BCL10_RAT
ID BCL10_RAT Reviewed; 233 AA.
AC Q9QYN5;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=B-cell lymphoma/leukemia 10;
DE AltName: Full=B-cell CLL/lymphoma 10 {ECO:0000303|PubMed:10753917};
DE Short=Bcl-10 {ECO:0000303|PubMed:10753917};
DE AltName: Full=R-RCD1;
DE Short=RCD;
GN Name=Bcl10 {ECO:0000303|PubMed:10753917, ECO:0000312|RGD:620544};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryonic brain;
RX PubMed=10753917; DOI=10.1074/jbc.275.15.11114;
RA Yoneda T., Imaizumi K., Maeda M., Yui D., Manabe T., Katayama T., Sato N.,
RA Gomi F., Morihara T., Mori Y., Miyoshi K., Hitomi J., Ugawa S., Yamada S.,
RA Okabe M., Tohyama M.;
RT "Regulatory mechanisms of TRAF2-mediated signal transduction by Bcl10, a
RT MALT lymphoma-associated protein.";
RL J. Biol. Chem. 275:11114-11120(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Plays a key role in both adaptive and innate immune signaling
CC by bridging CARD domain-containing proteins to immune activation. Acts
CC by channeling adaptive and innate immune signaling downstream of CARD
CC domain-containing proteins CARD9, CARD11 and CARD14 to activate NF-
CC kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14)
CC pathways which stimulate expression of genes encoding pro-inflammatory
CC cytokines and chemokines. Recruited by activated CARD domain-containing
CC proteins: homooligomerized CARD domain-containing proteins form a
CC nucleating helical template that recruits BCL10 via CARD-CARD
CC interaction, thereby promoting polymerization of BCL10, subsequent
CC recruitment of MALT1 and formation of a CBM complex. This leads to
CC activation of NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13
CC and/or MAPK14) pathways which stimulate expression of genes encoding
CC pro-inflammatory cytokines and chemokines. Activated by CARD9
CC downstream of C-type lectin receptors; CARD9-mediated signals are
CC essential for antifungal immunity. Activated by CARD11 downstream of T-
CC cell receptor (TCR) and B-cell receptor (BCR). Promotes apoptosis, pro-
CC caspase-9 maturation and activation of NF-kappa-B via NIK and IKK.
CC {ECO:0000250|UniProtKB:O95999}.
CC -!- SUBUNIT: Homomultimer; homooligomerized following recruitment by CARD
CC domain-containing proteins that form a nucleating helical template that
CC recruits BCL10 via CARD-CARD interaction. Self-associates by CARD-CARD
CC interaction and interacts with other CARD-proteins such as CARD9,
CC CARD10, CARD11 and CARD14. Forms a complex with CARD14 and MALT1;
CC resulting in the formation of a CBM (CARD14-BCL10-MALT1) complex. Forms
CC a complex with CARD11 and MALT1; resulting in the formation of a CBM
CC (CARD11-BCL10-MALT1) complex (By similarity). Forms a complex with
CC CARD9 and MALT1; resulting in the formation of a CBM (CARD9-BCL10-
CC MALT1) complex (By similarity). Found in a membrane raft complex, at
CC least composed of BCL10, CARD11, DPP4 and IKBKB. Binds caspase-9 with
CC its C-terminal domain. Interacts with TRAF2 and BIRC2/c-IAP2 (By
CC similarity). Interacts with PELI2 and SOCS3; these interactions may be
CC mutually exclusive (By similarity). {ECO:0000250|UniProtKB:O95999,
CC ECO:0000250|UniProtKB:Q9Z0H7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:O95999}. Membrane raft
CC {ECO:0000250|UniProtKB:O95999}. Note=Appears to have a perinuclear,
CC compact and filamentous pattern of expression. Also found in the
CC nucleus of several types of tumor cells. Colocalized with DPP4 in
CC membrane rafts. {ECO:0000250|UniProtKB:O95999}.
CC -!- PTM: Phosphorylated. Phosphorylation results in dissociation from TRAF2
CC and binding to BIRC2/c-IAP2. Phosphorylated by IKBKB/IKKB.
CC {ECO:0000250|UniProtKB:O95999}.
CC -!- PTM: Ubiquitinated via both 'Lys-63'-linked and linear ('Met-1'-linked)
CC polyubiquitin chains in response to T-cell receptor (TCR) activation.
CC Ubiquitination is recognized by IKBKG/NEMO, the regulatory subunit of
CC I-kappa-B kinase (IKK), and is required for TCR-induced NF-kappa-B
CC activation. Linear ubiquitination at Lys-17, Lys-31 and Lys-63 is
CC mediated by RNF31/HOIP; linear ubiquitination is recognized with much
CC higher affinity than 'Lys-63'-linked ubiquitin by IKBKG/NEMO. CARD11 is
CC required for linear ubiquitination by HOIP by promoting the targeting
CC of BCL10 to RNF31/HOIP. {ECO:0000250|UniProtKB:O95999}.
