PO4F2_RAT
ID PO4F2_RAT Reviewed; 412 AA.
AC G3V7L5;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=POU domain, class 4, transcription factor 2 {ECO:0000305};
DE AltName: Full=Brain-specific homeobox/POU domain protein 3B;
DE Short=Brain-3B;
DE Short=Brn-3B;
DE AltName: Full=Brn-3.2;
GN Name=Pou4f2 {ECO:0000312|RGD:620075};
GN Synonyms=Brn3b {ECO:0000303|PubMed:8835784};
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;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=8835784; DOI=10.1007/bf02736850;
RA Liu Y.Z., Dawson S.J., Latchman D.S.;
RT "Alternative splicing of the Brn-3a and Brn-3b transcription factor RNAs is
RT regulated in neuronal cells.";
RL J. Mol. Neurosci. 7:77-85(1996).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18368538; DOI=10.1007/s12192-008-0028-2;
RA Farooqui-Kabir S.R., Diss J.K., Henderson D., Marber M.S., Latchman D.S.,
RA Budhram-Mahadeo V., Heads R.J.;
RT "Cardiac expression of Brn-3a and Brn-3b POU transcription factors and
RT regulation of Hsp27 gene expression.";
RL Cell Stress Chaperones 13:297-312(2008).
CC -!- FUNCTION: Tissue-specific DNA-binding transcription factor involved in
CC the development and differentiation of target cells. Functions either
CC as activator or repressor modulating the rate of target gene
CC transcription through RNA polymerase II enzyme in a promoter-dependent
CC manner. Binds to the consensus octamer motif 5'-AT[A/T]A[T/A]T[A/T]A-3'
CC of promoter of target genes. Plays a fundamental role in the gene
CC regulatory network essential for retinal ganglion cell (RGC)
CC differentiation. Binds to an octamer site to form a ternary complex
CC with ISL1; cooperates positively with ISL1 and ISL2 to potentiate
CC transcriptional activation of RGC target genes being involved in RGC
CC fate commitment in the developing retina and RGC axon formation and
CC pathfinding. Inhibits DLX1 and DLX2 transcriptional activities
CC preventing DLX1- and DLX2-mediated ability to promote amacrine cell
CC fate specification. In cooperation with TP53 potentiates
CC transcriptional activation of BAX promoter activity increasing neuronal
CC cell apoptosis. Negatively regulates BAX promoter activity in the
CC absence of TP53. Acts as a transcriptional coactivator via its
CC interaction with the transcription factor ESR1 by enhancing its effect
CC on estrogen response element (ERE)-containing promoter. Antagonizes the
CC transcriptional stimulatory activity of POU4F1 by preventing its
CC binding to an octamer motif. Involved in TNFSF11-mediated terminal
CC osteoclast differentiation. {ECO:0000250|UniProtKB:Q63934}.
CC -!- SUBUNIT: Interacts with POU4F1; this interaction inhibits both POU4F1
CC DNA-binding and transcriptional activities. Interacts (C-terminus) with
CC ESR1 (via DNA-binding domain); this interaction increases the estrogen
CC receptor ESR1 transcriptional activity in a DNA- and ligand 17-beta-
CC estradiol-independent manner. Interacts (via C-terminus) with TP53 (via
CC N-terminus). Interacts with DLX1 (via homeobox DNA-binding domain);
CC this interaction suppresses DLX1-mediated transcriptional activity in
CC postnatal retina enhancing retinal ganglion cell (RGC) differentiation.
CC Interacts with DLX2 (via homeobox DNA-binding domain); this interaction
CC enhances RGC differentiation. Interacts (via C-terminus) with ISL1 (via
CC C-terminus). Interacts with ISL2. Interacts with LHX2.
CC {ECO:0000250|UniProtKB:Q63934}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18368538}. Nucleus
CC speckle {ECO:0000250|UniProtKB:Q12837}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q63934}.
CC -!- TISSUE SPECIFICITY: Expressed in the heart, brain and spinal cord
CC (PubMed:8835784, PubMed:18368538). Expressed in cardiomyocytes (at
CC protein level) (PubMed:18368538). Expressed in brain and spinal cord
CC (PubMed:8835784, PubMed:18368538). Expressed in dorsal root ganglion
CC (RGD) neurons (PubMed:8835784). {ECO:0000269|PubMed:18368538,
CC ECO:0000269|PubMed:8835784}.
CC -!- DOMAIN: The N-terminal transcriptional activation region is sufficient
CC to induce transcriptional activity. {ECO:0000250|UniProtKB:Q63934}.
CC -!- DOMAIN: The POU-specific domain and POU homeodomain regions are
CC necessary for DNA-binding activity and transcriptional repression.
CC {ECO:0000250|UniProtKB:Q63934}.
CC -!- DOMAIN: The polyhistidine motif acts as a targeting signal to nuclear
CC speckles. {ECO:0000250|UniProtKB:Q12837}.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-4
CC subfamily. {ECO:0000305}.
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DR EMBL; AABR07043626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473972; EDL92324.1; -; Genomic_DNA.
