ID RFXK_MOUSE Reviewed; 269 AA. AC Q9Z205; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 185. DE RecName: Full=DNA-binding protein RFXANK; DE AltName: Full=Ankyrin repeat-containing adapter protein Tvl-1; DE AltName: Full=Regulatory factor X subunit B; DE Short=RFX-B; DE AltName: Full=Regulatory factor X-associated ankyrin-containing protein; GN Name=Rfxank; Synonyms=Rfxb, Tvl1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; TISSUE=Spleen; RX PubMed=9806546; DOI=10.1038/3081; RA Masternak K., Barras E., Zufferey M., Conrad B., Corthals G., Aebersold R., RA Sanchez J.-C., Hochstrasser D.F., Mach B., Reith W.; RT "A gene encoding a novel RFX-associated transactivator is mutated in the RT majority of MHC class II deficiency patients."; RL Nat. Genet. 20:273-277(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION RP WITH RAF1, SUBUNIT, DOMAIN, AND PHOSPHORYLATION. RC TISSUE=T-cell; RX PubMed=10329666; DOI=10.1074/jbc.274.21.14706; RA Lin J.-H., Makris A., McMahon C., Bear S.E., Patriotis C., Prasad V.R., RA Brent R., Golemis E.A., Tsichlis P.N.; RT "The ankyrin repeat-containing adaptor protein tvl-1 is a novel substrate RT and regulator of raf-1."; RL J. Biol. Chem. 274:14706-14715(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT). RC STRAIN=FVB/N; TISSUE=Salivary gland; 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: Activates transcription from class II MHC promoters. CC Activation requires the activity of the MHC class II CC transactivator/CIITA. May regulate other genes in the cell. RFX binds CC the X1 box of MHC-II promoters (By similarity). May also potentiate the CC activation of RAF1 (PubMed:10329666). {ECO:0000250|UniProtKB:O14593, CC ECO:0000269|PubMed:10329666}. CC -!- SUBUNIT: Forms homodimers (PubMed:10329666). The RFX heterotetrameric CC complex consists of 2 molecules of RFX5 and one each of RFXAP and RFX- CC B/RFXANK; with each subunit representing a separate complementation CC group. Interacts (via ankyrin repeats) with RFX5 (via PxLPxI/L motif); CC the interaction is direct. RFX forms cooperative DNA binding complexes CC with X2BP and CBF/NF-Y. RFX associates with CIITA to form an active CC transcriptional complex (By similarity). Interacts with RAF1 CC (PubMed:10329666). Interacts with RFX7 (By similarity). CC {ECO:0000250|UniProtKB:O14593, ECO:0000269|PubMed:10329666}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10329666}. Nucleus CC {ECO:0000269|PubMed:10329666}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=Q9Z205-1; Sequence=Displayed; CC Name=Short; CC IsoId=Q9Z205-2; Sequence=VSP_000285; CC -!- TISSUE SPECIFICITY: Expressed primarily in thymus, lung and testis. CC -!- DOMAIN: Interacts with RAF-1 via its C-terminal ankyrin repeat domain. CC The same domain also mediates its homodimerization (PubMed:10329666). CC The third ankyrin repeat is required for association with the two other CC RFX subunits; RFX5 and RFXAP. The three central ANK repeats mediate CC binding to the PxLPxI/L motif of RFX5 (By similarity). CC {ECO:0000250|UniProtKB:O14593, ECO:0000269|PubMed:10329666}. CC -!- PTM: Phosphorylated by RAF1. {ECO:0000269|PubMed:10329666}. 