ID PO2F2_PIG Reviewed; 478 AA. AC Q29013; Q29089; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JAN-2024, entry version 135. DE RecName: Full=POU domain, class 2, transcription factor 2; 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; Synonyms=OCT2, OTF2; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Spleen; RX PubMed=7943947; DOI=10.1111/j.1365-2052.1994.tb00102.x; RA Tuggle C.K., Helm J., Rothschild M.F.; RT "Cloning, sequencing and restriction fragment length polymorphism analysis RT of a porcine cDNA for OCT2."; RL Anim. Genet. 25:141-145(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 210-350. RC STRAIN=Duroc; RX PubMed=8270542; DOI=10.2527/1993.71113172x; RA Tuggle C.K.; RT "Cloning and sequence analysis of the swine Oct-2 POU-domain genomic RT region."; RL J. Anim. Sci. 71:3172-3172(1993). CC -!- FUNCTION: Transcription factor that specifically binds to the octamer CC motif (5'-ATTTGCAT-3'). Regulates IL6 expression in B cells with CC POU2AF1. Regulates transcription in a number of tissues in addition to CC activating immunoglobulin gene expression. Modulates transcription CC transactivation by NR3C1, AR and PGR. {ECO:0000250|UniProtKB:P09086, CC ECO:0000250|UniProtKB:Q00196}. CC -!- ACTIVITY REGULATION: Transactivation activity is enhanced by CC transcriptional coactivator POU2AF1. {ECO:0000250|UniProtKB:Q00196}. 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: Nucleus. CC -!- TISSUE SPECIFICITY: Predominantly expressed in B-cells. CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-2 CC subfamily. {ECO:0000305}. 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; U00794; AAA80148.1; -; mRNA. DR EMBL; L03842; AAA74657.1; -; Genomic_DNA. DR PIR; I47154; I47154. DR RefSeq; NP_999205.1; NM_214040.1. DR AlphaFoldDB; Q29013; -. DR SMR; Q29013; -. DR STRING; 9823.ENSSSCP00000060397; -. DR GeneID; 397105; -. DR KEGG; ssc:397105; -. DR CTD; 5452; -. DR InParanoid; Q29013; -. DR OrthoDB; 4250502at2759; -. DR ChiTaRS; SLC22A2; pig. DR Proteomes; UP000008227; Unplaced. DR Proteomes; UP000314985; Unplaced. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS: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; IBA:GO_Central. DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB. DR GO; GO:0098586; P:cellular response to virus; ISS:UniProtKB. DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. 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. PE 2: Evidence at transcript level; KW Activator; DNA-binding; Homeobox; Nucleus; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1..478 FT /note="POU domain, class 2, transcription factor 2" FT /id="PRO_0000100716" FT DOMAIN 195..269 FT /note="POU-specific" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530" FT DNA_BIND 297..356 FT /note="Homeobox" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108" FT REGION 1..82 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 167..199 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 275..298 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 357..391 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 389..410 FT /note="Leucine-zipper" FT REGION 409..478 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 431..445 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 446..472 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CONFLICT 212 FT /note="Q -> V (in Ref. 2; AAA74657)" FT /evidence="ECO:0000305" FT CONFLICT 215 FT /note="I -> M (in Ref. 2; AAA74657)" FT /evidence="ECO:0000305" FT CONFLICT 222 FT /note="G -> V (in Ref. 2; AAA74657)" FT /evidence="ECO:0000305" FT CONFLICT 233 FT /note="G -> A (in Ref. 2; AAA74657)" FT /evidence="ECO:0000305" FT CONFLICT 238 FT /note="Q -> K (in Ref. 2; AAA74657)" FT /evidence="ECO:0000305" FT CONFLICT 285 FT /note="R -> S (in Ref. 2; AAA74657)" FT /evidence="ECO:0000305" SQ SEQUENCE 478 AA; 51099 MW; FD196758B603B718 CRC64; MVHSSMGAPE IRMSKPLEAE KQGLDSPSEH TDTERNGPDT NHQNPQNKTS PFSVSPTGPS TKIKAEDPSG DSAPAGPPPP QAVQAHLSQV QLMLTGRQLA GDIQQILQLQ QLVLVPGHHL QPPAQFLLPQ AQQSQPGLLP TPNLFQLPQQ TQGALLTSQP RAGLPTQAVT RPTLSDPHLS HPQPPKCLEP PSHPEEASDL EELEQFARTF KQRRIKLGFT QGDVGLAMGK LYGNDFSQTT ISRFEALNLS FKNMCKLKPL LEKWLNDAET MSVDSSLPSP NQLSRPSLGF DGLPGRRRKK RTSIETNVRF ALEKSFLANQ KPTSEEILLI AEQLHMEKEV IRVWFCNRRQ KEKRINPCSA APMLPSPGKP ASYSPHLVTP QGGAGTLPLS QASSSLSTTV TTLSSAVGTL HPSRTAGGGA AGGGAAPPLN SIPSVTPPPP ATTNSTNPSP QGSHSAIGLS GLNPSTGPGL WNPAPYQP //