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 02-OCT-2024, entry version 216. DE RecName: Full=Pre-B-cell leukemia transcription factor 1; DE AltName: Full=Homeobox protein PBX1; GN Name=Pbx1; Synonyms=Pbx-1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PBX1B), PARTIAL PROTEIN SEQUENCE, AND RP FUNCTION. RC TISSUE=Adrenal gland; RX PubMed=7913464; DOI=10.1016/s0021-9258(17)32223-8; 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 the RT 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/6J; 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP FUNCTION, AND INTERACTION WITH HOXA5; HOXB7; HOXB8; HOXC8 AND HOXD4. RX PubMed=7791786; DOI=10.1128/mcb.15.7.3786; RA Lu Q., Knoepfler P.S., Scheele J., Wright D.D., Kamps M.P.; RT "Both Pbx1 and E2A-Pbx1 bind the DNA motif ATCAATCAA cooperatively with the RT products of multiple murine Hox genes, some of which are themselves RT oncogenes."; RL Mol. Cell. Biol. 15:3786-3795(1995). RN [5] RP INTERACTION WITH MEIS1. RX PubMed=9315626; DOI=10.1128/mcb.17.10.5679; 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 but not RT chimeric Pbx proteins."; RL Mol. Cell. Biol. 17:5679-5687(1997). RN [6] RP INTERACTION WITH MEIS1. RX 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 cooperatively RT bind a cAMP-responsive sequence (CRS1) from bovine CYP17."; RL J. Biol. Chem. 273:7941-7948(1998). RN [7] RP IDENTIFICATION IN A COMPLEX WITH PDX1 AND MEIS2. RX PubMed=9710595; DOI=10.1128/mcb.18.9.5109; RA Swift G.H., Liu Y., Rose S.D., Bischof L.J., Steelman S., Buchberg A.M., RA Wright C.V., MacDonald R.J.; RT "An endocrine-exocrine switch in the activity of the pancreatic homeodomain RT protein PDX1 through formation of a trimeric complex with PBX1b and MRG1 RT (MEIS2)."; RL Mol. Cell. Biol. 18:5109-5120(1998). RN [8] RP INTERACTION WITH HOXA9 AND MEIS1. RX PubMed=10082572; DOI=10.1128/mcb.19.4.3051; 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 [9] RP INTERACTION WITH HOXD4; HOXD9; HOXD10 AND MEIS1. RX PubMed=10523646; DOI=10.1128/mcb.19.11.7577; RA Shanmugam K., Green N.C., Rambaldi I., Saragovi H.U., Featherstone M.S.; RT "PBX and MEIS as non-DNA-binding partners in trimeric complexes with HOX RT proteins."; RL Mol. Cell. Biol. 19:7577-7588(1999). RN [10] RP INTERACTION WITH MEIS2, AND IDENTIFICATION IN A COMPLEX WITH PDX1 AND RP MEIS2. RX PubMed=11279116; DOI=10.1074/jbc.m100678200; RA Liu Y., MacDonald R.J., Swift G.H.; RT "DNA binding and transcriptional activation by a PDX1.PBX1b.MEIS2b trimer RT and cooperation with a pancreas-specific basic helix-loop-helix complex."; RL J. Biol. Chem. 276:17985-17993(2001). RN [11] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=12529389; DOI=10.1128/mcb.23.3.831-841.2003; RA Chao S.H., Walker J.R., Chanda S.K., Gray N.S., Caldwell J.S.; RT "Identification of homeodomain proteins, PBX1 and PREP1, involved in the RT transcription of murine leukemia virus."; RL Mol. Cell. Biol. 23:831-841(2003). RN [12] RP FUNCTION. RX PubMed=19799567; DOI=10.1042/bj20090694; RA Mojsin M., Stevanovic M.; RT "PBX1 and MEIS1 up-regulate SOX3 gene expression by direct interaction with RT a consensus binding site within the basal promoter region."; RL Biochem. J. 425:107-116(2009). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [14] RP FUNCTION. RX PubMed=22560297; DOI=10.1016/j.devcel.2012.02.009; RA Koss M., Bolze A., Brendolan A., Saggese M., Capellini T.D., Bojilova E., RA Boisson B., Prall O.W., Elliott D.A., Solloway M., Lenti E., Hidaka C., RA Chang C.P., Mahlaoui N., Harvey R.P., Casanova J.L., Selleri L.; RT "Congenital asplenia in mice and humans with mutations in a Pbx/Nkx2-5/p15 RT module."; RL Dev. Cell 22:913-926(2012). RN [15] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, RP DOMAIN, SITE, AND MUTAGENESIS OF ARG-237; ASN-286 AND ARG-290. RX PubMed=32190943; DOI=10.1096/fj.202000121r; RA Xu X., Zhou Y., Fu B., Zhang J., Dong Z., Zhang X., Shen N., Sun R., RA Tian Z., Wei H.; RT "PBX1 promotes development of natural killer cells by binding directly to RT the Nfil3 promoter."; RL FASEB J. 34:6479-6492(2020). RN [16] RP STRUCTURE BY NMR OF 241-294. RX 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 extension RT upon binding DNA and HOX-derived YPWM peptides(,)."; RL Biochemistry 39:9943-9950(2000). RN [17] 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 homeodomain."; RL J. Biol. Chem. 278:1053-1058(2003). CC -!