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; AF094761; AAC69884.1; -; mRNA. DR EMBL; AF123704; AAD24798.1; -; mRNA. DR EMBL; BC010971; AAH10971.1; -; mRNA. DR CCDS; CCDS22360.1; -. [Q9Z205-1] DR CCDS; CCDS85552.1; -. [Q9Z205-2] DR RefSeq; NP_001020760.1; NM_001025589.1. [Q9Z205-2] DR RefSeq; NP_035396.1; NM_011266.2. [Q9Z205-1] DR AlphaFoldDB; Q9Z205; -. DR SMR; Q9Z205; -. DR BioGRID; 202875; 7. DR IntAct; Q9Z205; 2. DR STRING; 10090.ENSMUSP00000148739; -. DR PhosphoSitePlus; Q9Z205; -. DR EPD; Q9Z205; -. DR MaxQB; Q9Z205; -. DR PaxDb; 10090-ENSMUSP00000075140; -. DR ProteomicsDB; 255317; -. [Q9Z205-1] DR ProteomicsDB; 255318; -. [Q9Z205-2] DR Antibodypedia; 15290; 399 antibodies from 21 providers. DR DNASU; 19727; -. DR Ensembl; ENSMUST00000075724.9; ENSMUSP00000075140.9; ENSMUSG00000036120.11. [Q9Z205-2] DR Ensembl; ENSMUST00000212320.2; ENSMUSP00000148739.2; ENSMUSG00000036120.11. [Q9Z205-1] DR GeneID; 19727; -. DR KEGG; mmu:19727; -. DR UCSC; uc009lyt.1; mouse. [Q9Z205-1] DR AGR; MGI:1333865; -. DR CTD; 8625; -. DR MGI; MGI:1333865; Rfxank. DR VEuPathDB; HostDB:ENSMUSG00000036120; -. DR eggNOG; KOG0502; Eukaryota. DR GeneTree; ENSGT00940000160753; -. DR HOGENOM; CLU_000134_23_0_1; -. DR InParanoid; Q9Z205; -. DR OMA; EQYMTAV; -. DR OrthoDB; 5477021at2759; -. DR PhylomeDB; Q9Z205; -. DR TreeFam; TF333112; -. DR BioGRID-ORCS; 19727; 5 hits in 80 CRISPR screens. DR ChiTaRS; Rfxank; mouse. DR PRO; PR:Q9Z205; -. DR Proteomes; UP000000589; Chromosome 8. DR RNAct; Q9Z205; Protein. DR Bgee; ENSMUSG00000036120; Expressed in granulocyte and 269 other cell types or tissues. DR ExpressionAtlas; Q9Z205; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0045171; C:intercellular bridge; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl. DR GO; GO:0042826; F:histone deacetylase binding; IDA:MGI. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0007265; P:Ras protein signal transduction; IPI:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR036770; Ankyrin_rpt-contain_sf. DR InterPro; IPR017362; DNA-bd_RFXANK. DR PANTHER; PTHR24124; ANKYRIN REPEAT FAMILY A; 1. DR PANTHER; PTHR24124:SF4; DNA-BINDING PROTEIN RFXANK; 1. DR Pfam; PF00023; Ank; 1. DR Pfam; PF12796; Ank_2; 1. DR PIRSF; PIRSF038034; DNA-binding_RFXANK; 1. DR SMART; SM00248; ANK; 4. DR SUPFAM; SSF48403; Ankyrin repeat; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 3. DR Genevisible; Q9Z205; MM. PE 1: Evidence at protein level; KW Activator; Alternative splicing; ANK repeat; Cytoplasm; DNA-binding; KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; KW Transcription regulation. FT CHAIN 1..269 FT /note="DNA-binding protein RFXANK" FT /id="PRO_0000067050" FT REPEAT 88..127 FT /note="ANK 1" FT REPEAT 132..161 FT /note="ANK 2" FT REPEAT 165..194 FT /note="ANK 3" FT REPEAT 198..227 FT /note="ANK 4" FT REPEAT 231..260 FT /note="ANK 5" FT REGION 1..36 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 112..121 FT /note="Missing (in isoform Short)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_000285" SQ SEQUENCE 269 AA; 29232 MW; 5713F335DC669E87 CRC64; MEPTQVAENL VPNQQPPVPD LEDPEDTRDE SPENSDTVVL SLFPCTPDAV NPEADASASS LQGSFLKHST TLTNRQRGNE VSALPATLDS LSIHQLAAQG ELSQLKDHLR KGACPACTCL SGNNLINKPD ERGFTPLIWA SAFGEIETVR FLLDWGADPH ILAKERESAL SLASMGGYTD IVRLLLDRDV DINIYDWNGG TPLLYAVRGN HVKCVEALLA RGADLTTEAD SGYTPMDLAV ALGYRKVQQV MESHILRLFQ STLGPVDPE //