PO2F2_MOUSE
ID PO2F2_MOUSE Reviewed; 463 AA.
AC Q00196; Q00197; Q00198; Q00199; Q00200; Q00201; Q05882; Q3KR47; Q3U127;
AC Q5XML1; Q5XML2; Q61995; Q61996; Q64245;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 4.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=POU domain, class 2, transcription factor 2 {ECO:0000305};
DE AltName: Full=Lymphoid-restricted immunoglobulin octamer-binding protein NF-A2;
DE AltName: Full=Octamer-binding protein 2;
DE Short=Oct-2;
DE AltName: Full=Octamer-binding transcription factor 2;
DE Short=OTF-2;
GN Name=Pou2f2 {ECO:0000312|MGI:MGI:101897}; Synonyms=Oct2, Otf2;
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] (ISOFORMS OCT2.2 AND OCT2.5).
RC TISSUE=B-cell;
RX PubMed=1976089; DOI=10.1242/dev.109.2.349;
RA Hatzopoulos A.K., Stoykova A.S., Erselius J.R., Goulding M.D., Neuman T.,
RA Gruss P.;
RT "Structure and expression of the mouse Oct2a and Oct2b, two differentially
RT spliced products of the same gene.";
RL Development 109:349-362(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS OCT2.1; OCT2.2; OCT2.3; OCT2.4; OCT2.5
RP AND OCT2.6), AND FUNCTION.
RC TISSUE=Pre-B cell;
RX PubMed=2011512; DOI=10.1093/nar/19.1.43;
RA Wirth T., Priess A., Annweiler A., Zwilling S., Oeler B.;
RT "Multiple Oct2 isoforms are generated by alternative splicing.";
RL Nucleic Acids Res. 19:43-51(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM OCT2.1), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 5-263 (ISOFORM OCT2.7), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=C3H/HeN; TISSUE=Mammary gland;
RX PubMed=17285328; DOI=10.1007/s00441-006-0368-0;
RA Dong B., Zhao F.-Q.;
RT "Expression of the Oct-2 transcription factor in mouse mammary gland and
RT cloning and characterization of a novel Oct-2 isoform.";
RL Cell Tissue Res. 328:595-606(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS OCT2.1 AND OCT2.3).
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 167-361 (ISOFORM OCT2.2).
RC STRAIN=129/Sv;
RX PubMed=7888080; DOI=10.1515/bchm3.1994.375.10.675;
RA Matsuo K., Clay O., Kuenzler P., Georgiev O., Urbanek P., Schaffner W.;
RT "Short introns interrupting the Oct-2 POU domain may prevent recombination
RT between POU family genes without interfering with potential POU domain
RT 'shuffling' in evolution.";
RL Biol. Chem. Hoppe-Seyler 375:675-683(1994).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 203-325 (ISOFORM OCT2.1).
RC STRAIN=T6 / TW1; TISSUE=Testis;
RX PubMed=1970171; DOI=10.1093/nar/18.6.1634;
RA Goldsborough A., Ashworth A., Willison K.R.;
RT "Cloning and sequencing of POU-boxes expressed in mouse testis.";
RL Nucleic Acids Res. 18:1634-1634(1990).
RN [8]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM OCT2.2).
RX PubMed=1425197;
RA Stepchenko A.G.;
RT "Interaction of Oct-binding transcription factors with a large series of
RT 'noncanonical' oct-sequences. Primary sequence of murine Oct-2B cDNA.";
RL Dokl. Akad. Nauk SSSR 325:175-178(1992).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=1281152; DOI=10.1016/s0021-9258(19)73991-x;
RA Lillycrop K.A., Latchman D.S.;
RT "Alternative splicing of the Oct-2 transcription factor RNA is
RT differentially regulated in neuronal cells and B cells and results in
RT protein isoforms with opposite effects on the activity of
RT octamer/TAATGARAT-containing promoters.";
RL J. Biol. Chem. 267:24960-24965(1992).
RN [10]
RP ALTERNATIVE SPLICING.
RX PubMed=1550677; DOI=10.1016/0896-6273(92)90282-i;
RA Stoykova A.S., Sterrer S., Erselius J.R., Hatzopoulos A.K., Gruss P.;
RT "Mini-Oct and Oct-2c: two novel, functionally diverse murine Oct-2 gene
RT products are differentially expressed in the CNS.";
RL Neuron 8:541-558(1992).
RN [11]
RP FUNCTION.
