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RFX2_RAT
ID   RFX2_RAT                Reviewed;         692 AA.
AC   B2GV50;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=DNA-binding protein RFX2;
DE   AltName: Full=Regulatory factor X 2;
GN   Name=Rfx2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=15229132; DOI=10.1095/biolreprod.104.032268;
RA   Horvath G.C., Kistler W.S., Kistler M.K.;
RT   "RFX2 is a potential transcriptional regulatory factor for histone H1t and
RT   other genes expressed during the meiotic phase of spermatogenesis.";
RL   Biol. Reprod. 71:1551-1559(2004).
RN   [4]
RP   FUNCTION, AND DNA-BINDING.
RX   PubMed=14743396; DOI=10.1002/jcb.10748;
RA   Wolfe S.A., Wilkerson D.C., Prado S., Grimes S.R.;
RT   "Regulatory factor X2 (RFX2) binds to the H1t/TE1 promoter element and
RT   activates transcription of the testis-specific histone H1t gene.";
RL   J. Cell. Biochem. 91:375-383(2004).
RN   [5]
RP   FUNCTION, AND DNA-BINDING.
RX   PubMed=15526285; DOI=10.1002/jcb.20320;
RA   Grimes S.R., Prado S., Wolfe S.A.;
RT   "Transcriptional activation of the testis-specific histone H1t gene by RFX2
RT   may require both proximal promoter X-box elements.";
RL   J. Cell. Biochem. 94:317-326(2005).
RN   [6]
RP   FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=16676351; DOI=10.1002/jcb.20959;
RA   Wolfe S.A., van Wert J., Grimes S.R.;
RT   "Transcription factor RFX2 is abundant in rat testis and enriched in nuclei
RT   of primary spermatocytes where it appears to be required for transcription
RT   of the testis-specific histone H1t gene.";
RL   J. Cell. Biochem. 99:735-746(2006).
RN   [7]
RP   FUNCTION, AND DNA-BINDING.
RX   PubMed=18247329; DOI=10.1002/jcb.21694;
RA   VanWert J.M., Wolfe S.A., Grimes S.R.;
RT   "Binding of RFX2 and NF-Y to the testis-specific histone H1t promoter may
RT   be required for transcriptional activation in primary spermatocytes.";
RL   J. Cell. Biochem. 104:1087-1101(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Transcription factor that acts as a key regulator of
CC       spermatogenesis (By similarity). Acts by regulating expression of genes
CC       required for the haploid phase during spermiogenesis, such as genes
CC       required for cilium assembly and function (By similarity). Recognizes
CC       and binds the X-box, a regulatory motif with DNA sequence 5'-GTNRCC(0-
CC       3N)RGYAAC-3' present on promoters (PubMed:14743396, PubMed:15526285,
CC       PubMed:16676351, PubMed:18247329). Probably activates transcription of
CC       the testis-specific histone gene H1-6 (PubMed:14743396,
CC       PubMed:15526285, PubMed:16676351, PubMed:18247329).
CC       {ECO:0000250|UniProtKB:P48379, ECO:0000269|PubMed:14743396,
CC       ECO:0000269|PubMed:15526285, ECO:0000269|PubMed:16676351,
CC       ECO:0000269|PubMed:18247329}.
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:0000255|PROSITE-ProRule:PRU00858,
CC       ECO:0000269|PubMed:16676351}. Cytoplasm {ECO:0000269|PubMed:16676351}.
CC       Note=Mainly expressed in the nucleus and at lower level in cytoplasm.
CC       {ECO:0000269|PubMed:16676351}.
CC   -!- TISSUE SPECIFICITY: Expressed at highest level in testis. Expressed at
CC       lower level in thymus. Also expressed in stomach, kidney, liver, brain
CC       and heart. Weakly expressed in spleen and lung (PubMed:16676351).
CC       Within testis, most abundantly present in spermatocytes: present from
CC       pachytene spermatocytes to early spermatids (at protein level)
CC       (PubMed:15229132, PubMed:16676351). Also present in non-germinal
CC       tissues (PubMed:16676351). {ECO:0000269|PubMed:15229132,
CC       ECO:0000269|PubMed:16676351}.