- FUNCTION: Transcription factor which binds the DNA sequence 5'- CC TGATTGAT-3' as part of a heterodimer with HOX proteins such as HOXA1, CC HOXA5, HOXB7 and HOXB8 (By similarity). Binds the DNA sequence 5'- CC TGATTGAC-3' in complex with a nuclear factor which is not a class I HOX CC protein (By similarity). Has also been shown to bind the DNA sequence CC 5'-ATCAATCAA-3' cooperatively with HOXA5, HOXB7, HOXB8, HOXC8 and HOXD4 CC (PubMed:7791786). Acts as a transcriptional activator of PF4 in complex CC with MEIS1 (By similarity). Also activates transcription of SOX3 in CC complex with MEIS1 by binding to the 5'-TGATTGAC-3' consensus sequence CC (PubMed:19799567). In natural killer cells, binds to the NFIL3 promoter CC and acts as a transcriptional activator of NFIL3, promoting natural CC killer cell development (PubMed:32190943). Plays a role in the cAMP- CC dependent regulation of CYP17A1 gene expression via its cAMP-regulatory CC sequence (CRS1) (PubMed:7913464). Probably in complex with MEIS2, is CC involved in transcriptional regulation by KLF4 (By similarity). Acts as CC a transcriptional activator of NKX2-5 and a transcriptional repressor CC of CDKN2B (PubMed:22560297). Together with NKX2-5, required for spleen CC development through a mechanism that involves CDKN2B repression CC (PubMed:22560297). {ECO:0000250|UniProtKB:P40424, CC ECO:0000269|PubMed:19799567, ECO:0000269|PubMed:22560297, CC ECO:0000269|PubMed:32190943, ECO:0000269|PubMed:7791786, CC ECO:0000269|PubMed:7913464}. CC -!- FUNCTION: [Isoform PBX1b]: As part of a PDX1:PBX1b:MEIS2B complex in CC pancreatic acinar cells, is involved in the transcriptional activation CC of the ELA1 enhancer; the complex binds to the enhancer B element and CC cooperates with the transcription factor 1 complex (PTF1) bound to the CC enhancer A element. {ECO:0000269|PubMed:11279116}. CC -!- FUNCTION: (Microbial infection) In complex with PREP1, binds to the 5'- CC TGATTGAC-3' consensus sequence in the U5 region of Moloney murine CC leukemia virus and promotes viral transcription. CC {ECO:0000269|PubMed:12529389}. CC -!- SUBUNIT: Forms a heterodimer with MEIS1 which binds DNA CC (PubMed:19799567, PubMed:9525891). The PBX1-MEIS1 heterodimer binds a CC cAMP-responsive sequence in CYP17 (PubMed:9525891). It also binds a CC consensus region in the SOX3 promoter (PubMed:19799567). PBX1 forms CC heterotrimers with MEIS1 and a number of HOX proteins including HOXA9, CC HOXD4, HOXD9 and HOXD10 (PubMed:10082572, PubMed:10523646, CC PubMed:12409300, PubMed:9315626). Forms heterodimers with HOXA1, HOXA5, CC HOXB7 and HOXB8 which bind the 5'-TGATTGAT-3' consensus sequence (By CC similarity). Also forms heterodimers with HOXA5, HOXB7, HOXB8, HOXC8 CC and HOXD4 which bind the 5'-ATCAATCAA-3' consensus sequence CC (PubMed:7791786). Interacts with PBXIP1 (By similarity). Interacts with CC TLX1 (By similarity). Interacts with FOXC1 (By similarity). Interacts CC with MN1 (By similarity). {ECO:0000250|UniProtKB:P40424, CC ECO:0000269|PubMed:10082572, ECO:0000269|PubMed:10523646, CC ECO:0000269|PubMed:12409300, ECO:0000269|PubMed:19799567, CC ECO:0000269|PubMed:7791786, ECO:0000269|PubMed:9315626, CC ECO:0000269|PubMed:9525891}. CC -!- SUBUNIT: [Isoform PBX1a]: Interacts with MEIS2 isoform Meis2D, SP1, SP3 CC and KLF4. {ECO:0000250|UniProtKB:P40424}. CC -!