RX PubMed=7935477; DOI=10.1128/mcb.14.11.7633-7642.1994;
RA Lillycrop K.A., Dawson S.J., Estridge J.K., Gerster T., Matthias P.,
RA Latchman D.S.;
RT "Repression of a herpes simplex virus immediate-early promoter by the Oct-2
RT transcription factor is dependent on an inhibitory region at the N terminus
RT of the protein.";
RL Mol. Cell. Biol. 14:7633-7642(1994).
RN [12]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, INDUCTION BY LPS, AND
RP ACTIVITY REGULATION.
RX PubMed=23045607; DOI=10.1084/jem.20111504;
RA Karnowski A., Chevrier S., Belz G.T., Mount A., Emslie D., D'Costa K.,
RA Tarlinton D.M., Kallies A., Corcoran L.M.;
RT "B and T cells collaborate in antiviral responses via IL-6, IL-21, and
RT transcriptional activator and coactivator, Oct2 and OBF-1.";
RL J. Exp. Med. 209:2049-2064(2012).
CC -!- FUNCTION: Transcription factor that specifically binds to the octamer
CC motif (5'-ATTTGCAT-3') (PubMed:2011512, PubMed:1281152). Regulates IL6
CC expression in B cells with POU2AF1 (PubMed:23045607). Regulates
CC transcription in a number of tissues in addition to activating
CC immunoglobulin gene expression. Modulates transcription transactivation
CC by NR3C1, AR and PGR. {ECO:0000250|UniProtKB:P09086,
CC ECO:0000269|PubMed:1281152, ECO:0000269|PubMed:17285328,
CC ECO:0000269|PubMed:2011512, ECO:0000269|PubMed:23045607,
CC ECO:0000269|PubMed:7935477}.
CC -!- FUNCTION: [Isoform OCT2.1]: Activates octamer-containing promoters.
CC {ECO:0000269|PubMed:1281152, ECO:0000269|PubMed:2011512}.
CC -!- FUNCTION: [Isoform OCT2.2]: Activates octamer-containing promoters.
CC {ECO:0000269|PubMed:1281152, ECO:0000269|PubMed:2011512}.
CC -!- FUNCTION: [Isoform OCT2.3]: Activates octamer-containing promoters.
CC {ECO:0000269|PubMed:1281152, ECO:0000269|PubMed:2011512}.
CC -!- FUNCTION: [Isoform OCT2.4]: Represses some promoters and activate
CC others. {ECO:0000269|PubMed:1281152, ECO:0000269|PubMed:2011512}.
CC -!- FUNCTION: [Isoform OCT2.5]: Represses some promoters and activate
CC others (PubMed:1281152, PubMed:2011512). Activates the U2 small nuclear
CC RNA (snRNA) promoter (By similarity). {ECO:0000250|UniProtKB:P09086,
CC ECO:0000269|PubMed:1281152, ECO:0000269|PubMed:2011512}.
CC -!- FUNCTION: [Isoform OCT2.7]: Unable to bind to the octamer motif, but
CC can still activate the beta-casein gene promoter at low levels.
CC {ECO:0000269|PubMed:17285328}.
CC -!- ACTIVITY REGULATION: Transactivation activity is enhanced by
CC transcriptional coactivator POU2AF1. {ECO:0000269|PubMed:23045607}.
CC -!- SUBUNIT: Interacts with NR3C1, AR and PGR. Interacts with POU2AF1; the
CC interaction increases POU2F2 transactivation activity.
CC {ECO:0000250|UniProtKB:P09086}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17285328}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-
CC ProRule:PRU00530, ECO:0000269|PubMed:17285328}. Note=In alveolus
CC epithelial cells of mammary glands, present in the nucleus and
CC cytoplasm. In HC11 mammary epithelial cells, present in the nucleus and
CC preinuclear regions.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Comment=Additional isoforms seem to exist.;
CC Name=OCT2.1; Synonyms=Major form;
CC IsoId=Q00196-1; Sequence=Displayed;
CC Name=OCT2.2; Synonyms=OCT2a;
CC IsoId=Q00196-2; Sequence=VSP_002328;
CC Name=OCT2.3;
CC IsoId=Q00196-3; Sequence=VSP_002326;
CC Name=OCT2.4;
CC IsoId=Q00196-4; Sequence=VSP_002329, VSP_002330;
CC Name=OCT2.5; Synonyms=OCT2b;
CC IsoId=Q00196-5; Sequence=VSP_002331;
CC Name=OCT2.6;
CC IsoId=Q00196-6; Sequence=VSP_002327;
CC Name=OCT2.7;
CC IsoId=Q00196-7; Sequence=VSP_002326, VSP_032188;
CC -!- TISSUE SPECIFICITY: Highest in B cells, but also present in brain
CC (neuronal and glial cells), intestine, kidney, and testes.
