ID BRDT_MOUSE Reviewed; 956 AA. AC Q91Y44; G3X8Z8; Q59HJ4; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2012, sequence version 3. DT 27-MAR-2024, entry version 151. DE RecName: Full=Bromodomain testis-specific protein; DE AltName: Full=Bromodomain-containing female sterile homeotic-like protein; DE AltName: Full=RING3-like protein; GN Name=Brdt; Synonyms=Fsrg3; 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 1), AND TISSUE SPECIFICITY. RC TISSUE=Testis; RX PubMed=15261828; DOI=10.1016/j.modgep.2004.03.002; RA Shang E., Salazar G., Crowley T.E., Wang X., Lopez R.A., Wang X., RA Wolgemuth D.J.; RT "Identification of unique, differentiation stage-specific patterns of RT expression of the bromodomain-containing genes Brd2, Brd3, Brd4, and Brdt RT in the mouse testis."; RL Gene Expr. Patterns 4:513-519(2004). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Testis; RA Taniguchi Y.; RT "The Brd paralogous genes: testis-specific expression of the splicing RT variants."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). 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. RN [5] RP FUNCTION, INTERACTION WITH HISTONE H4, AND MUTAGENESIS OF 50-PRO-PHE-51; RP VAL-55; 293-PRO-PHE-294 AND VAL-298. RX PubMed=12861021; DOI=10.1128/mcb.23.15.5354-5365.2003; RA Pivot-Pajot C., Caron C., Govin J., Vion A., Rousseaux S., Khochbin S.; RT "Acetylation-dependent chromatin reorganization by BRDT, a testis-specific RT bromodomain-containing protein."; RL Mol. Cell. Biol. 23:5354-5365(2003). RN [6] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE. RX PubMed=17728347; DOI=10.1242/dev.004481; RA Shang E., Nickerson H.D., Wen D., Wang X., Wolgemuth D.J.; RT "The first bromodomain of Brdt, a testis-specific member of the BET sub- RT family of double-bromodomain-containing proteins, is essential for male RT germ cell differentiation."; RL Development 134:3507-3515(2007). RN [7] RP TISSUE SPECIFICITY. RX PubMed=17049203; DOI=10.1016/j.ygeno.2006.09.002; RA Paillisson A., Levasseur A., Gouret P., Callebaut I., Bontoux M., RA Pontarotti P., Monget P.; RT "Bromodomain testis-specific protein is expressed in mouse oocyte and RT evolves faster than its ubiquitously expressed paralogs BRD2, -3, and -4."; RL Genomics 89:215-223(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [9] RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE. RX PubMed=22020252; DOI=10.1016/j.ydbio.2011.10.005; RA Berkovits B.D., Wolgemuth D.J.; RT "The first bromodomain of the testis-specific double bromodomain protein RT Brdt is required for chromocenter organization that is modulated by genetic RT background."; RL Dev. Biol. 360:358-368(2011). RN [10] RP FUNCTION. RX PubMed=22901802; DOI=10.1016/j.cell.2012.06.045; RA Matzuk M.M., McKeown M.R., Filippakopoulos P., Li Q., Ma L., Agno J.E., RA Lemieux M.E., Picaud S., Yu R.N., Qi J., Knapp S., Bradner J.E.; RT "Small-molecule inhibition of BRDT for male contraception."; RL Cell 150:673-684(2012). RN [11] RP FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND INTERACTION WITH RP CDK9 AND CCNT1. RX PubMed=22922464; DOI=10.1038/emboj.2012.233; RA Gaucher J., Boussouar F., Montellier E., Curtet S., Buchou T., Bertrand S., RA Hery P., Jounier S., Depaux A., Vitte A.L., Guardiola P., Pernet K., RA Debernardi A., Lopez F., Holota H., Imbert J., Wolgemuth D.J., Gerard M., RA Rousseaux S., Khochbin S.; RT "Bromodomain-dependent stage-specific male genome programming by Brdt."; RL EMBO J. 31:3809-3820(2012). RN [12] RP FUNCTION, AND INTERACTION WITH SRSF2; DDX5; HNRNPK AND TARDBP. RX PubMed=22570411; DOI=10.1093/nar/gks342; RA Berkovits B.D., Wang L., Guarnieri P., Wolgemuth D.J.; RT "The testis-specific double