BCL6_CHICK
ID BCL6_CHICK Reviewed; 708 AA.
AC Q5ZM39;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=B-cell lymphoma 6 protein homolog;
GN Name=BCL6 {ECO:0000250|UniProtKB:P41182}; ORFNames=RCJMB04_3d20;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000312|EMBL:CAG31204.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB {ECO:0000312|EMBL:CAG31204.1};
RC TISSUE=Bursa of Fabricius {ECO:0000312|EMBL:CAG31204.1};
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Transcriptional repressor mainly required for germinal center
CC (GC) formation and antibody affinity maturation which has different
CC mechanisms of action specific to the lineage and biological functions.
CC Forms complexes with different corepressors and histone deacetylases to
CC repress the transcriptional expression of different subsets of target
CC genes. Represses its target genes by binding directly to the DNA
CC sequence 5'-TTCCTAGAA-3' (BCL6-binding site) or indirectly by
CC repressing the transcriptional activity of transcription factors. In GC
CC B-cells, represses genes that function in differentiation,
CC inflammation, apoptosis and cell cycle control, also autoregulates its
CC transcriptional expression and up-regulates, indirectly, the expression
CC of some genes important for GC reactions, such as AICDA, through the
CC repression of microRNAs expression. An important function is to allow
CC GC B-cells to proliferate very rapidly in response to T-cell dependent
CC antigens and tolerate the physiological DNA breaks required for
CC immunglobulin class switch recombination and somatic hypermutation
CC without inducing a p53/TP53-dependent apoptotic response. In follicular
CC helper CD4(+) T-cells (T(FH) cells), promotes the expression of T(FH)-
CC related genes but inhibits the differentiation of T(H)1, T(H)2 and
CC T(H)17 cells. Also required for the establishment and maintenance of
CC immunological memory for both T- and B-cells. Suppresses macrophage
CC proliferation through competition with STAT5 for STAT-binding motifs
CC binding on certain target genes, such as CCL2 and CCND2. In response to
CC genotoxic stress, controls cell cycle arrest in GC B-cells in both
CC p53/TP53-dependedent and -independent manners. Besides, also controls
CC neurogenesis through the alteration of the composition of NOTCH-
CC dependent transcriptional complexes at selective NOTCH targets, such as
CC HES5, including the recruitment of the deacetylase SIRT1 and resulting
CC in an epigenetic silencing leading to neuronal differentiation (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P41183}.
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DR EMBL; AJ719545; CAG31204.1; -; mRNA.
DR RefSeq; NP_001012948.1; NM_001012930.1.
DR AlphaFoldDB; Q5ZM39; -.
DR SMR; Q5ZM39; -.
DR STRING; 9031.ENSGALP00000011884; -.
DR PaxDb; Q5ZM39; -.
DR GeneID; 424912; -.
DR KEGG; gga:424912; -.
DR CTD; 604; -.
DR VEuPathDB; HostDB:geneid_424912; -.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q5ZM39; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q5ZM39; -.
DR PRO; PR:Q5ZM39; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0030183; P:B cell differentiation; ISS:UniProtKB.
DR GO; GO:0000902; P:cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0048821; P:erythrocyte development; ISS:UniProtKB.
DR GO; GO:0002467; P:germinal center formation; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISS:UniProtKB.
DR GO; GO:0048294; P:negative regulation of isotype switching to IgE isotypes; ISS:UniProtKB.
DR GO; GO:0032764; P:negative regulation of mast cell cytokine production; ISS:UniProtKB.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0002829; P:negative regulation of type 2 immune response; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; ISS:UniProtKB.
DR GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0002682; P:regulation of immune system process; IBA:GO_Central.
DR GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0043380; P:regulation of memory T cell differentiation; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007266; P:Rho protein signal transduction; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR GO; GO:0042092; P:type 2 immune response; IBA:GO_Central.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 2: Evidence at transcript level;
KW Activator; DNA-binding; Immunity; Inflammatory response; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..708
FT /note="B-cell lymphoma 6 protein homolog"
FT /id="PRO_0000296300"
FT DOMAIN 32..99
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 520..543
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 548..570
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 576..598
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 604..626
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 632..654
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 660..683
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 303..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 708 AA; 79587 MW; DD2669821722CDCD CRC64;
MASPADSCIQ FTRHASDVLL NLNRLRSRDI LTDVVIIVNR EQFRAHKTVL MACSGLFYSI
FTDQLKCNLN VINLDPEINP EGFCILLDFM YTSRLNLREN NIMAVMATAL YLQMEHVVDT
CRRFVKSSEA EMVSAVKTPR EEFLAGRMLN HPEVMAYRGR DVSENSMPLQ NGSLCNGRAF
APGLFNSLPG SSISYPGYSP LPLNGFLVDD ELREMRMPLS ELSRVSAFPK ERIPCDGSRT
IPAEYMRTIT DISANMCHAT IYSPKEGAAE EARSDMHYSV ASGPKPVVPS IRNNPYFSCD
KVAKEEERTS SEDEISQHFE PTNTPLDRKG LISPQSPQKS DCQPNSPTES SSSKNARISQ
NSNSLFTKSP TDPKACNWKK YKFIVLNSLN QSTKQDSADQ NEMGTLSPRT YMPMSTCQQS
MEPEHLNVQS PTKMSVNGED SNIPQASRLN NIVNRSRDGS PRSSEGQSPL YMHSSKCSSC
GCQSPQHTEM CLHTSGSAFG EEMGETQSEY SDSSCENGAF FCNECDCRFS EEASLKRHSL
QVHSDKPYKC DRCQASFRYK GNLASHKTVH TGEKPYRCNI CGAQFNRPAN LKTHTRIHSG
EKPYKCETCG ARFVQVAHLR AHVLIHTGEK PYPCEICGTR FRHLQTLKSH LRIHTGEKPY
HCEKCNLHFR HKSQLRLHLR QKHGAITNTK VQYRISANEV PPELPKAC
