPR002487; TF_Kbox.
DR   InterPro; IPR002100; TF_MADSbox.
DR   InterPro; IPR036879; TF_MADSbox_sf.
DR   Pfam; PF01486; K-box; 1.
DR   Pfam; PF00319; SRF-TF; 1.
DR   PRINTS; PR00404; MADSDOMAIN.
DR   SMART; SM00432; MADS; 1.
DR   SUPFAM; SSF55455; SSF55455; 1.
DR   PROSITE; PS51297; K_BOX; 1.
DR   PROSITE; PS00350; MADS_BOX_1; 1.
DR   PROSITE; PS50066; MADS_BOX_2; 1.
PE   2: Evidence at transcript level;
KW   Activator; Coiled coil; Developmental protein; Differentiation;
KW   DNA-binding; Flowering; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..254
FT                   /note="Transcription factor CAULIFLOWER"
FT                   /id="PRO_0000417147"
FT   DOMAIN          1..61
FT                   /note="MADS-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00251"
FT   DOMAIN          90..180
FT                   /note="K-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00629"
FT   REGION          182..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..205
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   254 AA;  29852 MW;  E9C35C6CBBAD0B87 CRC64;
     MGRGRVEMKR IENKINRQVT FSKRRAGLLK KAHEISILCD AEVSLIVFSH KGKLFEYSSE
     SCMEKVLERY ERYSYAEKQL KAPDSHVNAQ TNWSMEYSRL KAKIELLERN QRHYLGEDLE
     SISIKELQNL EQQLDTSLKH IRSRKNQLMH ESLNHLQRKE KEILEENSML TKQIKERESI
     LRTHQNQSEQ QNRSHHVAPQ PQPQLNPYMI SHQASPFLSM GGMYQGEDPT AVRRNRLDLT
     LEPIYNCNLG YFAA