CC {ECO:0000269|PubMed:1281152, ECO:0000269|PubMed:17285328,
CC ECO:0000269|PubMed:23045607}.
CC -!- TISSUE SPECIFICITY: [Isoform OCT2.1]: Expressed at higher levels in B-
CC cells than in neuronal cells. {ECO:0000269|PubMed:1281152}.
CC -!- TISSUE SPECIFICITY: [Isoform OCT2.2]: Expressed in neuronal cell lines
CC and brain, but not dorsal root ganglia. {ECO:0000269|PubMed:1281152}.
CC -!- TISSUE SPECIFICITY: [Isoform OCT2.3]: Expressed at lower levels in
CC neuronal cells than in B cells. {ECO:0000269|PubMed:1281152}.
CC -!- TISSUE SPECIFICITY: [Isoform OCT2.4]: Expressed in neuronal cell lines,
CC and at lower levels in neuroblastoma and dorsal root ganglia.
CC {ECO:0000269|PubMed:1281152}.
CC -!- TISSUE SPECIFICITY: [Isoform OCT2.5]: Widely expressed in the
CC developing nervous system but expression is confined to very specific
CC regions in the adult brain, it is expressed at a lower level in B
CC cells. {ECO:0000269|PubMed:1281152}.
CC -!- TISSUE SPECIFICITY: [Isoform OCT2.6]: Either absent in, or expressed at
CC very low levels in neuronal cells and brain.
CC {ECO:0000269|PubMed:1281152}.
CC -!- TISSUE SPECIFICITY: [Isoform OCT2.7]: Expressed in all tissues tested:
CC mammary gland, liver, spleen, lung, kidney intestine, uterus and ovary
CC of a virgin mouse. Levels of isoform OCT2.7 are highest in spleen and
CC lung. In mammary gland, expression is localized to the alveolus
CC epithelial cells. {ECO:0000269|PubMed:17285328}.
CC -!- DEVELOPMENTAL STAGE: Widely but not homogeneously expressed in
CC developing nervous system. Expression levels in mammary glands are
CC barely detectable in virgin mice, levels increase during pregnancy,
CC reaching a maximum during late pregnancy, then decrease during
CC lactation becoming very low post-lactation.
CC {ECO:0000269|PubMed:17285328}.
CC -!- INDUCTION: In B cells, expression is highly increased upon activation
CC by LPS or CpG. {ECO:0000269|PubMed:23045607}.
CC -!- DISRUPTION PHENOTYPE: Mutants show normal development of germinal
CC center B cells when infected by influenza virus.
CC {ECO:0000269|PubMed:23045607}.
CC -!- MISCELLANEOUS: [Isoform OCT2.2]: The isoform OCT2b described in
CC PubMed:7888080 corresponds to the isoform OCT2a of PubMed:1976089. To
CC avoid any confusion, we use the nomenclature from PubMed:2011512 to
CC describe the different isoforms.
CC -!- MISCELLANEOUS: [Isoform OCT2.5]: The isoform OCT2b described in
CC PubMed:7888080 corresponds to the isoform OCT2a of PubMed:1976089. To
CC avoid any confusion, we use the nomenclature from PubMed:2011512 to
CC describe the different isoforms.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-2
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAU95617.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE33673.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X53654; CAA37702.1; -; mRNA.
DR EMBL; X57936; CAA41004.1; -; mRNA.
DR EMBL; X57937; CAA41005.1; -; mRNA.
DR EMBL; X57938; CAA41006.1; -; mRNA.
DR EMBL; X57939; CAA41007.1; -; mRNA.
DR EMBL; X57940; CAA41008.1; -; mRNA.
DR EMBL; X57941; CAA41009.1; -; mRNA.
DR EMBL; AY746973; AAU95616.1; -; mRNA.
DR EMBL; AY746974; AAU95617.1; ALT_INIT; mRNA.
DR EMBL; AK156322; BAE33673.1; ALT_FRAME; mRNA.
DR EMBL; BC104488; AAI04489.1; -; mRNA.
DR EMBL; BC105647; AAI05648.1; -; mRNA.
DR EMBL; BC105920; AAI05921.1; -; mRNA.
DR EMBL; BC105921; AAI05922.1; -; mRNA.
