ID   RFX2_MACFA              Reviewed;         723 AA.
AC   Q4R3Z4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=DNA-binding protein RFX2;
DE   AltName: Full=Regulatory factor X 2;
GN   Name=RFX2; ORFNames=QtsA-13154;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcription factor that acts as a key regulator of
CC       spermatogenesis. Acts by regulating expression of genes required for
CC       the haploid phase during spermiogenesis, such as 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. Probably activates transcription of the testis-specific
CC       histone gene H1-6. {ECO:0000250|UniProtKB:P48379}.
CC   -!- SUBUNIT: Homodimer; probably only forms homodimers in testis.
CC       Heterodimer; heterodimerizes with RFX1 and RFX3.
CC       {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   -!- 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; AB179121; BAE02172.1; -; mRNA.
DR   AlphaFoldDB; Q4R3Z4; -.
DR   SMR; Q4R3Z4; -.
DR   STRING; 9541.XP_005587739.1; -.
DR   PRIDE; Q4R3Z4; -.
DR   eggNOG; KOG3712; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0001675; P:acrosome assembly; ISS:UniProtKB.
DR   GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0007286; P:spermatid development; ISS: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; 1.
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; Differentiation; DNA-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Spermatogenesis;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..723
FT                   /note="DNA-binding protein RFX2"
FT                   /id="PRO_0000380694"
FT   DNA_BIND        199..274
FT                   /note="RFX-type winged-helix"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00858"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          689..723
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..332
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        689..717
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         28
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48378"
FT   MOD_RES         416
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:B2GV50"
SQ   SEQUENCE   723 AA;  79865 MW;  A430D15041111C5E CRC64;
     MQNSEGGADS PASVALRPSA AAPPVPASPQ RVLVQAASSA PKGAQMQPVS LPRVQQVPQQ
     VQPAQHVYPA QVQYVEGGDA VYTNGAIRTA YTYNPEPQMY APSSAASYFE APGGAQVTVA
     ASSPPAVPSH SMVGITMDVG GSPIVSSTGA YLIHGGMDST RHSLAHTSRS SPATLEMAIE
     NLQKSEGITS HKSGLLNSHL QWLLDNYETA EGVSLPRSSL YNHYLRHCQE HKLDPVNAAS
     FGKLIRSVFM GLRTRRLGTR GNSKYHYYGI RLKPDSPLNR LQEDTQYMAM RQQPMHQKPR
     YRPAQKTDSL GDSGSHSSLH STPEQTMAAQ SQHHQQYIDV SHVFPEFPAP DLGSVLLQDG
     VTLHDVKALQ LVYRRHCEAT VDVVMNLQFH YIEKLWLSFW NSKASSSDGP TSLPASDEDP
     EGAVLPKDKL ISLCQCDPIL RWMRSCDHIL YQALVEILIP DVLRPVPSTL TQAIRNFAKS
     LEGWLTNAMS DFPQQVIQTK VGVVSAFAQT LRRYTSLNHL AQAARAVLQN TSQINQMLSD
     LNRVDFANVQ EQASWVCQCE ESVVQRLEQD FKLTLQQQSS LDQWASWLDS VVTQVLKQHA
     GSPSFPKAAR QFLLKWSFYS SMVIRDLTLR SAASFGSFHL IRLLYDEYMF YLVEHRVAEA
     TGETPIAVMG EFNDLASLSL TLLDKDDMGD ERRGSEAGPD AHSLGEPLVK RERSDPNHSL
     QGI