bromodomain-containing protein BRDT forms a RT complex with multiple spliceosome components and is required for mRNA RT splicing and 3'-UTR truncation in round spermatids."; RL Nucleic Acids Res. 40:7162-7175(2012). RN [13] RP FUNCTION, AND DOMAIN. RX PubMed=27105113; DOI=10.1016/j.molcel.2016.03.014; RA Goudarzi A., Zhang D., Huang H., Barral S., Kwon O.K., Qi S., Tang Z., RA Buchou T., Vitte A.L., He T., Cheng Z., Montellier E., Gaucher J., RA Curtet S., Debernardi A., Charbonnier G., Puthier D., Petosa C., Panne D., RA Rousseaux S., Roeder R.G., Zhao Y., Khochbin S.; RT "Dynamic competing histone H4 K5K8 acetylation and butyrylation are RT hallmarks of highly active gene promoters."; RL Mol. Cell 62:169-180(2016). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 17-136 AND 257-382 IN COMPLEX WITH RP HISTONE H4 PEPTIDE, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=19794495; DOI=10.1038/nature08397; RA Moriniere J., Rousseaux S., Steuerwald U., Soler-Lopez M., Curtet S., RA Vitte A.L., Govin J., Gaucher J., Sadoul K., Hart D.J., Krijgsveld J., RA Khochbin S., Muller C.W., Petosa C.; RT "Cooperative binding of two acetylation marks on a histone tail by a single RT bromodomain."; RL Nature 461:664-668(2009). CC -!- FUNCTION: Testis-specific chromatin protein that specifically binds CC histone H4 acetylated at 'Lys-5' and 'Lys-8' (H4K5ac and H4K8ac, CC respectively) and plays a key role in spermatogenesis (PubMed:12861021, CC PubMed:19794495, PubMed:22901802, PubMed:22922464). Required in late CC pachytene spermatocytes: plays a role in meiotic and post-meiotic cells CC by binding to acetylated histones at the promoter of specific meiotic CC and post-meiotic genes, facilitating their activation at the CC appropriate time. In the post-meiotic phase of spermatogenesis, binds CC to hyperacetylated histones and participates in their general removal CC from DNA (PubMed:22901802). Also recognizes and binds a subset of CC butyrylated histones: able to bind histone H4 butyrylated at 'Lys-8' CC (H4K8ac), while it is not able to bind H4 butyrylated at 'Lys-5' CC (H4K5ac) (PubMed:27105113). Also acts as a component of the splicing CC machinery in pachytene spermatocytes and round spermatids and CC participates in 3'-UTR truncation of specific mRNAs in post-meiotic CC spermatids (PubMed:22570411). Required for chromocenter organization, a CC structure comprised of peri-centromeric heterochromatin CC (PubMed:22020252). {ECO:0000269|PubMed:12861021, CC ECO:0000269|PubMed:19794495, ECO:0000269|PubMed:22020252, CC ECO:0000269|PubMed:22570411, ECO:0000269|PubMed:22901802, CC ECO:0000269|PubMed:22922464, ECO:0000269|PubMed:27105113}. CC -!- SUBUNIT: Interacts with SMARCE1 (By similarity). Interacts with mRNA CC splicing machinery proteins SRSF2, DDX5, HNRNPK and TARDBP. Interacts CC with the acetylated N-terminus of histone H1, H2, H3 and H4. Interacts CC with P-TEFb components CDK9 and CCNT1/cyclin-T1. CC {ECO:0000250|UniProtKB:Q58F21, ECO:0000269|PubMed:12861021, CC ECO:0000269|PubMed:19794495, ECO:0000269|PubMed:22570411, CC ECO:0000269|PubMed:22922464}. CC -!- INTERACTION: CC Q91Y44; Q9QWV9: Ccnt1; NbExp=2; IntAct=EBI-6260929, EBI-2655009; CC Q91Y44; Q99J95: Cdk9; NbExp=3; IntAct=EBI-6260929, EBI-2654963; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17728347, CC ECO:0000269|PubMed:19794495, ECO:0000269|PubMed:22020252}. CC Note=Detected on chromatin (PubMed:19794495). Excluded from the CC chromocenter. {ECO:0000269|PubMed:19794495, CC ECO:0000269|PubMed:22020252}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q91Y44-1; Sequence=Displayed; CC Name=2; CC IsoId=Q91Y44-2; Sequence=VSP_019119, VSP_019120; CC -!