DR EMBL; X81031; CAA56934.1; -; Genomic_DNA.
DR EMBL; X51961; CAA36220.1; -; mRNA.
DR EMBL; X57089; CAA40369.1; -; mRNA.
DR EMBL; S55236; AAA11815.1; -; mRNA.
DR CCDS; CCDS39834.1; -. [Q00196-2]
DR CCDS; CCDS52143.1; -. [Q00196-1]
DR CCDS; CCDS52144.1; -. [Q00196-5]
DR CCDS; CCDS52145.1; -. [Q00196-3]
DR PIR; S22539; S22539.
DR PIR; S22542; S22542.
DR PIR; S22543; S22543.
DR PIR; S22544; S22544.
DR RefSeq; NP_001157026.1; NM_001163554.1. [Q00196-5]
DR RefSeq; NP_001157027.1; NM_001163555.1. [Q00196-3]
DR RefSeq; NP_001157028.1; NM_001163556.1. [Q00196-1]
DR RefSeq; NP_035268.2; NM_011138.2. [Q00196-2]
DR RefSeq; XP_006539722.1; XM_006539659.2. [Q00196-7]
DR AlphaFoldDB; Q00196; -.
DR SMR; Q00196; -.
DR STRING; 10090.ENSMUSP00000104056; -.
DR iPTMnet; Q00196; -.
DR PhosphoSitePlus; Q00196; -.
DR MaxQB; Q00196; -.
DR PaxDb; Q00196; -.
DR PRIDE; Q00196; -.
DR ProteomicsDB; 289642; -. [Q00196-1]
DR ProteomicsDB; 289643; -. [Q00196-2]
DR ProteomicsDB; 289644; -. [Q00196-3]
DR ProteomicsDB; 289645; -. [Q00196-4]
DR ProteomicsDB; 289646; -. [Q00196-5]
DR ProteomicsDB; 289647; -. [Q00196-6]
DR ProteomicsDB; 289648; -. [Q00196-7]
DR Antibodypedia; 3745; 586 antibodies from 43 providers.
DR DNASU; 18987; -.
DR Ensembl; ENSMUST00000098679; ENSMUSP00000096276; ENSMUSG00000008496. [Q00196-7]
DR Ensembl; ENSMUST00000108413; ENSMUSP00000104051; ENSMUSG00000008496. [Q00196-4]
DR Ensembl; ENSMUST00000108415; ENSMUSP00000104053; ENSMUSG00000008496. [Q00196-2]
DR Ensembl; ENSMUST00000108416; ENSMUSP00000104054; ENSMUSG00000008496. [Q00196-6]
DR Ensembl; ENSMUST00000108417; ENSMUSP00000104055; ENSMUSG00000008496. [Q00196-3]
DR Ensembl; ENSMUST00000108418; ENSMUSP00000104056; ENSMUSG00000008496. [Q00196-5]
DR Ensembl; ENSMUST00000175774; ENSMUSP00000135075; ENSMUSG00000008496. [Q00196-1]
DR GeneID; 18987; -.
DR KEGG; mmu:18987; -.
DR UCSC; uc009frm.1; mouse. [Q00196-7]
DR UCSC; uc009frn.2; mouse. [Q00196-2]
DR UCSC; uc009fro.2; mouse. [Q00196-5]
DR UCSC; uc009frp.2; mouse. [Q00196-1]
DR UCSC; uc009frq.2; mouse. [Q00196-3]
DR UCSC; uc009frr.2; mouse. [Q00196-4]
DR UCSC; uc012ffp.1; mouse. [Q00196-6]
DR CTD; 5452; -.
DR MGI; MGI:101897; Pou2f2.
DR VEuPathDB; HostDB:ENSMUSG00000008496; -.
DR eggNOG; KOG3802; Eukaryota.
DR GeneTree; ENSGT00940000160115; -.
DR HOGENOM; CLU_013065_4_1_1; -.
DR InParanoid; Q00196; -.
DR OMA; PMKISPF; -.
DR OrthoDB; 873012at2759; -.
DR PhylomeDB; Q00196; -.
DR TreeFam; TF316413; -.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR BioGRID-ORCS; 18987; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Pou2f2; mouse.
DR PRO; PR:Q00196; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q00196; protein.
DR Bgee; ENSMUSG00000008496; Expressed in embryonic brain and 118 other tissues.
DR ExpressionAtlas; Q00196; baseline and differential.
DR Genevisible; Q00196; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
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:0019904; F:protein domain specific binding; IPI:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0048469; P:cell maturation; IMP:MGI.
