ID   PBX1_MOUSE              Reviewed;         430 AA.
AC   P41778;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2002, sequence version 2.
DT   15-JAN-2008, entry version 81.
DE   Pre-B-cell leukemia transcription factor 1 (Homeobox protein PBX1).
GN   Name=Pbx1; Synonyms=Pbx-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PBX1B), AND PARTIAL PROTEIN
RP   SEQUENCE.
RC   TISSUE=Adrenal gland;
RX   MEDLINE=94308119; PubMed=7913464;
RA   Kagawa N., Ogo A., Takahashi Y., Iwamatsu A., Waterman M.R.;
RT   "A cAMP-regulatory sequence (CRS1) of CYP17 is a cellular target for
RT   the homeodomain protein Pbx1.";
RL   J. Biol. Chem. 269:18716-18719(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PBX1A).
RA   Liu Y., MacDonald R.J.;
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PBX1A).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH MEIS1.
RX   PubMed=9315626;
RA   Chang C.-P., Jacobs Y., Nakamura T., Jenkins N.A., Copeland N.G.,
RA   Cleary M.L.;
RT   "Meis proteins are major in vivo DNA binding partners for wild-type
RT   but not chimeric Pbx proteins.";
RL   Mol. Cell. Biol. 17:5679-5687(1997).
RN   [5]
RP   INTERACTION WITH MEIS1.
RX   MEDLINE=98192578; PubMed=9525891; DOI=10.1074/jbc.273.14.7941;
RA   Bischof L.J., Kagawa N., Moskow J.J., Takahashi Y., Iwamatsu A.,
RA   Buchberg A.M., Waterman M.R.;
RT   "Members of the Meis1 and Pbx homeodomain protein families
RT   cooperatively bind a cAMP-responsive sequence (CRS1) from bovine
RT   CYP17.";
RL   J. Biol. Chem. 273:7941-7948(1998).
RN   [6]
RP   INTERACTION WITH HOXA9 AND MEIS1.
RX   MEDLINE=99182493; PubMed=10082572;
RA   Shen W.-F., Rozenfeld S., Kwong A., Koemueves L.G., Lawrence H.J.,
RA   Largman C.;
RT   "HOXA9 forms triple complexes with PBX2 and MEIS1 in myeloid cells.";
RL   Mol. Cell. Biol. 19:3051-3061(1999).
RN   [7]
RP   INTERACTION WITH HOXD4; HOXD9; HOXD10 AND MEIS1.
RX   PubMed=10523646;
RA   Shanmugam K., Green N.C., Rambaldi I., Saragovi H.U.,
RA   Featherstone M.S.;
RT   "PBX and MEIS as non-DNA-binding partners in trimeric complexes with
RT   HOX proteins.";
RL   Mol. Cell. Biol. 19:7577-7588(1999).
RN   [8]
RP   STRUCTURE BY NMR OF 241-294.
RX   MEDLINE=20393887; PubMed=10933814; DOI=10.1021/bi0001067;
RA   Sprules T., Green N., Featherstone M., Gehring K.;
RT   "Conformational changes in the PBX homeodomain and C-terminal
RT   extension upon binding DNA and HOX-derived YPWM peptides(,).";
RL   Biochemistry 39:9943-9950(2000).
RN   [9]
RP   STRUCTURE BY NMR OF 233-313 IN COMPLEX WITH DNA.
RX   PubMed=12409300; DOI=10.1074/jbc.M207504200;
RA   Sprules T., Green N., Featherstone M., Gehring K.;
RT   "Lock and key binding of the HOX YPWM peptide to the PBX
RT   homeodomain.";
RL   J. Biol. Chem. 278:1053-1058(2003).
CC   -!- FUNCTION: Plays a role in the cAMP-dependent regulation of CYP17
CC       gene expression via its cAMP-regulatory sequence (CRS1) 5'-
CC       ATCAATCAA-3'. Acts as a transcriptional activator of PF4 in
CC       complex with MEIS1. May have a role in steroidogenesis and,
CC       subsequently, sexual development and differentiation.
CC   -!- SUBUNIT: Forms a heterodimer with MEIS1 which binds DNA including
CC       a cAMP-responsive sequence in CYP17. Also forms heterotrimers with
CC       MEIS1 and a number of HOX proteins including HOXA9, HOXD4, HOXD9
CC       and HOXD10. Interacts with PBXIP1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=PBX1a;
CC         IsoId=P41778-1; Sequence=Displayed;
CC       Name=PBX1b;
CC         IsoId=P41778-2; Sequence=VSP_002273, VSP_002274;
CC   -!- TISSUE SPECIFICITY: Widely distributed in steroidogenic and non-
CC       steroidogenic cells.
