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   24-JAN-2024, entry version 196.
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.
DR   AlphaFoldDB; Q00196; -.
DR   SMR; Q00196; -.
DR   STRING; 10090.ENSMUSP00000104056; -.
DR   iPTMnet; Q00196; -.
DR   PhosphoSitePlus; Q00196; -.
DR   MaxQB; Q00196; -.
DR   PaxDb; 10090-ENSMUSP00000104056; -.
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   Pumba; Q00196; -.
DR   Antibodypedia; 3745; 665 antibodies from 43 providers.
DR   DNASU; 18987; -.
DR   Ensembl; ENSMUST00000098679.10; ENSMUSP00000096276.3; ENSMUSG00000008496.20. [Q00196-7]
DR   Ensembl; ENSMUST00000108413.8; ENSMUSP00000104051.2; ENSMUSG00000008496.20. [Q00196-4]
DR   Ensembl; ENSMUST00000108415.10; ENSMUSP00000104053.3; ENSMUSG00000008496.20. [Q00196-2]
DR   Ensembl; ENSMUST00000108416.10; ENSMUSP00000104054.3; ENSMUSG00000008496.20. [Q00196-6]
DR   Ensembl; ENSMUST00000108417.10; ENSMUSP00000104055.3; ENSMUSG00000008496.20. [Q00196-3]
DR   Ensembl; ENSMUST00000108418.11; ENSMUSP00000104056.4; ENSMUSG00000008496.20. [Q00196-5]
DR   Ensembl; ENSMUST00000175774.9; ENSMUSP00000135075.2; ENSMUSG00000008496.20. [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   AGR; MGI:101897; -.
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; 4250502at2759; -.
DR   PhylomeDB; Q00196; -.
DR   TreeFam; TF316413; -.
DR   Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR   BioGRID-ORCS; 18987; 2 hits in 79 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 119 other cell types or tissues.
DR   ExpressionAtlas; Q00196; baseline and differential.
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:0015606; F:spermidine transmembrane transporter activity; IDA:UniProtKB.
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:0045893; P:positive regulation of DNA-templated transcription; IDA: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:0006355; P:regulation of DNA-templated transcription; IDA:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0015848; P:spermidine transport; IDA:UniProtKB.
DR   CDD; cd00086; homeodomain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 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   PANTHER; PTHR11636; POU DOMAIN; 1.
DR   PANTHER; PTHR11636:SF46; POU DOMAIN, CLASS 2, TRANSCRIPTION FACTOR 2; 1.
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; Homeodomain-like; 1.
DR   SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 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.
DR   Genevisible; Q00196; MM.
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;
FT                   CAA41004/CAA41005/CAA41006/CAA41008/CAA41009)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        411
FT                   /note="P -> L (in Ref. 2;
FT                   CAA41004/CAA41005/CAA41006/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
//