CC -!- PTM: Proteolytically cleaved by MALT1; required for T-cell activation.
CC {ECO:0000250|UniProtKB:O95999}.
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DR EMBL; AB016069; BAA88822.1; -; mRNA.
DR EMBL; BC061772; AAH61772.1; -; mRNA.
DR RefSeq; NP_112618.1; NM_031328.1.
DR AlphaFoldDB; Q9QYN5; -.
DR BMRB; Q9QYN5; -.
DR SMR; Q9QYN5; -.
DR BioGRID; 249715; 2.
DR STRING; 10116.ENSRNOP00000019911; -.
DR iPTMnet; Q9QYN5; -.
DR PhosphoSitePlus; Q9QYN5; -.
DR PaxDb; Q9QYN5; -.
DR Ensembl; ENSRNOT00000019911; ENSRNOP00000019911; ENSRNOG00000042389.
DR GeneID; 83477; -.
DR KEGG; rno:83477; -.
DR CTD; 8915; -.
DR RGD; 620544; Bcl10.
DR eggNOG; ENOG502RXGH; Eukaryota.
DR GeneTree; ENSGT00490000043442; -.
DR HOGENOM; CLU_103803_0_0_1; -.
DR InParanoid; Q9QYN5; -.
DR OMA; CRITQTK; -.
DR OrthoDB; 1472514at2759; -.
DR PhylomeDB; Q9QYN5; -.
DR Reactome; R-RNO-202424; Downstream TCR signaling.
DR Reactome; R-RNO-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-RNO-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-RNO-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR PRO; PR:Q9QYN5; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000042389; Expressed in jejunum and 20 other tissues.
DR Genevisible; Q9QYN5; RN.
DR GO; GO:0032449; C:CBM complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0001772; C:immunological synapse; ISO:RGD.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0002096; C:polkadots; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0050700; F:CARD domain binding; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0140296; F:general transcription initiation factor binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0019209; F:kinase activator activity; IEA:Ensembl.
DR GO; GO:0019900; F:kinase binding; ISS:UniProtKB.
DR GO; GO:0051059; F:NF-kappaB binding; ISS:UniProtKB.
DR GO; GO:0002020; F:protease binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISS:UniProtKB.
DR GO; GO:0043422; F:protein kinase B binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; ISS:UniProtKB.
DR GO; GO:0061760; P:antifungal innate immune response; ISS:UniProtKB.
DR GO; GO:0001783; P:B cell apoptotic process; ISO:RGD.
DR GO; GO:0008219; P:cell death; ISS:UniProtKB.
DR GO; GO:0006968; P:cellular defense response; ISO:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; ISO:RGD.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0002906; P:negative regulation of mature B cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0001843; P:neural tube closure; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:RGD.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISO:RGD.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISS:UniProtKB.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0050870; P:positive regulation of T cell activation; ISO:RGD.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0050856; P:regulation of T cell receptor signaling pathway; ISO:RGD.
DR GO; GO:0032094; P:response to food; ISS:UniProtKB.
DR GO; GO:0009620; P:response to fungus; ISO:RGD.
DR GO; GO:0070231; P:T cell apoptotic process; ISO:RGD.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; ISO:RGD.
DR CDD; cd08810; CARD_BCL10; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR033238; BCL10/E10.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR042143; CARD_BCL10.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR PANTHER; PTHR34920; PTHR34920; 1.
DR Pfam; PF00619; CARD; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR PROSITE; PS50209; CARD; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Adaptive immunity; Apoptosis; Cytoplasm; Immunity;
KW Innate immunity; Isopeptide bond; Membrane; Phosphoprotein;
KW Reference proteome; Tumor suppressor; Ubl conjugation.
FT CHAIN 1..233
FT /note="B-cell lymphoma/leukemia 10"
FT /id="PRO_0000144076"
FT DOMAIN 13..101
FT /note="CARD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT REGION 130..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 228..229
FT /note="Cleavage; by MALT1"
FT /evidence="ECO:0000250|UniProtKB:O95999"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O95999"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95999"
FT CROSSLNK 17
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O95999"
FT CROSSLNK 31
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O95999"
FT CROSSLNK 63
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O95999"
SQ SEQUENCE 233 AA; 25999 MW; B43274B4B825FC7D CRC64;
MEAPAPSLTE EDLTEVKKDA LENLRVYLCE KIIAERHFDH LRAKKILSRE DTEEISCRTS
SRKRAGKLLD YLQENPKGLD TLVESIRREK TQNFLIQKIT DEVLKLRNIK LEHLKGLKCS
SCEPFAAGAT NNLSRSNSDE SNFSEKQRPS TVIYHPEGES STAPFFSTES SLNLPVLEVG
RLENSSFSSA SLPRPGDPGA PPLPPDLRLE EGGSCGNSSE MFLPLRSRAL SRQ