- SUBUNIT: [Isoform PBX1b]: Part of a PDX1:PBX1b:MEIS2B complex; PBX1b CC recruits MEIS2B to the complex. {ECO:0000269|PubMed:11279116, CC ECO:0000269|PubMed:9710595}. CC -!- INTERACTION: CC P41778; P09631: Hoxa9; NbExp=2; IntAct=EBI-6996259, EBI-925334; CC P41778; P09023: Hoxb6; NbExp=2; IntAct=EBI-6996259, EBI-15992861; CC P41778; P09632: Hoxb8; NbExp=4; IntAct=EBI-6996259, EBI-925374; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32190943}. 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: Expressed constitutively in natural killer cell CC precursors in bone marrow. {ECO:0000269|PubMed:32190943}. CC -!- DOMAIN: The homeobox is required for PBX1 nuclear localization and for CC transcriptional activation of NFIL3. {ECO:0000269|PubMed:32190943}. CC -!- DISRUPTION PHENOTYPE: Conditional knockout in hematopoietic cells leads CC to a reduction in the number of natural killer cell-committed CC progenitors in bone marrow, decreases the number of natural killer CC cells in bone marrow and spleen and reduces NFIL3 expression in bone CC marrow and splenic natural killer cells. {ECO:0000269|PubMed:32190943}. CC -!- SIMILARITY: Belongs to the TALE/PBX homeobox family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L27453; AAA21832.1; -; mRNA. DR EMBL; AF020196; AAB71191.1; -; mRNA. DR EMBL; BC058390; AAH58390.1; -; mRNA. DR CCDS; CCDS15461.1; -. [P41778-1] DR CCDS; CCDS15462.1; -. [P41778-2] DR PIR; A54863; A54863. DR RefSeq; NP_001278437.1; NM_001291508.1. [P41778-2] DR RefSeq; NP_032809.1; NM_008783.3. [P41778-2] DR RefSeq; NP_899198.1; NM_183355.3. [P41778-1] DR PDB; 1DU6; NMR; -; A=241-294. DR PDB; 1LFU; NMR; -; P=233-313. DR PDBsum; 1DU6; -. DR PDBsum; 1LFU; -. DR AlphaFoldDB; P41778; -. DR BMRB; P41778; -. DR SMR; P41778; -. DR BioGRID; 202037; 23. DR CORUM; P41778; -. DR DIP; DIP-6107N; -. DR IntAct; P41778; 20. DR MINT; P41778; -. DR STRING; 10090.ENSMUSP00000135516; -. DR iPTMnet; P41778; -. DR PhosphoSitePlus; P41778; -. DR PaxDb; 10090-ENSMUSP00000135516; -. DR ProteomicsDB; 287793; -. [P41778-1] DR ProteomicsDB; 287794; -. [P41778-2] DR Pumba; P41778; -. DR Antibodypedia; 1079; 470 antibodies from 37 providers. DR DNASU; 18514; -. DR Ensembl; ENSMUST00000072863.6; ENSMUSP00000072640.5; ENSMUSG00000052534.16. [P41778-2] DR Ensembl; ENSMUST00000176540.8; ENSMUSP00000135516.2; ENSMUSG00000052534.16. [P41778-1] DR Ensembl; ENSMUST00000176790.8; ENSMUSP00000134925.2; ENSMUSG00000052534.16. [P41778-2] DR Ensembl; ENSMUST00000188912.7; ENSMUSP00000140606.2; ENSMUSG00000052534.16. [P41778-2] DR GeneID; 18514; -. DR KEGG; mmu:18514; -. DR UCSC; uc007dle.2; mouse. [P41778-1] DR AGR; MGI:97495; -. DR CTD; 5087; -. DR MGI; MGI:97495; Pbx1. DR VEuPathDB; HostDB:ENSMUSG00000052534; -. DR eggNOG; KOG0774; Eukaryota. DR GeneTree; ENSGT00940000154374; -. DR HOGENOM; CLU_041153_1_0_1; -. DR InParanoid; P41778; -. DR OMA; STPNSAX; -. DR OrthoDB; 3684468at2759; -. DR PhylomeDB; P41778; -. DR TreeFam; TF314340; -. DR BioGRID-ORCS; 18514; 1 hit in 79 CRISPR screens. DR ChiTaRS; Pbx1; mouse. DR EvolutionaryTrace; P41778; -. DR PRO; PR:P41778; -. DR Proteomes; UP000000589; Chromosome 1. DR RNAct; P41778; protein. DR Bgee; ENSMUSG00000052534; Expressed in rostral migratory stream and 239 other cell types or tissues. DR ExpressionAtlas; P41778; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl. DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProtKB. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI. DR GO; GO:0001222; F:transcription corepressor binding; IEA:Ensembl. DR GO; GO:0030325; P:adrenal gland development; IMP:MGI. DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI. DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI. DR GO; GO:0007420; P:brain development; IBA:GO_Central. DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IDA:MGI. DR GO; GO:0008283; P:cell population proliferation; IMP:MGI. DR GO; GO:0035162; P:embryonic hemopoiesis; IMP:MGI. DR GO; GO:0030326; P:embryonic limb morphogenesis; IGI:MGI. DR GO; GO:0048568; P:embryonic organ development; IMP:MGI. DR GO; GO:0048706; P:embryonic skeletal system development; IMP:MGI. DR GO; GO:0001654; P:eye development; IBA:GO_Central. