PO2F1_RAT
ID PO2F1_RAT Reviewed; 632 AA.
AC P31503; Q62719; Q63387;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=POU domain, class 2, transcription factor 1;
DE AltName: Full=NF-A1;
DE AltName: Full=Octamer-binding protein 1;
DE Short=Oct-1;
DE AltName: Full=Octamer-binding transcription factor 1;
DE Short=OTF-1;
DE Flags: Fragment;
GN Name=Pou2f1; Synonyms=Oct-1, Otf-1, Otf1;
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 [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Heart muscle;
RA Amacher S.L., Buskin J.N., Hauschka S.D.;
RT "Identification of a muscle creatine kinase enhancer A/T-rich site binding
RT factor as Oct-1.";
RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 172-325, AND TISSUE SPECIFICITY.
RX PubMed=8424955; DOI=10.1016/0167-4781(93)90071-k;
RA Kambe F., Tsukahara S., Kato T., Seo H.;
RT "The POU-domain protein Oct-1 is widely expressed in adult rat organs.";
RL Biochim. Biophys. Acta 1171:307-310(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 194-313.
RC TISSUE=Spinal ganglion;
RX PubMed=1677182; DOI=10.1093/nar/19.13.3744;
RA Lillycrop K.A., Latchman D.S.;
RT "Cloning and sequencing of the rat Oct-1 POU box.";
RL Nucleic Acids Res. 19:3744-3744(1991).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Transcription factor that binds to the octamer motif (5'-
CC ATTTGCAT-3') and activates the promoters of the genes for some small
CC nuclear RNAs (snRNA) and of genes such as those for histone H2B and
CC immunoglobulins. Modulates transcription transactivation by NR3C1, AR
CC and PGR. {ECO:0000250|UniProtKB:P14859}.
CC -!- SUBUNIT: Interacts with POU2AF1; the interaction increases POU2F1
CC transactivation activity. Interacts with NR3C1, AR, PGR and HCFC1.
CC {ECO:0000250|UniProtKB:P14859}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8424955}.
CC -!- PTM: Phosphorylated by PRKDC. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-2
CC subfamily. {ECO:0000305}.
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DR EMBL; U17013; AAA53185.1; -; mRNA.
DR EMBL; D12978; BAA02355.1; -; mRNA.
DR EMBL; X59429; CAA42059.1; -; mRNA.
DR PIR; S16445; S16445.
DR PIR; S28181; S28181.
DR RefSeq; NP_001094109.1; NM_001100639.1.
DR AlphaFoldDB; P31503; -.
DR SMR; P31503; -.
DR CORUM; P31503; -.
DR STRING; 10116.ENSRNOP00000044416; -.
DR PaxDb; P31503; -.
DR PeptideAtlas; P31503; -.
DR PRIDE; P31503; -.
DR GeneID; 171068; -.
DR KEGG; rno:171068; -.
DR UCSC; RGD:621689; rat.
DR CTD; 5451; -.
DR RGD; 621689; Pou2f1.
DR eggNOG; KOG3802; Eukaryota.
DR InParanoid; P31503; -.
DR OrthoDB; 873012at2759; -.
DR Reactome; R-RNO-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-RNO-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; IDA:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:RGD.
DR GO; GO:0060235; P:lens induction in camera-type eye; ISO:RGD.
DR GO; GO:0097421; P:liver regeneration; IEP:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0030910; P:olfactory placode formation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
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; IPR045703; POU2F1_C.
DR InterPro; IPR000327; POU_dom.
DR InterPro; IPR000972; TF_octamer.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00157; Pou; 1.
DR Pfam; PF19536; POU2F1_C; 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 1: Evidence at protein level;
KW Activator; DNA-binding; Homeobox; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN <1..632
FT /note="POU domain, class 2, transcription factor 1"
FT /id="PRO_0000100711"
FT DOMAIN 167..241
FT /note="POU-specific"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT DNA_BIND 268..327
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 243..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 157
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14859"
FT MOD_RES 163
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14859"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14859"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14859"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14859"
FT CONFLICT 218
FT /note="A -> S (in Ref. 3; CAA42059)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="K -> S (in Ref. 3; CAA42059)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="S -> L (in Ref. 3; CAA42059)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="R -> S (in Ref. 3; CAA42059)"
FT /evidence="ECO:0000305"
FT CONFLICT 281..282
FT /note="VA -> WS (in Ref. 3; CAA42059)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 632 AA; 65170 MW; D8CEA4C27346274B CRC64;
LTPAQQQLLL QQAQAQAQLL AAAVQQHSAS QQHSAAGATI SASAATPMTQ IPLSQPIQIA
QDLQQLQQLQ QQNLNLQQFV LVHPTTNLQP AQFIISQTPQ GQQGLLQAQN LLTQLPQQSQ
ANLLQPQPSI TLTSQPTTPT RTIAATPIQT LPQSQTTPKR IDTPSLEEPS DLEELEQFAK
TFKQRRIKLG FTQGDVGLAM GKLYGNDFSQ TTISRFEALN LSFKNMCKLK PLLEKWLNDA
ENLSSDSTAS SPSALNSPGL GAEGLNRRRK KRTSIETNIR VALEKSFMEN QKPTSEDITL
IAEQLNMEKE VIRVWFCNRR QKEKRINPPS SGGTSSSPIK AIFPSPTSLV ATTPSLVTSS
TATTLTVNPV LPLTSAAMTN LSLTGTTDST SNNTATVIST APPASSAVTS PSLSPSPSAS
ASTSEASSAS ETSTTQTTST PLPSPLGASQ VMVTASGLQT AAAAALQGAA QLPANASLAA
MAAAAGLNPG LMAPSQFAAG GALLSLNPGT LGGALSPALM SNSTLATIQA LASSGSLPIT
SLDATGNLVF ANAGGAPNIV TAPLFLNPQN LSLLTSNPVS LVSAAAASTG NSAPTASLHA
SSTSTESIQN SLFTVASASG AASTTTAASK AQ
