ID   P3F1B_XENLA             Reviewed;         375 AA.
AC   Q561L5;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=POU domain, class 3, transcription factor 1-B;
DE   AltName: Full=Homeotic protein NRL-34 {ECO:0000303|PubMed:2235499};
DE            Short=XlNRL-34;
DE   AltName: Full=Homeotic protein NRL-34-A;
GN   Name=pou3f1-b; Synonyms=nrl-34 {ECO:0000303|PubMed:2235499}, nrl34-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1] {ECO:0000312|EMBL:AAH93556.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye {ECO:0000312|EMBL:AAH93556.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 220-324.
RC   TISSUE=Neurula {ECO:0000269|PubMed:2235499};
RX   PubMed=2235499; DOI=10.1093/nar/18.20.6131;
RA   Baltzinger M., Stiegler P., Remy P.;
RT   "Cloning and sequencing of POU-boxes expressed in Xenopus laevis neurula
RT   embryos.";
RL   Nucleic Acids Res. 18:6131-6131(1990).
CC   -!- FUNCTION: Acts as a transcription factor (By similarity). May play a
CC       role in neuronal differentiation (By similarity).
CC       {ECO:0000250|UniProtKB:P21952, ECO:0000250|UniProtKB:P31363}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P31361,
CC       ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-
CC       ProRule:PRU00530}.
CC   -!- SIMILARITY: Belongs to the POU transcription factor family. Class-3
CC       subfamily. {ECO:0000255}.
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DR   EMBL; BC093556; AAH93556.1; -; mRNA.
DR   EMBL; X54684; CAA38498.1; -; mRNA.
DR   RefSeq; NP_001096655.1; NM_001103185.1.
DR   AlphaFoldDB; Q561L5; -.
DR   SMR; Q561L5; -.
DR   DNASU; 378582; -.
DR   GeneID; 378582; -.
DR   KEGG; xla:378582; -.
DR   AGR; Xenbase:XB-GENE-866479; -.
DR   Xenbase; XB-GENE-866479; pou3f1.L.
DR   OrthoDB; 4250502at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 378582; Expressed in zone of skin and 5 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0007420; P:brain development; IEA:InterPro.
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; IPR016362; TF_POU_3.
DR   PANTHER; PTHR11636; POU DOMAIN; 1.
DR   PANTHER; PTHR11636:SF133; POU DOMAIN, CLASS 3, TRANSCRIPTION FACTOR 1; 1.
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; 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   Developmental protein; DNA-binding; Homeobox; Neurogenesis; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..375
FT                   /note="POU domain, class 3, transcription factor 1-B"
FT                   /id="PRO_0000389614"
FT   DOMAIN          194..268
FT                   /note="POU-specific"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT   DNA_BIND        286..345
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          56..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          151..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..139
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..200
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   375 AA;  41860 MW;  33DB834E1D5C1257 CRC64;
     MAATAQYLPR NNSLPSNPLM HPDSDRMHQG TTYREVQKMM HQEYLQGLAT NAGHPMSLTH
     HQWLPNPTSD WGSGSHLGAQ AEHGKSGVQS SREDLSSSFH HHRSHLVHQQ TPSSHAWAQS
     GGHHLPSMSP GSNSHQPLIY SQSSYTNLNG MLGPQASSLH HSMRDPLHDD PGVHDTHVES
     PPQHLGHHQD HSDEDAPSSD DLEQFAKQFK QRRIKLGFTQ ADVGLALGTL YGNVFSQTTI
     CRFEALQLSF KNMCKLKPLL NKWLEETDST TGSPTNLDKI AAQGRKRKKR TSIEVGVKGA
     LENHFLKCPK PSAHEITSLA DSLQLEKEVV RVWFCNRRQK EKRMTPAGVP HPPMEDVYSQ
     AETPPLHHTL QTSVQ
//