- TISSUE SPECIFICITY: Testis-specific. Expressed in germinal cells from CC the early meiotic (pachytene) spermatocytes and during spermiogenesis CC in the round and elongating spermatids until the condensed late CC spermatids. No expression seen in spermatogonia. CC {ECO:0000269|PubMed:15261828, ECO:0000269|PubMed:17049203, CC ECO:0000269|PubMed:17728347}. CC -!- DEVELOPMENTAL STAGE: First detected when type B spermatogonia give rise CC to early meiotic cells (preleptotene, leptotene and zygotene) at 10-12 CC days post partum (dpp), producing a clearly detectable protein at 12 CC dpp (at protein level). {ECO:0000269|PubMed:22922464}. CC -!- DOMAIN: Bromo domains mediate interaction with histones that have CC acetylated lysine residues at specific positions. Bromo domain 1 CC mediates binding with histone H4 acetylated at 'Lys-5' and 'Lys-8' CC (H4K5ac and H4K8ac, respectively) (PubMed:19794495). The bromo domains CC also recognize and bind a subset of butyrylated histones: able to bind CC histone H4 butyrylated at 'Lys-8' (H4K8ac), while it is not able to CC bind H4 butyrylated at 'Lys-5' (H4K5ac) (PubMed:27105113). CC {ECO:0000269|PubMed:19794495, ECO:0000269|PubMed:27105113}. CC -!- DISRUPTION PHENOTYPE: Mice are viable but males are sterile, producing CC fewer and morphologically abnormal sperm. Aberrant morphogenesis are CC first detected in step 9 elongating spermatids, and those elongated CC spermatids that are formed lack the distinctive foci of heterochromatin CC at the peri-nuclear envelope. Spermatid nuclei show a fragmented CC chromocenter. {ECO:0000269|PubMed:17728347, CC ECO:0000269|PubMed:22020252, ECO:0000269|PubMed:22922464}. CC -!- MISCELLANEOUS: Brdt is a promising target for male contraception. CC Inhibition by thienodiazepine inhibitor (+)-JQ1 that binds Asn-108, CC prevents recognition of acetylated histone H4. Treatment of mice with CC JQ1 reduces seminiferous tubule area, testis size and spermatozoa CC number and motility without affecting hormone levels. JQ1 causes a CC complete and reversible contraceptive effect in male mice CC (PubMed:22901802). {ECO:0000305|PubMed:22901802}. CC -!- SIMILARITY: Belongs to the BET family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Asking life to be patient CC - Issue 144 of November 2012; CC URL="https://web.expasy.org/spotlight/back_issues/144"; 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; AF358660; AAK50736.1; -; mRNA. DR EMBL; AB208640; BAD91553.1; -; mRNA. DR EMBL; AC126598; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466529; EDL20168.1; -; Genomic_DNA. DR CCDS; CCDS19500.1; -. [Q91Y44-1] DR CCDS; CCDS39197.1; -. [Q91Y44-2] DR RefSeq; NP_001073342.1; NM_001079873.1. [Q91Y44-2] DR RefSeq; NP_473395.2; NM_054054.2. [Q91Y44-1] DR PDB; 2WP1; X-ray; 2.10 A; A/B=257-382. DR PDB; 2WP2; X-ray; 2.37 A; A/B=17-136. DR PDBsum; 2WP1; -. DR PDBsum; 2WP2; -. DR AlphaFoldDB; Q91Y44; -. DR SMR; Q91Y44; -. DR BioGRID; 227777; 2. DR DIP; DIP-48975N; -. DR IntAct; Q91Y44; 6. DR MINT; Q91Y44; -. DR STRING; 10090.ENSMUSP00000031215; -. DR GuidetoPHARMACOLOGY; 2729; -. DR GlyGen; Q91Y44; 6 sites, 1 O-linked glycan (6 sites). DR iPTMnet; Q91Y44; -. DR PhosphoSitePlus; Q91Y44; -. DR MaxQB; Q91Y44; -. DR PaxDb; 10090-ENSMUSP00000031215; -. DR PeptideAtlas; Q91Y44; -. DR ProteomicsDB; 273763; -. [Q91Y44-1] DR ProteomicsDB; 273764; -. [Q91Y44-2] DR Antibodypedia; 3212; 140 antibodies from 23 providers. DR DNASU; 114642; -. DR Ensembl; ENSMUST00000031215.15; ENSMUSP00000031215.9; ENSMUSG00000029279.16. [Q91Y44-1] DR Ensembl; ENSMUST00000112677.10; ENSMUSP00000108297.4; ENSMUSG00000029279.16. [Q91Y44-2] DR GeneID; 114642; -. DR KEGG; mmu:114642; -. DR UCSC; uc008ymb.1; mouse. [Q91Y44-2] DR