BDP1_HUMAN
ID BDP1_HUMAN Reviewed; 2624 AA.
AC A6H8Y1; Q68DS6; Q68DY5; Q6MZL9; Q6PIM7; Q86W98; Q96LR8; Q9C0H4; Q9H197;
AC Q9H1A1; Q9HAW1; Q9HAW2; Q9HCY0; Q9ULH9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Transcription factor TFIIIB component B'' homolog;
DE AltName: Full=Transcription factor IIIB 150;
DE Short=TFIIIB150;
DE AltName: Full=Transcription factor-like nuclear regulator;
GN Name=BDP1; Synonyms=KIAA1241, KIAA1689, TFNR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), FUNCTION, AND VARIANTS
RP GLU-38 AND MET-1347.
RX PubMed=11040218; DOI=10.1101/gad.836400;
RA Schramm L., Pendergrast P.S., Sun Y., Hernandez N.;
RT "Different human TFIIIB activities direct RNA polymerase III transcription
RT from TATA-containing and TATA-less promoters.";
RL Genes Dev. 14:2650-2663(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [GENOMIC DNA]
RP OF 1-2187 (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2189-2624
RP (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANTS GLU-38;
RP MET-1347 AND LEU-2013.
RX PubMed=11161782; DOI=10.1006/geno.2000.6396;
RA Kelter A.R., Herchenbach J., Wirth B.;
RT "The transcription factor-like nuclear regulator (TFNR) contains a novel
RT 55-amino-acid motif repeated nine times and maps closely to SMN1.";
RL Genomics 70:315-326(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND VARIANTS CYS-757;
RP MET-1264 AND MET-1347.
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLU-38;
RP CYS-757; ILE-1244; MET-1264; MET-1347 AND GLU-1469.
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [5]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1947-2624 (ISOFORM 7), AND VARIANT LEU-2013.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLU-38;
RP CYS-757; ILE-1244; MET-1264; MET-1347 AND GLU-1469.
RC TISSUE=Lung;
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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-881 (ISOFORM 1).
RA Teichmann M., Wang Z., Ito M., Seifart K.H., Roeder R.G.;
RT "Molecular cloning and functional characterization of human TFIIIB 150.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-655 (ISOFORM 6).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [11]
RP IDENTIFICATION OF TFIIIB-ALPHA COMPLEX.
RX PubMed=11121026; DOI=10.1073/pnas.97.26.14200;
RA Teichmann M., Wang Z., Roeder R.G.;
RT "A stable complex of a novel transcription factor IIB- related factor,
RT human TFIIIB50, and associated proteins mediate selective transcription by
RT RNA polymerase III of genes with upstream promoter elements.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14200-14205(2000).
RN [12]
RP INTERACTION WITH BRF1.
RX PubMed=14592981; DOI=10.1093/emboj/cdg544;
RA Fairley J.A., Scott P.H., White R.J.;
RT "TFIIIB is phosphorylated, disrupted and selectively released from tRNA
RT promoters during mitosis in vivo.";
RL EMBO J. 22:5841-5850(2003).
RN [13]
RP IDENTIFICATION OF TFIIIC1 COMPLEX.
RX PubMed=15096501; DOI=10.1074/jbc.m312790200;
RA Weser S., Gruber C., Hafner H.M., Teichmann M., Roeder R.G., Seifart K.H.,
RA Meissner W.;
RT "Transcription factor (TF)-like nuclear regulator, the 250-kDa form of Homo
RT sapiens TFIIIB', is an essential component of human TFIIIC1 activity.";
RL J. Biol. Chem. 279:27022-27029(2004).
RN [14]
RP PHOSPHORYLATION, AND MUTAGENESIS OF SER-390; SER-426; SER-431; THR-437 AND
RP SER-446.
RX PubMed=15469824; DOI=10.1016/j.molcel.2004.09.008;
RA Hu P., Samudre K., Wu S., Sun Y., Hernandez N.;
RT "CK2 phosphorylation of Bdp1 executes cell cycle-specific RNA polymerase
RT III transcription repression.";
RL Mol. Cell 16:81-92(2004).
RN [15]
RP INTERACTION WITH ZBTB43.
RX PubMed=16542149; DOI=10.1515/bc.2006.037;
RA Schoenen F., Wirth B.;
RT "The zinc finger protein ZNF297B interacts with BDP1, a subunit of
RT TFIIIB.";
RL Biol. Chem. 387:277-284(2006).
RN [16]
RP SUBUNIT.
RX PubMed=16769183; DOI=10.1016/j.gene.2006.03.012;
RA Emran F., Florens L., Ma B., Swanson S.K., Washburn M.P., Hernandez N.;
RT "A role for Yin Yang-1 (YY1) in the assembly of snRNA transcription
RT complexes.";
RL Gene 377:96-108(2006).
RN [17]
RP INDUCTION.