DR GO; GO:0098586; P:cellular response to virus; IMP:UniProtKB.
DR GO; GO:0002335; P:mature B cell differentiation; IMP:MGI.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 1.10.260.40; -; 1.
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 InterPro; IPR000972; TF_octamer.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00157; Pou; 1.
DR PRINTS; PR00029; OCTAMER.
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 2: Evidence at transcript level;
KW Activator; Alternative splicing; Cytoplasm; DNA-binding; Homeobox; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..463
FT /note="POU domain, class 2, transcription factor 2"
FT /id="PRO_0000100715"
FT DOMAIN 179..253
FT /note="POU-specific"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT DNA_BIND 281..340
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..394
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255"
FT REGION 393..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..86
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..429
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 62
FT /note="K -> KVGILSGLHLTFWGPGPCLSPPQ (in isoform OCT2.3 and
FT isoform OCT2.7)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17285328, ECO:0000303|PubMed:2011512"
FT /id="VSP_002326"
FT VAR_SEQ 63..101
FT /note="Missing (in isoform OCT2.6)"
FT /evidence="ECO:0000303|PubMed:2011512"
FT /id="VSP_002327"
FT VAR_SEQ 167
FT /note="Q -> QAMTRPTLPDPHLSHPQ (in isoform OCT2.2)"
FT /evidence="ECO:0000303|PubMed:1976089,
FT ECO:0000303|PubMed:2011512"
FT /id="VSP_002328"
FT VAR_SEQ 384..400
FT /note="VTTLSSAVGTLHPSRTA -> AQTRALKAATRLLACRA (in isoform
FT OCT2.4)"
FT /evidence="ECO:0000303|PubMed:2011512"
FT /id="VSP_002329"
FT VAR_SEQ 401..463
FT /note="Missing (in isoform OCT2.4)"
FT /evidence="ECO:0000303|PubMed:2011512"
FT /id="VSP_002330"
FT VAR_SEQ 452..463
FT /note="PGLWWNPAPYQP -> STMVGLSSGLSPALMSNNPLATIQALASGGTLPLTS
FT LDGSGNLVLGAAGAAPGSPSLVTSPLFLNHTGLPLLSAPPGVGLVSAAAAAVAASISSK
FT SPGLSSSSSSSSSSTCSDVAAQTPGGPGGPEAGSKAE (in isoform OCT2.5)"
FT /evidence="ECO:0000303|PubMed:1976089,
FT ECO:0000303|PubMed:2011512"
FT /id="VSP_002331"
FT VAR_SEQ 452..463
FT /note="PGLWWNPAPYQP -> STMVGLSSGLSPALMSNNPLATIQGACCLMSPHCHQ
FT SCPLLGLEPTLPHCCPSHAIPPPCSLHCSPLHPHLSSGKV (in isoform
FT OCT2.7)"
FT /evidence="ECO:0000303|PubMed:17285328"
FT /id="VSP_032188"
FT CONFLICT 409
FT /note="A -> R (in Ref. 2; CAA41004/CAA41005/CAA41006/
FT CAA41008/CAA41009)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="P -> L (in Ref. 2; CAA41004/CAA41005/CAA41006/
FT CAA41008/CAA41009)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 49439 MW; B6669B5885ABD789 CRC64;
MVHSSMGAPE IRMSKPLEAE KQSLDSPSEH TDTERNGPDI NHQNPQNKAS PFSVSPTGPS
TKIKAEDPSG DSAPAAPPPP QPAQPHLPQA QLMLTGSQLA GDIQQLLQLQ QLVLVPGHHL
QPPAQFLLPQ AQQSQPGLLP TPNLFQLPQQ TQGALLTSQP RAGLPTQPPK CLEPPSHPEE
PSDLEELEQF ARTFKQRRIK LGFTQGDVGL AMGKLYGNDF SQTTISRFEA LNLSFKNMCK
LKPLLEKWLN DAETMSVDSS LPSPNQLSSP SLGFDGLPGR RRKKRTSIET NVRFALEKSF
LANQKPTSEE ILLIAEQLHM EKEVIRVWFC NRRQKEKRIN PCSAAPMLPS PGKPTSYSPH
LVTPQGGAGT LPLSQASSSL STTVTTLSSA VGTLHPSRTA GGGGGGGGAA PPLNSIPSVT
PPPPATTNST NPSPQGSHSA IGLSGLNPSA GPGLWWNPAP YQP
