PO3F1_RAT
ID PO3F1_RAT Reviewed; 451 AA.
AC P20267;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 2.
DT 25-MAY-2022, entry version 159.
DE RecName: Full=POU domain, class 3, transcription factor 1;
DE AltName: Full=Octamer-binding protein 6;
DE Short=Oct-6;
DE AltName: Full=Octamer-binding transcription factor 6;
DE Short=OTF-6;
DE AltName: Full=POU domain transcription factor SCIP;
DE AltName: Full=Tst-1;
GN Name=Pou3f1; Synonyms=Oct-6, Otf-6, Otf6, Scip;
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], FUNCTION, AND INDUCTION BY INJURY.
RX PubMed=1975954; DOI=10.1126/science.1975954;
RA Monuki E.S., Kuhn R., Weinmaster G., Trapp B.D., Lemke G.;
RT "Expression and activity of the POU transcription factor SCIP.";
RL Science 249:1300-1303(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 265-369.
RX PubMed=2739723; DOI=10.1038/340035a0;
RA He X., Treacy M.N., Simmons D.M., Ingraham H.A., Swanson L.W.,
RA Rosenfeld M.G.;
RT "Expression of a large family of POU-domain regulatory genes in mammalian
RT brain development.";
RL Nature 340:35-42(1989).
RN [3]
RP ERRATUM OF PUBMED:2739723, AND SEQUENCE REVISION TO 320.
RA He X., Treacy M.N., Simmons D.M., Ingraham H.A., Swanson L.W.,
RA Rosenfeld M.G.;
RL Nature 340:662-662(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-451.
RX PubMed=1705013; DOI=10.1128/mcb.11.3.1739-1744.1991;
RA He X., Gerrero M.R., Simmons D.M., Park R.E., Lin C.R., Swanson L.W.,
RA Rosenfeld M.G.;
RT "Tst-1, a member of the POU domain gene family, binds the promoter of the
RT gene encoding the cell surface adhesion molecule P0.";
RL Mol. Cell. Biol. 11:1739-1744(1991).
CC -!- FUNCTION: Transcription factor that binds to the octamer motif (5'-
CC ATTTGCAT-3') (By similarity). Acts as a transcriptional activator when
CC binding cooperatively with SOX4, SOX11, or SOX12 to gene promoters (By
CC similarity). Acts as a transcriptional repressor of myelin-specific
CC genes (PubMed:1975954). {ECO:0000250|UniProtKB:P21952,
CC ECO:0000269|PubMed:1975954}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P21952}.
CC -!- TISSUE SPECIFICITY: Neural tissues and testis.
CC -!- INDUCTION: Transiently increased in rapidly dividing Schwann cells in
CC response to sciatic nerve transection 2 days post-injury.
CC {ECO:0000269|PubMed:1975954}.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-3
CC subfamily. {ECO:0000305}.
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DR EMBL; M72711; AAA42118.1; -; mRNA.
DR EMBL; M63712; AAA42303.1; -; mRNA.
DR PIR; A40168; A40168.
DR RefSeq; NP_620193.1; NM_138838.1.
DR AlphaFoldDB; P20267; -.
DR SMR; P20267; -.
DR GeneID; 192110; -.
DR KEGG; rno:192110; -.
DR UCSC; RGD:619767; rat.
DR CTD; 5453; -.
DR RGD; 619767; Pou3f1.
DR InParanoid; P20267; -.
DR OrthoDB; 752252at2759; -.
DR PhylomeDB; P20267; -.
DR PRO; PR:P20267; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
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:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0008544; P:epidermis development; ISO:RGD.
DR GO; GO:0030900; P:forebrain development; ISO:RGD.
DR GO; GO:0010001; P:glial cell differentiation; IDA:RGD.
DR GO; GO:0030216; P:keratinocyte differentiation; ISO:RGD.
DR GO; GO:0042552; P:myelination; ISO:RGD.
DR GO; GO:0022011; P:myelination in peripheral nervous system; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
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:RGD.
DR GO; GO:0014044; P:Schwann cell development; ISO:RGD.
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; IPR016362; TF_POU_3.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00157; Pou; 1.
DR PIRSF; PIRSF002629; Transcription_factor_POU; 1.
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; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..451
FT /note="POU domain, class 3, transcription factor 1"
FT /id="PRO_0000100722"
FT DOMAIN 247..321
FT /note="POU-specific"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT DNA_BIND 339..398
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..451
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 423
FT /note="S -> G (in Ref. 4; AAA42118/AAA42303)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 451 AA; 45496 MW; E32626A759125EAA CRC64;
MATTAQYLPR GPGGGAGGTG PLMHPDAAAA AAAAAAAERL HAGAAYREVQ KLMHHEWLGA
GAGHPVGLAH PQWLPTGGGG GGDWAGGPHL EHGKAGGGST GRADDGGGGG GFHARLVHQG
AAHAGAAWAQ GGTAHHLGPA MSPSPGAGGG HQPQPLGLYA QAAYPGGGGG GLAGMLAAGG
GGAGPGLHHA LHEDGHEAQL EPSPPPHLGA HGHAHGHAHA GGLHAAAAHL HPGAGGGGSS
VGEHSDEDAP SSDDLEQFAK QFKQRRIKLG FTQADVGLAL GTLYGNVFSQ TTICRFEALQ
LSFKNMCKLK PLLNKWLEET DSSSGSPTNL DKIAAQGRKR KKRTSIEVGV KGALESHFLK
CPKPSAHEIT GLADSLQLEK EVVRVWFCNR RQKEKRMTPA AGAGHPPMDD VYAPGELGPG
GGSASPPSAP PPPPPAALHH HHHHTLPGSV Q
