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PO2F2_PIG
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   25-MAY-2022, entry version 130.
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}.
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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   PRIDE; Q29013; -.
DR   GeneID; 397105; -.
DR   KEGG; ssc:397105; -.
DR   CTD; 5452; -.
DR   InParanoid; Q29013; -.
DR   ChiTaRS; SLC22A2; pig.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; 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; 1.10.260.40; -; 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; 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
 
 
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