CBF11_SCHPO
ID CBF11_SCHPO Reviewed; 613 AA.
AC O74954;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Transcription factor cbf11;
DE AltName: Full=C-promoter element-binding factor-like protein 11;
GN Name=cbf11; ORFNames=SPCC736.08;
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 [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).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP INDUCTION, SUBCELLULAR LOCATION, DNA-BINDING, DISRUPTION PHENOTYPE, AND
RP FUNCTION.
RX PubMed=19101542; DOI=10.1016/j.yexcr.2008.12.001;
RA Prevorovsky M., Grousl T., Stanurova J., Rynes J., Nellen W., Puta F.,
RA Folk P.;
RT "Cbf11 and Cbf12, the fission yeast CSL proteins, play opposing roles in
RT cell adhesion and coordination of cell and nuclear division.";
RL Exp. Cell Res. 315:1533-1547(2009).
CC -!- FUNCTION: Transcription factor that behaves as a negative regulator of
CC adhesion. Recognizes specifically the canonical CSL response element
CC GTGA/GGAA. May also play a cbf12-antagonistic role in the regulation of
CC a number of other important processes such as extracellular material
CC production, colony morphogenesis, ploidy maintenance, or meiosis.
CC {ECO:0000269|PubMed:19101542}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- INDUCTION: Expression is fairly constant throughout the growth phases
CC of haploid cells and similar mRNA levels were found in vegetative
CC diploid cells. {ECO:0000269|PubMed:19101542}.
CC -!- DISRUPTION PHENOTYPE: Leads to cold sensitivity, slow growth, and
CC altered colony morphology. {ECO:0000269|PubMed:19101542}.
CC -!- SIMILARITY: Belongs to the Su(H) family. {ECO:0000305}.
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DR EMBL; CU329672; CAA19272.1; -; Genomic_DNA.
DR PIR; T41565; T41565.
DR RefSeq; NP_587779.1; NM_001022772.2.
DR AlphaFoldDB; O74954; -.
DR SMR; O74954; -.
DR BioGRID; 276121; 308.
DR STRING; 4896.SPCC736.08.1; -.
DR iPTMnet; O74954; -.
DR MaxQB; O74954; -.
DR PaxDb; O74954; -.
DR PRIDE; O74954; -.
DR EnsemblFungi; SPCC736.08.1; SPCC736.08.1:pep; SPCC736.08.
DR GeneID; 2539560; -.
DR KEGG; spo:SPCC736.08; -.
DR PomBase; SPCC736.08; cbf11.
DR VEuPathDB; FungiDB:SPCC736.08; -.
DR eggNOG; KOG3743; Eukaryota.
DR HOGENOM; CLU_455048_0_0_1; -.
DR InParanoid; O74954; -.
DR OMA; CASNVAW; -.
DR PhylomeDB; O74954; -.
DR PRO; PR:O74954; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:PomBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:CACAO.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:PomBase.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:PomBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:PomBase.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:PomBase.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IMP:PomBase.
DR Gene3D; 2.60.40.1450; -; 1.
DR InterPro; IPR015350; Beta-trefoil_DNA-bd_dom.
DR InterPro; IPR036358; BTD_sf.
DR InterPro; IPR040159; CLS_fam.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR015351; RBP-J/Cbf11/Cbf12_DNA-bd.
DR InterPro; IPR037095; RBP-J/Cbf11_DNA-bd_sf.
DR PANTHER; PTHR10665; PTHR10665; 1.
DR Pfam; PF09270; BTD; 1.
DR Pfam; PF09271; LAG1-DNAbind; 1.
DR SMART; SM01268; BTD; 1.
DR SMART; SM01267; LAG1_DNAbind; 1.
DR SUPFAM; SSF110217; SSF110217; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cytoplasm; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..613
FT /note="Transcription factor cbf11"
FT /id="PRO_0000363405"
FT REGION 32..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 613 AA; 67173 MW; 5B6235FB6565CD2C CRC64;
MGDYFAWDFA NISGSNTSGS LNLNQLNLDN INNGLHNQED GAGGRNENSE RVGSGSPGSV
SMQVLSLFSA VNSALATLEK SEEFPSVVKD EQSIFPAVAK ASNSLDELAQ NIIPAPSPPG
FNRKRKTFDE DSSVEMIRRA ISDHLDLLNN CCIGIANLNE DSVHKISLTR SGKPSQLVTV
SCRHSSVIQK SYGSEKRYLC PPPMVYINGN YSSIFNQSFR TEISIMNDFG QCSQPISEEY
TGQGCMIFRS LHISSLVAAK SKNLRLSLDM FSNVNNQLLS HLVTSSISIV SKPSKKGSKL
KISNITLRSG SVVSLYNRIN SQTVRTKYTS IEAGQFCLRG DRWVPLRINL LLPDENGKLK
VCDDVDNPEP IKYGSIVELV DEATGTTSDP LIIRRVEKDH IAEEDGYVNQ MHRIVLESAY
PISNVRHLKI AEHSSLAYSN NISVRWFLGA TSAQNRNASS EAILPIEWEA VGNLSSNEMT
RVGDSVCWTI VGISHFDCTM MLPFNQNPVP TVTDYPYIEE PPEYLESSRS LQFKIGGYSV
GLQIWLGVHG PLSYSFTAAA DTSTMGTVTL GLSQISYDPS CAEQKYPLLF VIPGGIVIIG
KCEILLTSSA FGN