CC   -!- SIMILARITY: Belongs to the TALE/PBX homeobox family.
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain.
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DR   EMBL; L27453; AAA21832.1; -; mRNA.
DR   EMBL; AF020196; AAB71191.1; -; mRNA.
DR   EMBL; BC058390; AAH58390.1; -; mRNA.
DR   PIR; A54863; A54863.
DR   RefSeq; NP_899198.1; -.
DR   UniGene; Mm.43358; -.
DR   UniGene; Mm.440114; -.
DR   PDB; 1DU6; NMR; -; A=241-294.
DR   PDB; 1LFU; NMR; -; P=233-313.
DR   PDBsum; 1DU6; -.
DR   PDBsum; 1LFU; -.
DR   DIP; DIP:6107N; -.
DR   TRANSFAC; T02088; -.
DR   TRANSFAC; T03451; -.
DR   Ensembl; ENSMUSG00000052534; Mus musculus.
DR   GeneID; 18514; -.
DR   MGI; MGI:97495; Pbx1.
DR   ArrayExpress; P41778; -.
DR   CleanEx; MM_PBX1; -.
DR   GermOnline; ENSMUSG00000052534; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
DR   GO; GO:0030325; P:adrenal gland development; IMP:MGI.
DR   GO; GO:0048568; P:embryonic organ development; IMP:MGI.
DR   GO; GO:0009887; P:organ morphogenesis; IMP:MGI.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from R...; IDA:MGI.
DR   GO; GO:0048536; P:spleen development; IGI:MGI.
DR   GO; GO:0048538; P:thymus development; IMP:MGI.
DR   GO; GO:0001658; P:ureteric bud branching; IDA:MGI.
DR   InterPro; IPR001356; Homeobox.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR005542; PBX.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Pfam; PF00046; Homeobox; 1.
DR   Pfam; PF03792; PBC; 1.
DR   PRINTS; PR00024; HOMEOBOX.
DR   ProDom; PD000010; Homeobox; 1.
DR   SMART; SM00389; HOX; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; Differentiation;
KW   Direct protein sequencing; DNA-binding; Homeobox; Nucleus;
KW   Sexual differentiation; Steroidogenesis; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    430       Pre-B-cell leukemia transcription factor
FT                                1.
FT                                /FTId=PRO_0000049236.
FT   DNA_BIND    233    295       Homeobox; TALE-type.
FT   COMPBIAS    127    135       Poly-Ala.
FT   VAR_SEQ     334    347       SSSSFNMSNSGDLF -> GYPSPCYQPDRRIQ (in
FT                                isoform PBX1b).
FT                                /FTId=VSP_002273.
FT   VAR_SEQ     348    430       Missing (in isoform PBX1b).
FT                                /FTId=VSP_002274.
FT   STRAND      236    240
FT   TURN        241    243
FT   HELIX       244    254
FT   TURN        255    257
FT   HELIX       263    273
FT   HELIX       277    287
FT   TURN        288    290
FT   HELIX       295    307
SQ   SEQUENCE   430 AA;  46626 MW;  AD3FFACBC5A9E715 CRC64;
     MDEQPRLMHS HAGVGMAGHP GLSQHLQDGA GGTEGEGGRK QDIGDILQQI MTITDQSLDE
     AQARKHALNC HRMKPALFNV LCEIKEKTVL SIRGAQEEEP TDPQLMRLDN MLLAEGVAGP
     EKGGGSAAAA AAAAASGGAG SDNSVEHSDY RAKLSQIRQI YHTELEKYEQ ACNEFTTHVM
     NLLREQSRTR PISPKEIERM VSIIHRKFSS IQMQLKQSTC EAVMILRSRF LDARRKRRNF
     NKQATEILNE YFYSHLSNPY PSEEAKEELA KKCGITVSQV SNWFGNKRIR YKKNIGKFQE
     EANIYAAKTA VTATNVSAHG SQANSPSTPN SAGSSSSFNM SNSGDLFMSV QSLNGDSYQG
     AQVGANVQSQ VDTLRHVISQ TGGYSDGLAA SQMYSPQGIS ANGGWQDATT PSSVTSPTEG
     PGSVHSDTSN
//