UCSC; uc008ymc.1; mouse. [Q91Y44-1] DR AGR; MGI:1891374; -. DR CTD; 676; -. DR MGI; MGI:1891374; Brdt. DR VEuPathDB; HostDB:ENSMUSG00000029279; -. DR eggNOG; KOG1474; Eukaryota. DR GeneTree; ENSGT00940000154549; -. DR HOGENOM; CLU_001499_0_0_1; -. DR InParanoid; Q91Y44; -. DR OMA; DFKTMFL; -. DR OrthoDB; 152619at2759; -. DR PhylomeDB; Q91Y44; -. DR TreeFam; TF317345; -. DR BioGRID-ORCS; 114642; 0 hits in 82 CRISPR screens. DR ChiTaRS; Brdt; mouse. DR EvolutionaryTrace; Q91Y44; -. DR PRO; PR:Q91Y44; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; Q91Y44; Protein. DR Bgee; ENSMUSG00000029279; Expressed in animal zygote and 194 other cell types or tissues. DR GO; GO:0000785; C:chromatin; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0042393; F:histone binding; IDA:UniProtKB. DR GO; GO:0140566; F:histone reader activity; IMP:UniProtKB. DR GO; GO:0070577; F:lysine-acetylated histone binding; IMP:UniProtKB. DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB. DR GO; GO:0007141; P:male meiosis I; IMP:UniProtKB. DR GO; GO:0007140; P:male meiotic nuclear division; IMP:UniProtKB. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:0043484; P:regulation of RNA splicing; IMP:UniProtKB. DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR GO; GO:0035092; P:sperm DNA condensation; IMP:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB. DR CDD; cd05497; Bromo_Brdt_I_like; 1. DR CDD; cd05498; Bromo_Brdt_II_like; 1. DR Gene3D; 1.20.1270.220; -; 1. DR Gene3D; 1.20.920.10; Bromodomain-like; 2. DR InterPro; IPR031354; BRD4_CDT. DR InterPro; IPR043508; Bromo_Brdt_I. DR InterPro; IPR043509; Bromo_Brdt_II. DR InterPro; IPR001487; Bromodomain. DR InterPro; IPR036427; Bromodomain-like_sf. DR InterPro; IPR018359; Bromodomain_CS. DR InterPro; IPR027353; NET_dom. DR InterPro; IPR038336; NET_sf. DR PANTHER; PTHR22880:SF175; BROMODOMAIN TESTIS-SPECIFIC PROTEIN; 1. DR PANTHER; PTHR22880; FALZ-RELATED BROMODOMAIN-CONTAINING PROTEINS; 1. DR Pfam; PF17035; BET; 1. DR Pfam; PF17105; BRD4_CDT; 1. DR Pfam; PF00439; Bromodomain; 2. DR PRINTS; PR00503; BROMODOMAIN. DR SMART; SM00297; BROMO; 2. DR SUPFAM; SSF47370; Bromodomain; 2. DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1. DR PROSITE; PS00633; BROMODOMAIN_1; 2. DR PROSITE; PS50014; BROMODOMAIN_2; 2. DR PROSITE; PS51525; NET; 1. DR Genevisible; Q91Y44; MM. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; Bromodomain; KW Chromatin regulator; Coiled coil; Differentiation; Meiosis; KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Spermatogenesis; Transcription; KW Transcription regulation. FT CHAIN 1..956 FT /note="Bromodomain testis-specific protein" FT /id="PRO_0000239227" FT DOMAIN 43..115 FT /note="Bromo 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT DOMAIN 286..358 FT /note="Bromo 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT DOMAIN 496..578 FT /note="NET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00857" FT REGION 210..239 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 391..420 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 442..508 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 607..747 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 859..934 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 417..442 FT /evidence="ECO:0000255" FT COILED 844..940 FT /evidence="ECO:0000255" FT MOTIF 208..219 FT /note="Nuclear localization signal" FT /evidence="ECO:0000250|UniProtKB:Q58F21" FT COMPBIAS 210..235 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 391..408 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 461..483 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 491..508 