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:MGI. DR GO; GO:0001779; P:natural killer cell differentiation; IMP:UniProtKB. DR GO; GO:0045665; P:negative regulation of neuron differentiation; IGI:MGI. DR GO; GO:0048666; P:neuron development; IBA:GO_Central. DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:MGI. DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0009954; P:proximal/distal pattern formation; IMP:MGI. DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI. DR GO; GO:0030278; P:regulation of ossification; IMP:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0007548; P:sex differentiation; IEA:UniProtKB-KW. DR GO; GO:0048536; P:spleen development; IMP:MGI. DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI. DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0048538; P:thymus development; IMP:MGI. DR GO; GO:0001655; P:urogenital system development; IMP:MGI. DR CDD; cd00086; homeodomain; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. DR InterPro; IPR001356; HD. DR InterPro; IPR017970; Homeobox_CS. DR InterPro; IPR009057; Homeodomain-like_sf. DR InterPro; IPR008422; KN_HD. DR InterPro; IPR005542; PBX_PBC_dom. DR InterPro; IPR050224; TALE_homeobox. DR PANTHER; PTHR11850; HOMEOBOX PROTEIN TRANSCRIPTION FACTORS; 1. DR PANTHER; PTHR11850:SF89; PRE-B-CELL LEUKEMIA TRANSCRIPTION FACTOR 1; 1. DR Pfam; PF05920; Homeobox_KN; 1. DR Pfam; PF03792; PBC; 1. DR SMART; SM00389; HOX; 1. DR SUPFAM; SSF46689; Homeodomain-like; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS51978; PBC; 1. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; Developmental protein; KW Differentiation; Direct protein sequencing; DNA-binding; Homeobox; Nucleus; KW Reference proteome; Sexual differentiation; Steroidogenesis; Transcription; KW Transcription regulation. FT CHAIN 1..430 FT /note="Pre-B-cell leukemia transcription factor 1" FT /id="PRO_0000049236" FT DOMAIN 38..232 FT /note="PBC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01322" FT DNA_BIND 233..295 FT /note="Homeobox; TALE-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108" FT REGION 1..40 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 45..124 FT /note="PBC-A" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01322" FT REGION 127..232 FT /note="PBC-B" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01322" FT REGION 317..338 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 395..430 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 286 FT /note="Required for binding to the NFIL3 promoter" FT /evidence="ECO:0000269|PubMed:32190943" FT VAR_SEQ 334..347 FT /note="SSSSFNMSNSGDLF -> GYPSPCYQPDRRIQ (in isoform PBX1b)" FT /evidence="ECO:0000303|PubMed:7913464" FT /id="VSP_002273" FT VAR_SEQ 348..430 FT /note="Missing (in isoform PBX1b)" FT /evidence="ECO:0000303|PubMed:7913464" FT /id="VSP_002274" FT MUTAGEN 237 FT /note="R->A: Slightly reduced binding to NFIL3 promoter." FT /evidence="ECO:0000269|PubMed:32190943" FT MUTAGEN 286 FT /note="N->A: Significantly reduced binding to NFIL3 FT promoter." FT /evidence="ECO:0000269|PubMed:32190943" FT MUTAGEN 290 FT /note="R->A: Slightly reduced binding to NFIL3 promoter." FT /evidence="ECO:0000269|PubMed:32190943" FT STRAND 236..240 FT /evidence="ECO:0007829|PDB:1LFU" FT TURN 241..243 FT /evidence="ECO:0007829|PDB:1DU6" FT HELIX 244..254 FT /evidence="ECO:0007829|PDB:1DU6" FT TURN 255..257 FT /evidence="ECO:0007829|PDB:1DU6" FT HELIX 263..273 FT /evidence="ECO:0007829|PDB:1DU6" FT HELIX 277..287 FT /evidence="ECO:0007829|PDB:1DU6" FT TURN 288..290 FT /evidence="ECO:0007829|PDB:1DU6" FT HELIX 295..307 FT /evidence="ECO:0007829|PDB:1LFU" 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 //