ID NFKB1_CANFA STANDARD; PRT; 972 AA. AC Q6F3J0; DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 21-FEB-2006, entry version 14. DE Nuclear factor NF-kappa-B p105 subunit [Contains: Nuclear factor NF- DE kappa-B p50 subunit]. GN Name=NFKB1; OS Canis familiaris (Dog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Fissipedia; Canidae; OC Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Oguma K., Kano R., Hasegawa A.; RT "Canis familiaris nuclear factor of kappa light polypeptide gene RT enhancer in B-cells 1 (p105) (NFKB1), mRNA."; RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: P105 is the precursor of the p50 subunit of the nuclear CC factor NF-kappa-B, which binds to the kappa-B consensus sequence CC 5'-GGRNNYYCC-3', Located in the enhancer region of genes involved CC in immune response and acute phase reactions. The precursor CC protein itself does not bind to DNA (By similarity). CC -!- FUNCTION: NF-kappa-B p98 subunit (but not p84 or p105) acts as a CC transactivator of NF-kappa-B-regulated gene expression (By CC similarity). CC -!- SUBUNIT: Active NF-kappa-B is a heterodimer of an about 50 kDa CC DNA-binding subunit and the weak DNA-binding subunit p65. Two CC heterodimers might form a labile tetramer. Also interacts with CC MAP3K8. NF-kappa-B p50 subunit interacts with coactivator NCOA3, CC which may coactivate NF-kappa-B dependent expression via its CC histone acetyltransferase activity. Interacts with DSIPI; this CC interaction prevents nuclear translocation and DNA-binding (By CC similarity). CC -!- SUBCELLULAR LOCATION: Nuclear, but also found in the cytoplasm in CC an inactive form complexed to an inhibitor (I-kappa-B) (By CC similarity). CC -!- DOMAIN: The C-terminus of p105 might be involved in cytoplasmic CC retention, inhibition of DNA-binding by p50 homodimers, and/or CC transcription activation. CC -!- PTM: While translation occurs, the particular unfolded structure CC after the GRR repeat promotes the generation of p50 making it an CC acceptable substrate for the proteasome. This process is known as CC cotranslational processing. The processed form is active and the CC unprocessed form acts as an inhibitor (I kappa B-like), being able CC to form cytosolic complexes with NF-kappa B, trapping it in the CC cytoplasm. Complete folding of the region downstream of the GRR CC repeat precludes processing (By similarity). CC -!- SIMILARITY: Contains 7 ANK repeats. CC -!- SIMILARITY: Contains 1 death domain. CC -!- SIMILARITY: Contains 1 RHD (Rel-like) domain. 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; AB183419; BAD27479.1; -; mRNA. DR SMR; Q6F3J0; 1-82, 41-352. DR Ensembl; ENSCAFG00000010730; Canis familiaris. DR InterPro; IPR002110; ANK. DR InterPro; IPR000488; Death. DR InterPro; IPR011029; DEATH_like. DR InterPro; IPR002909; IPT_TIG_rcpt. DR InterPro; IPR000451; NF_Rel_dor. DR InterPro; IPR011539; RHD. DR Pfam; PF00023; Ank; 6. DR Pfam; PF00531; Death; 1. DR Pfam; PF00554; RHD; 1. DR Pfam; PF01833; TIG; 1. DR PRINTS; PR01415; ANKYRIN. DR PRINTS; PR00057; NFKBTNSCPFCT. DR SMART; SM00248; ANK; 5. DR SMART; SM00005; DEATH; 1. DR SMART; SM00429; IPT; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 5. DR PROSITE; PS50017; DEATH_DOMAIN; FALSE_NEG. DR PROSITE; PS01204; REL_1; 1. DR PROSITE; PS50254; REL_2; 1. KW Activator; ANK repeat; DNA-binding; Nuclear protein; Phosphorylation; KW Repeat; Transcription; Transcription regulation. FT CHAIN 1 972 Nuclear factor NF-kappa-B p105 subunit. FT /FTId=PRO_0000223240. FT CHAIN 1 433 Nuclear factor NF-kappa-B p50 subunit (By FT similarity). FT /FTId=PRO_0000223241. FT DOMAIN 39 246 RHD. FT REPEAT 539 568 ANK 1. FT REPEAT 578 607 ANK 2. FT REPEAT 611 640 ANK 3. FT REPEAT 647 676 ANK 4. FT REPEAT 681 711 ANK 5. FT REPEAT 715 744 ANK 6. FT REPEAT 768 798 ANK 7. FT DOMAIN 814 889 Death. FT REGION 372 394 GRR (By similarity). FT MOTIF 360 365 Nuclear localization signal (Potential). FT COMPBIAS 375 433 Gly-rich. FT SITE 433 434 Cleavage (when cotranslationally FT processed) (By similarity). FT MOD_RES 337 337 Phosphoserine (by PKA) (Potential). FT MOD_RES 931 931 Phosphoserine (By similarity). SQ SEQUENCE 972 AA; 105453 MW; 4B6472280209A09C CRC64; MAEDDTYLGA HEQMFHLDPL THTIFNPELF QPEMPLPTAD GPYLQILEQP KQRGFRFRYV CEGPSHGGLP GASSEKNKKS YPQVKICNYV GPAKVIVQLV TNGKNIHLHA HSLVGKHCED GICTVTAGPK DMVVGFANLG ILHVTKKKVF ETLEARMTEA CTKGYNPGLL VHPDLAYLQA EGGGDRQLTD REKEIIRQAA LQQTKEMDLS VVRLMFTAFL PDSTGSFTRR LEPVVSDAIY DSKAPNASNL KIVRMDRTAG CVTGGEEIYL LCDKVQKDDI QIRFYEEEGN GGIWGGFGDF SPTDVHRQFA IVFKTPKYKD VNITKPTSVF VQLRRKSDLE TSEPKPFLYY PEIKDKEEVQ RKRQKLMPNF SDSFGGGSGA GAGGGGMFGS GGGGGGAGST GPGYGFPHYG FPTYGGITFH PGTTKSNAGM KNGTIDTPSK NDSEGCGKNV DREAVNLSGK VTEPTEQDKE SSMGVDEVTL TYTVGIKEEN SRFQDNLFLE KAMQLAKRHA NALFDYAVTG DVKMLLAVQR HLTAVQDGNG DSVLHLAIIH LHAQLVRDLL EVTSGLISDD IINMRNDLYQ TPLHLAVITK QEAVVDDLLR AGADLSLLDR LGNSVLHLAA KEGQDKILSI LLKHKKAALL MDHPNGEGLN AIHIAVMSNS MPCLLLLVAA GADVNAQERK SGRTALHLAV EHDNISLAGC LLLEGDAHVD STTYDGTTPL HIAAGRGSTR LAALLKAAGA DPLVENFEPL YDLDDSWEKD GEDEGVVPGT TPLDMATNWQ VFDILNGKPY EPEFTSDDLL AQGDMKQLTE DAKLQLYKLL ETPDPDKNWA TLAQKLGQGI LNNAFRLSPA PSKTLMDNYE VSGGTIKELV EALRQMGYTE AIEVIQAAFC APETAAPSPG KGAPQTLSLP LSSASTRSPV DEVRDDSICD SGVETSFRRL SFTESLTSGS SLLTLNKAPH EYGQEGPIEG KI //