ID   NFKB1_CANFA             Reviewed;         972 AA.
AC   Q6F3J0;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   24-JUL-2007, entry version 27.
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; Caniformia; 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.
CC       Interacts with SPAG9 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity). Note=Nuclear, but also found in the cytoplasm in an
CC       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.
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DR   EMBL; AB183419; BAD27479.1; -; mRNA.
DR   UniGene; Cfa.10766; -.
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; IPR013783; Ig-like_fold.
DR   InterPro; IPR002909; IPT_TIG_rcpt.
DR   InterPro; IPR000451; NF_Rel_dor.
DR   InterPro; IPR011539; RHD.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Gene3D; G3DSA:1.10.533.10; DEATH_like; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Gene3D; G3DSA:2.60.40.340; RHD; 1.
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; 6.
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.
PE   2: Evidence at transcript level;
KW   Activator; ANK repeat; Cytoplasm; DNA-binding; Nucleus;
KW   Phosphorylation; 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
//