ID   PO2F3_RAT               Reviewed;         430 AA.
AC   P42571; A0A8I6A0U7; P42572;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2022, sequence version 2.
DT   24-JAN-2024, entry version 156.
DE   RecName: Full=POU domain, class 2, transcription factor 3;
DE   AltName: Full=Octamer-binding protein 11;
DE            Short=Oct-11;
DE   AltName: Full=Octamer-binding transcription factor 11;
DE            Short=OTF-11;
DE   AltName: Full=Transcription factor Skn-1;
GN   Name=Pou2f3; Synonyms=Otf11, Skn-1, Skn1;
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], TISSUE SPECIFICITY, AND FUNCTION (ISOFORMS 1
RP   AND 2).
RC   STRAIN=Fischer; TISSUE=Skin;
RX   PubMed=7682011; DOI=10.1126/science.7682011;
RA   Andersen B., Schonemann M.D., Flynn S.E., Pearse R.V. II, Singh H.,
RA   Rosenfeld M.G.;
RT   "Skn-1a and Skn-1i: two functionally distinct Oct-2-related factors
RT   expressed in epidermis.";
RL   Science 260:78-82(1993).
RN   [2]
RP   ERRATUM OF PUBMED:7682011.
RX   PubMed=8248794;
RA   Andersen B., Schonemann M.D., Flynn S.E., Pearse R.V. II, Singh H.,
RA   Rosenfeld M.G.;
RL   Science 262:1499-1499(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcription factor that binds to the octamer motif (5'-
CC       ATTTGCAT-3') and regulates cell type-specific differentiation pathways.
CC       Involved in the regulation of keratinocytes differentiation
CC       (PubMed:7682011). The POU2F3-POU2AF2/POU2AF3 complex drives the
CC       expression of tuft-cell-specific genes, a rare chemosensory cells that
CC       coordinate immune and neural functions within mucosal epithelial
CC       tissues (By similarity). {ECO:0000250|UniProtKB:Q9UKI9,
CC       ECO:0000269|PubMed:7682011}.
CC   -!- FUNCTION: [Isoform 2]: Inhibits transactivation by POU2F1.
CC       {ECO:0000269|PubMed:7682011}.
CC   -!- SUBUNIT: Interacts (via the POU domain) with POU2AF1 and POU2AF2 in a
CC       DNA-dependent manner; this interaction recruits POU2AF2 to chromatin
CC       and increases POU2F3 transactivation activity.
CC       {ECO:0000250|UniProtKB:Q9UKI9}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P31362}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Skn-1a {ECO:0000303|PubMed:7682011};
CC         IsoId=P42571-1; Sequence=Displayed;
CC       Name=2; Synonyms=Skn-1i {ECO:0000303|PubMed:7682011};
CC         IsoId=P42571-2; Sequence=VSP_002332;
CC   -!- TISSUE SPECIFICITY: Expressed in epidermis and hair follicles.
CC       {ECO:0000269|PubMed:7682011}.
CC   -!- SIMILARITY: Belongs to the POU transcription factor family. Class-2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; L23862; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; L23863; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; CH473975; EDL95261.1; -; Genomic_DNA.
DR   PIR; A46216; A46216.
DR   RefSeq; NP_001099215.1; NM_001105745.1. [P42571-1]
DR   AlphaFoldDB; P42571; -.
DR   SMR; P42571; -.
DR   STRING; 10116.ENSRNOP00000012170; -.
DR   PhosphoSitePlus; P42571; -.
DR   PaxDb; 10116-ENSRNOP00000012170; -.
DR   Ensembl; ENSRNOT00000107784.1; ENSRNOP00000084235.1; ENSRNOG00000009118.7. [P42571-1]
DR   Ensembl; ENSRNOT00055033337; ENSRNOP00055027048; ENSRNOG00055019514. [P42571-1]
DR   Ensembl; ENSRNOT00060037565; ENSRNOP00060030961; ENSRNOG00060021548. [P42571-1]
DR   Ensembl; ENSRNOT00065044129; ENSRNOP00065036211; ENSRNOG00065025576. [P42571-1]
DR   GeneID; 116544; -.
DR   KEGG; rno:116544; -.
DR   UCSC; RGD:621691; rat. [P42571-1]
DR   AGR; RGD:621691; -.
DR   CTD; 25833; -.
DR   RGD; 621691; Pou2f3.
DR   eggNOG; KOG3802; Eukaryota.
DR   GeneTree; ENSGT00940000157627; -.
DR   InParanoid; P42571; -.
DR   OMA; VKTCHLT; -.
DR   PhylomeDB; P42571; -.
DR   PRO; PR:P42571; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Proteomes; UP000234681; Chromosome 8.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; ISO:RGD.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR   GO; GO:0030154; P:cell differentiation; ISO:RGD.
DR   GO; GO:0008544; P:epidermis development; IDA:RGD.
DR   GO; GO:0030216; P:keratinocyte differentiation; ISO:RGD.
DR   GO; GO:0043922; P:negative regulation by host of viral transcription; IEA:Ensembl.
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; IDA:RGD.
DR   GO; GO:0042060; P:wound healing; ISO:RGD.
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:SF81; POU DOMAIN, CLASS 2, TRANSCRIPTION FACTOR 3; 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; Alternative splicing; DNA-binding; Homeobox; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..430
FT                   /note="POU domain, class 2, transcription factor 3"
FT                   /id="PRO_0000100719"
FT   DOMAIN          176..250
FT                   /note="POU-specific"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT   DNA_BIND        274..333
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          60..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          129..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          248..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          355..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..147
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..267
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..113
FT                   /note="MVNLEPMHTEIKMSGDVADSTDARSTFGQVESGNDRNGLDFNRQIKTEDLGD
FT                   TLQQSLSHRPCHLSQGPTMMPGNQMSGDMASLHPLQQLVLVPGHLQSVSQFLLSQTPPG
FT                   QQ -> MVSMFSLSFKWPGFCLFVCLFLCPFVLPCHS (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_002332"
FT   CONFLICT        55..56
FT                   /note="QQ -> HE (in Ref. 1; no nucleotide entry)"
FT   CONFLICT        66..67
FT                   /note="SQ -> TE (in Ref. 1; no nucleotide entry)"
FT   CONFLICT        254
FT                   /note="S -> A (in Ref. 1; no nucleotide entry)"
SQ   SEQUENCE   430 AA;  46805 MW;  44C12255EDC9C71D CRC64;
     MVNLEPMHTE IKMSGDVADS TDARSTFGQV ESGNDRNGLD FNRQIKTEDL GDTLQQSLSH
     RPCHLSQGPT MMPGNQMSGD MASLHPLQQL VLVPGHLQSV SQFLLSQTPP GQQGLQPNLL
     SFPQQQSTLL LPQTGPGLTS QAVGRPGLSG SSLEPHLEAS QHLPGPKHLP GPGGNDEPTD
     LEELEKFAKT FKQRRIKLGF TQGDVGLAMG KLYGNDFSQT TISRFEALNL SFKNMCKLKP
     LLEKWLNDAE SSPSDPSAST PSSYPTLSEV FGRKRKKRTS IETNIRLTLE KRFQDNPKPS
     SEEISMIAEQ LSMEKEVVRV WFCNRRQKEK RINCPVATPV KPPIYNSRLV SPSGSLGSLS
     VPPVHSTMPG TVTSSCSPGN NSRPSSPGSG LHASSPTASQ NNSKAAMNPS SAAFNSSGSW
     YRWNHPAYLH
//