DR RefSeq; NP_599182.1; NM_134355.1.
DR AlphaFoldDB; G3V7L5; -.
DR SMR; G3V7L5; -.
DR STRING; 10116.ENSRNOP00000016422; -.
DR PaxDb; G3V7L5; -.
DR Ensembl; ENSRNOT00000016422; ENSRNOP00000016422; ENSRNOG00000012167.
DR GeneID; 171355; -.
DR KEGG; rno:171355; -.
DR CTD; 5458; -.
DR RGD; 620075; Pou4f2.
DR eggNOG; KOG1168; Eukaryota.
DR GeneTree; ENSGT00940000160339; -.
DR HOGENOM; CLU_013065_0_0_1; -.
DR InParanoid; G3V7L5; -.
DR OMA; THAPHMA; -.
DR OrthoDB; 929123at2759; -.
DR TreeFam; TF316413; -.
DR Reactome; R-RNO-6804759; Regulation of TP53 Activity through Association with Co-factors.
DR PRO; PR:G3V7L5; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Proteomes; UP000234681; Chromosome 19.
DR Bgee; ENSRNOG00000012167; Expressed in cerebellum.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000791; C:euchromatin; ISO:RGD.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0002039; F:p53 binding; ISO:RGD.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0048675; P:axon extension; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; ISO:RGD.
DR GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISS:UniProtKB.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; ISS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:RGD.
DR GO; GO:0071453; P:cellular response to oxygen levels; IMP:BHF-UCL.
DR GO; GO:1990791; P:dorsal root ganglion development; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; ISO:RGD.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; ISO:RGD.
DR GO; GO:1904178; P:negative regulation of adipose tissue development; ISO:RGD.
DR GO; GO:1902870; P:negative regulation of amacrine cell differentiation; ISS:UniProtKB.
DR GO; GO:0045596; P:negative regulation of cell differentiation; ISS:UniProtKB.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0050885; P:neuromuscular process controlling balance; ISO:RGD.
DR GO; GO:0030182; P:neuron differentiation; ISO:RGD.
DR GO; GO:0045773; P:positive regulation of axon extension; ISS:UniProtKB.
DR GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IMP:BHF-UCL.
DR GO; GO:0045597; P:positive regulation of cell differentiation; ISS:UniProtKB.
DR GO; GO:0046326; P:positive regulation of glucose import; ISO:RGD.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; ISS:UniProtKB.
DR GO; GO:0043068; P:positive regulation of programmed cell death; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; ISS:UniProtKB.
DR GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0090259; P:regulation of retinal ganglion cell axon guidance; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060041; P:retina development in camera-type eye; ISO:RGD.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; ISO:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR CDD; cd00086; homeodomain; 1.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR013847; POU.
DR InterPro; IPR000327; POU_dom.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00157; Pou; 1.
DR PRINTS; PR00028; POUDOMAIN.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00352; POU; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS00035; POU_1; 1.
DR PROSITE; PS00465; POU_2; 1.
DR PROSITE; PS51179; POU_3; 1.
PE 1: Evidence at protein level;
KW Activator; Apoptosis; Cytoplasm; Developmental protein; Differentiation;
KW DNA-binding; Homeobox; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..412
FT /note="POU domain, class 4, transcription factor 2"
FT /id="PRO_0000438269"
FT DOMAIN 253..330
FT /note="POU-specific"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT DNA_BIND 348..407
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 29..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..240
FT /note="Required for transcriptional activation"
FT /evidence="ECO:0000250|UniProtKB:Q63934"
FT REGION 123..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..412
FT /note="Required for DNA-binding and transcriptional
FT repression"
FT /evidence="ECO:0000250|UniProtKB:Q63934"
FT MOTIF 113..122
FT /note="POU-IV box"
FT MOTIF 174..188
FT /note="Nuclear speckle targeting signal"
FT /evidence="ECO:0000250|UniProtKB:Q12837"
FT COMPBIAS 30..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..186
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 43230 MW; 7F8185EE9941EC72 CRC64;
MMMMSLNSKQ AFSMPHAGSL HVEPKYSALH SASPGSSAPA APSASSPSSS SNAGSGGGGG
GGGGGGGGGR SSSSSSSGSG GGGGGGSEAM RRACLPTPPS NIFGGLDESL LARAEALAAV
DIVSQSKSHH HHPPHHSPFK PDATYHTMNT IPCTSAASSS SVPISHPSAL AGTHHHHHHH
HHHHHQPHQA LEGELLEHLS PGLALGAMAG PDGTVVSTPA HAPHMATMNP MHQAALSMAH
AHGLPSHMGC MSDVDADPRD LEAFAERFKQ RRIKLGVTQA DVGSALANLK IPGVGSLSQS
TICRFESLTL SHNNMIALKP ILQAWLEEAE KSHREKLTKP ELFNGAEKKR KRTSIAAPEK
RSLEAYFAIQ PRPSSEKIAA IAEKLDLKKN VVRVWFCNQR QKQKRMKYSA GI