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 622..642 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 644..693 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 710..732 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 872..888 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 912..934 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 108 FT /note="Histone H4K5ac binding" FT /evidence="ECO:0000269|PubMed:19794495" FT SITE 113 FT /note="Histone H4K5ac binding" FT /evidence="ECO:0000269|PubMed:19794495" FT MOD_RES 186 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT VAR_SEQ 323..326 FT /note="GKMD -> VNTA (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_019119" FT VAR_SEQ 327..956 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_019120" FT MUTAGEN 50..51 FT /note="PF->AA: Abolishes interaction with histone H4 FT acetylated N-terminus; when associated with A-55." FT /evidence="ECO:0000269|PubMed:12861021" FT MUTAGEN 55 FT /note="V->A: Abolishes interaction with histone H4 FT acetylated N-terminus; when associated with 50-AA-51." FT /evidence="ECO:0000269|PubMed:12861021" FT MUTAGEN 293..294 FT /note="PF->AA: Abolishes interaction with histone H4 FT acetylated N-terminus; when associated with A-298." FT /evidence="ECO:0000269|PubMed:12861021" FT MUTAGEN 298 FT /note="V->A: Abolishes interaction with histone H4 FT acetylated N-terminus; when associated with 293-AA-294." FT /evidence="ECO:0000269|PubMed:12861021" FT CONFLICT 208 FT /note="K -> R (in Ref. 2; BAD91553)" FT /evidence="ECO:0000305" FT CONFLICT 691 FT /note="S -> F (in Ref. 1; AAK50736)" FT /evidence="ECO:0000305" FT HELIX 29..36 FT /evidence="ECO:0007829|PDB:2WP2" FT HELIX 38..43 FT /evidence="ECO:0007829|PDB:2WP2" FT HELIX 46..51 FT /evidence="ECO:0007829|PDB:2WP2" FT TURN 57..61 FT /evidence="ECO:0007829|PDB:2WP2" FT HELIX 65..68 FT /evidence="ECO:0007829|PDB:2WP2" FT HELIX 75..83 FT /evidence="ECO:0007829|PDB:2WP2" FT HELIX 90..107 FT /evidence="ECO:0007829|PDB:2WP2" FT HELIX 113..129 FT /evidence="ECO:0007829|PDB:2WP2" FT HELIX 264..282 FT /evidence="ECO:0007829|PDB:2WP1" FT HELIX 285..287 FT /evidence="ECO:0007829|PDB:2WP1" FT HELIX 288..291 FT /evidence="ECO:0007829|PDB:2WP1" FT HELIX 292..294 FT /evidence="ECO:0007829|PDB:2WP1" FT HELIX 300..303 FT /evidence="ECO:0007829|PDB:2WP1" FT HELIX 308..311 FT /evidence="ECO:0007829|PDB:2WP1" FT HELIX 318..326 FT /evidence="ECO:0007829|PDB:2WP1" FT HELIX 333..350 FT /evidence="ECO:0007829|PDB:2WP1" FT HELIX 356..372 FT /evidence="ECO:0007829|PDB:2WP1" FT STRAND 375..377 FT /evidence="ECO:0007829|PDB:2WP1" SQ SEQUENCE 956 AA; 107255 MW; E727044706A67260 CRC64; MSLPSRQTAI VNPPPPEYIN TKKSGRLTNQ LQFLQRVVLK ALWKHGFSWP FQQPVDAVKL KLPDYYTIIK TPMDLNTIKK RLENKYYEKA SECIEDFNTM FSNCYLYNKT GDDIVVMAQA LEKLFMQKLS QMPQEEQVVG GKERIKKDIQ QKIAVSSAKE QIPSKAAENV FKRQEIPSGL PDISLSPLNM AQEAPPICDS QSLVQITKGV KRRADTTTPT TSIAKASSES PPTLRETKPV NMPVKENTVK NVLPDSQQQH KVLKTVKVTE QLKHCSEILK EMLAKKHLPY AWPFYNPVDA DALGLHNYYD VVKNPMDLGT IKGKMDNQEY KDAYEFAADV RLMFMNCYKY NPPDHEVVAM ARTLQDVFEL HFAKIPDEPI ESMHACHLTT NSAQALSRES SSEASSGDAS SEDSEDERVQ HLAKLQEQLN AVHQQLQVLS QVPLRKLKKK NEKSKRAPKR KKVNNRDENP RKKPKQMKQK EKAKINQPKK KKPLLKSEEE DNAKPMNYDE KRQLSLDINK LPGDKLGRIV HIIQSREPSL RNSNPDEIEI DFETLKASTL RELEKYVLAC LRKRSLKPQA KKVVRSKEEL HSEKKLELER RLLDVNNQLN CRKRQTKRPA KVEKPPPPPP PPPPPPPPPE LASGSRLTDS SSSSGSGSGS SSSSSGSSSS SSSSGSASSS SDSSSSDSSD SEPEIFPKFT GVKQNDLPPK ENIKQIQSSV QDITSAEAPL AQQSTAPCGA PGKHSQQMLG CQVTQHLQAT ENTASVQTQP LSGDCKRVLL GPPVVHTSAE SLTVLEPECH APAQKDIKIK NADSWKSLGK PVKASSVLKS SDELFNQFRK AAIEKEVKAR TQEQMRKHLE HNAKDPKVSQ ENQREPGSGL TLESLSSKVQ DKSLEEDQSE QQPPSEAQDV SKLWLLKDRN LAREKEQERR RREAMAGTID MTLQSDIMTM FENNFD //