CC   -!- SIMILARITY: Belongs to the RFX family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00858}.
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DR   EMBL; CH474092; EDL83603.1; -; Genomic_DNA.
DR   EMBL; BC166527; AAI66527.1; -; mRNA.
DR   RefSeq; NP_001100347.1; NM_001106877.1.
DR   AlphaFoldDB; B2GV50; -.
DR   SMR; B2GV50; -.
DR   STRING; 10116.ENSRNOP00000064610; -.
DR   iPTMnet; B2GV50; -.
DR   PhosphoSitePlus; B2GV50; -.
DR   PaxDb; B2GV50; -.
DR   PRIDE; B2GV50; -.
DR   Ensembl; ENSRNOT00000073025; ENSRNOP00000064610; ENSRNOG00000045846.
DR   GeneID; 301121; -.
DR   KEGG; rno:301121; -.
DR   CTD; 5990; -.
DR   RGD; 1588579; Rfx2.
DR   eggNOG; KOG3712; Eukaryota.
DR   GeneTree; ENSGT01050000244879; -.
DR   HOGENOM; CLU_010393_1_1_1; -.
DR   InParanoid; B2GV50; -.
DR   PhylomeDB; B2GV50; -.
DR   PRO; PR:B2GV50; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Proteomes; UP000234681; Chromosome 9.
DR   Bgee; ENSRNOG00000045846; Expressed in testis and 18 other tissues.
DR   ExpressionAtlas; B2GV50; baseline and differential.
DR   Genevisible; B2GV50; RN.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
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; IDA:UniProtKB.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR   GO; GO:0001675; P:acrosome assembly; ISS:UniProtKB.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR   GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA: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   1: Evidence at protein level;
KW   Cilium biogenesis/degradation; Cytoplasm; Differentiation; DNA-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Spermatogenesis;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..692
FT                   /note="DNA-binding protein RFX2"
FT                   /id="PRO_0000380696"
FT   DNA_BIND        169..244
FT                   /note="RFX-type winged-helix"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00858"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          261..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          660..692
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..296
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..686
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         26
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48378"
FT   MOD_RES         386
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   692 AA;  76537 MW;  AB5EA2C1105A8017 CRC64;
     MQNSEGGADS PATVALRPAA QPVPASPQRV LVQAAGSTPK GTPMQTLTLP RVQPVPPQVQ
     HVYPAQVQYV EGGDAVYANG AIRAAYTYNP DPQLYAPSSA ASYFETPGGA QVTVAASSPP
     AVPSHGMVGI TMDVSGTPIV SGAGTYLIHG GMDSTRHSLA HTARSSPATL QWLLDNYETA
     EGVSLPRSSL YNHYLRHCQE HKLEPVNAAS FGKLIRSVFM GLRTRRLGTR GNSKYHYYGI
     RLKPDSPLNR LQEDTQYMAM RQQPTHQKPR YRPAQKSDSL GDGSAHSNMH STPEQAMAAQ
     GQHHQQYIDV SHVFPEFPAP DLGSTLLQES VTLHDVKALQ LVYRRHCEAT LDVVMNLQFQ
     YIEKLWLSFW NCKATSSDGR ASLPASDEEP EVTLLPKDKL ISLCKCEPIL QWMRSCDHIL
     YQALVETLIP DVLRPVPSSL TQAIRNFAKS LEGWLINAMS GFPQQVIQTK VGVVSAFAQT
     LRRYTSLNHL AQAARAVLQN TSQINQMLSD LNRVDFANVQ EQASWVCQCE ESLVQRLEHD
     FKVTLQQQSS LDQWASWLDN VVTQVLKQHA GSPSFPKAAR QFLLKWSFYS SMVIRDLTLR
     SAASFGSFHL IRLLYDEYMF YLVEHRVAQA TGETPIAVMG EFNDLASLSL TLLDKEDIGD
     GHSSEADVDG RSLGEPLVKR ERSDPSHPLQ GI
 
 
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