RFX5_MOUSE
ID RFX5_MOUSE Reviewed; 658 AA.
AC Q9JL61; D3Z1N0; G3X9S6; Q3U180;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=DNA-binding protein Rfx5;
DE AltName: Full=Regulatory factor X 5;
GN Name=Rfx5;
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], FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=10779326; DOI=10.1128/mcb.20.10.3364-3376.2000;
RA Villard J., Peretti M., Masternak K., Barras E., Caretti G., Mantovani R.,
RA Reith W.;
RT "A functionally essential domain of RFX5 mediates activation of major
RT histocompatibility complex class II promoters by promoting cooperative
RT binding between RFX and NF-Y.";
RL Mol. Cell. Biol. 20:3364-3376(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 454-658.
RC STRAIN=NOD; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: Activates transcription from class II MHC promoters.
CC Recognizes X-boxes. Mediates cooperative binding between RFX and NF-Y.
CC RFX binds the X1 box of MHC-II promoters.
CC {ECO:0000269|PubMed:10779326}.
CC -!- SUBUNIT: Homodimer. The RFX heterotetrameric complex consists of 2
CC molecules of RFX5 and one each of RFXAP and RFX-B/RFXANK; with each
CC subunit representing a separate complementation group
CC (PubMed:10779326). Interacts (via PxLPxI/L motif) with RFXANK (via
CC ankyrin repeats); the interaction is direct (By similarity). RFX forms
CC cooperative DNA binding complexes with X2BP and CBF/NF-Y. RFX
CC associates with CIITA to form an active transcriptional complex
CC (PubMed:10779326). {ECO:0000250|UniProtKB:P48382,
CC ECO:0000269|PubMed:10779326}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00858,
CC ECO:0000269|PubMed:10779326}.
CC -!- DOMAIN: The N-terminus is required for dimer formation, association
CC with RFXANK and RFXAP, assembly of the RFX complex, and for binding of
CC this complex to its X box target site in the MHC-II promoter. The C-
CC terminus mediates cooperative binding between the RFX complex and NF-Y.
CC -!- DOMAIN: The PxLPxI/L motif mediates interaction with ankyrin repeats of
CC RFXANK. {ECO:0000250|UniProtKB:P48382}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RFX family. {ECO:0000255|PROSITE-
CC ProRule:PRU00858}.
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; AF209854; AAF68260.1; -; mRNA.
DR EMBL; AC087062; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466620; EDL38756.1; -; Genomic_DNA.
DR EMBL; BC118948; AAI18949.1; -; mRNA.
DR EMBL; BC118949; AAI18950.1; -; mRNA.
DR EMBL; AK156195; BAE33620.1; -; mRNA.
DR CCDS; CCDS17598.1; -.
DR RefSeq; NP_059091.2; NM_017395.2.
DR RefSeq; XP_006501757.1; XM_006501694.3.
DR RefSeq; XP_006501758.1; XM_006501695.3.
DR RefSeq; XP_011238466.1; XM_011240164.2.
DR RefSeq; XP_017175140.1; XM_017319651.1.
DR AlphaFoldDB; Q9JL61; -.
DR SMR; Q9JL61; -.
DR BioGRID; 207542; 8.
DR IntAct; Q9JL61; 8.
DR STRING; 10090.ENSMUSP00000117963; -.
DR iPTMnet; Q9JL61; -.
DR PhosphoSitePlus; Q9JL61; -.
DR EPD; Q9JL61; -.
DR jPOST; Q9JL61; -.
DR MaxQB; Q9JL61; -.
DR PaxDb; Q9JL61; -.
DR PeptideAtlas; Q9JL61; -.
DR PRIDE; Q9JL61; -.
DR ProteomicsDB; 255189; -.
DR Antibodypedia; 683; 299 antibodies from 34 providers.
DR DNASU; 53970; -.
DR Ensembl; ENSMUST00000029772; ENSMUSP00000029772; ENSMUSG00000005774.
DR Ensembl; ENSMUST00000107255; ENSMUSP00000102876; ENSMUSG00000005774.
DR Ensembl; ENSMUST00000107260; ENSMUSP00000102881; ENSMUSG00000005774.
DR Ensembl; ENSMUST00000137088; ENSMUSP00000117963; ENSMUSG00000005774.
