RFX2_XENLA
ID RFX2_XENLA Reviewed; 694 AA.
AC Q32NR3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=DNA-binding protein RFX2;
DE AltName: Full=Regulatory factor X 2;
GN Name=rfx2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22227339; DOI=10.1016/j.ydbio.2011.12.029;
RA Chung M.I., Peyrot S.M., LeBoeuf S., Park T.J., McGary K.L., Marcotte E.M.,
RA Wallingford J.B.;
RT "RFX2 is broadly required for ciliogenesis during vertebrate development.";
RL Dev. Biol. 363:155-165(2012).
RN [3]
RP FUNCTION.
RX PubMed=24424412; DOI=10.7554/elife.01439;
RA Chung M.I., Kwon T., Tu F., Brooks E.R., Gupta R., Meyer M., Baker J.C.,
RA Marcotte E.M., Wallingford J.B.;
RT "Coordinated genomic control of ciliogenesis and cell movement by RFX2.";
RL Elife 3:E01439-E01439(2014).
CC -!- FUNCTION: Transcription factor that acts as a key regulator of
CC ciliogenesis. Specifically regulates expression of genes required for
CC cilium assembly and function. Recognizes and binds the X-box, a
CC regulatory motif with DNA sequence 5'-GTNRCC(0-3N)RGYAAC-3' present on
CC promoters (PubMed:22227339, PubMed:24424412). Required for neural tube
CC closure and neural ciliogenesis (PubMed:22227339).
CC {ECO:0000269|PubMed:22227339, ECO:0000269|PubMed:24424412}.
CC -!- SUBUNIT: Homodimer. Heterodimer; heterodimerizes with other rfx
CC proteins. {ECO:0000250|UniProtKB:P48379}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:B2GV50,
CC ECO:0000255|PROSITE-ProRule:PRU00858}. Cytoplasm
CC {ECO:0000250|UniProtKB:B2GV50}. Note=Mainly expressed in the nucleus
CC and at lower level in cytoplasm. {ECO:0000250|UniProtKB:B2GV50}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in ciliated tissues, such
CC as neural tube, gastrocoel roof plate, epidermal multiciliated cells,
CC otic vesicles and kidneys. {ECO:0000269|PubMed:22227339}.
CC -!- SIMILARITY: Belongs to the RFX family. {ECO:0000255|PROSITE-
CC ProRule:PRU00858}.
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DR EMBL; BC108517; AAI08518.1; -; mRNA.
DR RefSeq; NP_001090132.1; NM_001096663.1.
DR AlphaFoldDB; Q32NR3; -.
DR SMR; Q32NR3; -.
DR DNASU; 735210; -.
DR GeneID; 735210; -.
DR KEGG; xla:735210; -.
DR CTD; 735210; -.
DR Xenbase; XB-GENE-991777; rfx2.S.
DR OrthoDB; 346630at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 735210; Expressed in testis and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IDA:UniProtKB.
DR GO; GO:0001843; P:neural tube closure; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR003150; DNA-bd_RFX.
DR InterPro; IPR039779; RFX-like.
DR InterPro; IPR007668; RFX1_trans_act.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12619; PTHR12619; 2.
DR Pfam; PF04589; RFX1_trans_act; 1.
DR Pfam; PF02257; RFX_DNA_binding; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51526; RFX_DBD; 1.
PE 2: Evidence at transcript level;
KW Cilium biogenesis/degradation; Cytoplasm; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..694
FT /note="DNA-binding protein RFX2"
FT /id="PRO_0000380698"
FT DNA_BIND 174..249
FT /note="RFX-type winged-helix"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00858"
FT REGION 267..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 694 AA; 77784 MW; 5B0E1730A920F24D CRC64;
MQNSDSGSDS ATSVALRTST SAQAPVVQPV PASQQVQTVQ HVYPAQVQYV EGDTVYTNGA
IRTAYSYNAE TQIYAPSSGS SYFDSQGGGA QVTTVVSSPT AIPSHSMVGI TMDVSGSQII
SSSGAYLIHG GLENSRHTPS HTSRTFPATL EMAIENLQKN EGITSHKSSL LNSHLQWLLD
NYETAEGVSL PRSSLYNHYL RHCQDHKLDP VNAASFGKLI RSVFMGLRTR RLGTRGNSKY
HYYGIRLKPD SPLNRIQEDA QYMAIRQQPI HQKQRYRPAQ KIDGMGENPA NSSQHASPEQ
SVAAQSQHHQ QFIDTSHVFP DFPAPDLGSL LLPEGITMTD IKNLQLMYRR HCEATIDVVM
NLQFQYIEKL WQAFWNSKPS SPDGSNPMSS EDEQEPIIPN EKLMVLCKYE PIMRWMRNCD
HILYQALVEI LIPDVLRPVP STLTQAIRNF AKSLEGWLTN AMCDFPQQIV HAKVGVVSAF
AQTLRRYTSL NHLAQAARAV LQNTSQINQM LSDLNRVDFA NVQEQASWVC QCDEGMVQKL
EQDFKLTLQQ QSSLDQWANW LDNVVTQVLK PHEGSTSFPK AARQFLLKWS FYSSMVIRDL
TLRSAASFGS FHLIRLLYDE YMFYLVEHRV AQATGETPIA VMGEFSDFAS MSPVQMDKDD
VSELGSDTEG DPHISGQPPV KRERVELNHS MQEM