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 02-JUN-2021, entry version 135. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB016069; BAA88822.1; -; mRNA. DR EMBL; BC061772; AAH61772.1; -; mRNA. DR RefSeq; NP_112618.1; NM_031328.1. DR BMRB; Q9QYN5; -. DR BioGRID; 249715; 2. DR STRING; 10116.ENSRNOP00000019911; -. DR iPTMnet; Q9QYN5; -. DR PhosphoSitePlus; Q9QYN5; -. DR PaxDb; Q9QYN5; -. DR PRIDE; 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; MRPYLCD; -. 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 21 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: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:0008134; F:transcription factor binding; 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: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: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:0045893; P:positive regulation of transcription, DNA-templated; 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 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 //