DR GeneID; 53970; -.
DR KEGG; mmu:53970; -.
DR UCSC; uc008qhg.1; mouse.
DR CTD; 5993; -.
DR MGI; MGI:1858421; Rfx5.
DR VEuPathDB; HostDB:ENSMUSG00000005774; -.
DR eggNOG; KOG3712; Eukaryota.
DR GeneTree; ENSGT01050000244970; -.
DR HOGENOM; CLU_030500_0_0_1; -.
DR InParanoid; Q9JL61; -.
DR OMA; INMILPA; -.
DR OrthoDB; 67697at2759; -.
DR PhylomeDB; Q9JL61; -.
DR TreeFam; TF321340; -.
DR BioGRID-ORCS; 53970; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Rfx5; mouse.
DR PRO; PR:Q9JL61; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9JL61; protein.
DR Bgee; ENSMUSG00000005774; Expressed in vestibular ganglion and 236 other tissues.
DR ExpressionAtlas; Q9JL61; baseline and differential.
DR Genevisible; Q9JL61; MM.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO: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; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR003150; DNA-bd_RFX.
DR InterPro; IPR039779; RFX-like.
DR InterPro; IPR033486; RFX5.
DR InterPro; IPR029298; RFX5_C.
DR InterPro; IPR040889; RFX5_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12619; PTHR12619; 1.
DR PANTHER; PTHR12619:SF18; PTHR12619:SF18; 1.
DR Pfam; PF14621; RFX5_DNA_bdg; 1.
DR Pfam; PF18326; RFX5_N; 1.
DR Pfam; PF02257; RFX_DNA_binding; 1.
DR SMART; SM01306; RFX5_DNA_bdg; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51526; RFX_DBD; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P48382"
FT CHAIN 2..658
FT /note="DNA-binding protein Rfx5"
FT /id="PRO_0000419167"
FT DNA_BIND 91..167
FT /note="RFX-type winged-helix"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00858"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 24..89
FT /note="N-terminal domain"
FT /evidence="ECO:0000250"
FT REGION 61..65
FT /note="Leucine-rich region; critical for dimer formation
FT and for interaction with RFXAP"
FT /evidence="ECO:0000250"
FT REGION 250..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 172..177
FT /note="PxLPxI/L motif; mediates interaction with RFXANK"
FT /evidence="ECO:0000250|UniProtKB:P48382"
FT COMPBIAS 250..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..403
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P48382"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48382"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48382"
FT CONFLICT 569
FT /note="R -> Q (in Ref. 1; AAF68260 and 4; AAI18949/
FT AAI18950)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 658 AA; 69735 MW; E1807134D8FC4A19 CRC64;
MAEDKPDAKS PKTGARPQGG ADAGEPTTLL QRLRGTISKA VQNKVEGILQ EVQKFSDNDK
LYLYLQLPSG PSVGEKSSEP SLLSNEEYMY AYRWIRNHLE EHMDTCLPKQ SVYDAYRKYC
ESLACCRPLS TANFGKIIRE IFPDIKARRL GGRGQSKYCY SGIRRKTLVS MPPLPGLDLK
GSESPEMGPE VSPAPRDELV EAACALTCDW AERILKRSFS SIVQVARYLL QQHLISARSA
HAHVLKAGGL AEEDERAPRE RSLCKSKNVV ESLEGGGPKK PERPAQPPKE QEARAGTDLP
GRAERKKSVI DSSVPAASKP QVNALVARLP VLLPRAPRSL ITPISGTLKV ATLPLPTRVG
GPQTAVPIIN MILPPVPTLS GAGPGPGPGL GPRFGPGPGL GPGPGPGLGA GLGPGLGPGL
GAGPGPGLGA GLGAGLGLGP GRVPPRAPIL PRGAENREVG ISSDPRPHDK GIKRTAEVPL
SEASGQDPPV KEMKHETQDT TVSEAKRKRG RPRKKPGGSG ERNATPEKSA AIVNSPRSPR
LLWETWGSKR ENNFIGRPEG PGPGGEAERE TVLVQGQQDG AVSKGERSLS SQEAKEAEDK
IPPVTSKVSV IKGRIQKEAL QLVKGEADAA TQGNKGLKGR VLQSSLTPEH KDPKATPP