RX PubMed=16956891; DOI=10.1074/jbc.m600468200;
RA Felton-Edkins Z.A., Kondrashov A., Karali D., Fairley J.A., Dawson C.W.,
RA Arrand J.R., Young L.S., White R.J.;
RT "Epstein-Barr virus induces cellular transcription factors to allow active
RT expression of EBER genes by RNA polymerase III.";
RL J. Biol. Chem. 281:33871-33880(2006).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-915, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [19]
RP INVOLVEMENT IN DFNB112.
RX PubMed=24312468; DOI=10.1371/journal.pone.0080323;
RA Girotto G., Abdulhadi K., Buniello A., Vozzi D., Licastro D.,
RA d'Eustacchio A., Vuckovic D., Alkowari M.K., Steel K.P., Badii R.,
RA Gasparini P.;
RT "Linkage study and exome sequencing identify a BDP1 mutation associated
RT with hereditary hearing loss.";
RL PLoS ONE 8:E80323-E80323(2013).
CC -!- FUNCTION: General activator of RNA polymerase III transcription.
CC Requires for transcription from all three types of polymerase III
CC promoters. Requires for transcription of genes with internal promoter
CC elements and with promoter elements upstream of the initiation site.
CC {ECO:0000269|PubMed:11040218}.
CC -!- SUBUNIT: Component of TFIIIB complex. The TFIIIB complex has two
CC activities, alpha and beta. The TFIIIB-alpha and TFIIIB-beta activities
CC are required for transcription of genes with TFIIIC-bound internal
CC promoters and PSE transcription factor-bound external promoters,
CC respectively. The TFIIIB-alpha activity complex is composed of TBP,
CC BDP1, and a complex containing both BRF2 and at least four stably
CC associated proteins; YY1 facilitates the formation of TFIIIB-alpha
CC activity complex. The TFIIIB-beta activity complex is composed of TBP,
CC BDP1, and BRF1. Interacts with BRF1; this interaction diminishes during
CC mitosis resulting in the release of BDP1 from chromosomal templates.
CC Component of TFIIIC complex. The TFIIIC complex has two activities, C1
CC and C2. The TFIIIC2 activity complex is only required for transcription
CC of the 'classical' pol III genes whereas the TFIIIC1 activity complex
CC is required for transcription of all pol III genes. The TFIIIC1
CC activity complex is composed at least of BDP1. Interacts with ZBTB43.
CC {ECO:0000269|PubMed:14592981, ECO:0000269|PubMed:16542149,
CC ECO:0000269|PubMed:16769183}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11161782}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=A6H8Y1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A6H8Y1-2; Sequence=VSP_033577, VSP_033578;
CC Name=3;
CC IsoId=A6H8Y1-3; Sequence=VSP_033570, VSP_033574;
CC Name=4;
CC IsoId=A6H8Y1-4; Sequence=VSP_033572, VSP_033573;
CC Name=5;
CC IsoId=A6H8Y1-5; Sequence=VSP_033568, VSP_033571, VSP_033574;
CC Name=6;
CC IsoId=A6H8Y1-6; Sequence=VSP_033569;
CC Name=7;
CC IsoId=A6H8Y1-7; Sequence=VSP_033575, VSP_033581, VSP_033582;
CC Name=8;
CC IsoId=A6H8Y1-8; Sequence=VSP_033567, VSP_033576, VSP_033579,
CC VSP_033580;
CC -!- TISSUE SPECIFICITY: Isoform 2 is highly expressed in cerebellum.
CC {ECO:0000269|PubMed:11161782}.
CC -!- INDUCTION: By Epstein-Barr virus (EBV) resulting in the stimulation of
CC the EBV EBER genes. {ECO:0000269|PubMed:16956891}.
CC -!- PTM: Phosphorylated by CSNK2A1 during mitosis, resulting in its release
CC from chromatin and suppression of polymerase III transcription.
CC {ECO:0000269|PubMed:15469824}.
CC -!- DISEASE: Deafness, autosomal recessive, 112 (DFNB112) [MIM:618257]: A
CC form of non-syndromic, sensorineural deafness characterized by
CC postlingual progressive hearing impairment. Sensorineural deafness
CC results from damage to the neural receptors of the inner ear, the nerve
CC pathways to the brain, or the area of the brain that receives sound
CC information. {ECO:0000269|PubMed:24312468}. Note=The disease may be
CC caused by variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG09268.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH32146.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA86555.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB21780.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAH18085.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF298151; AAG30220.1; -; mRNA.
DR EMBL; AF298152; AAG30221.1; -; mRNA.
DR EMBL; AJ238520; CAC04245.1; -; mRNA.
DR EMBL; AJ278892; CAC17771.1; -; Genomic_DNA.
DR EMBL; AJ279120; CAC21448.1; -; Genomic_DNA.
DR EMBL; AJ279121; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279122; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279123; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279124; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279125; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279126; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279127; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279128; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279129; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279130; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279131; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279132; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279133; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279134; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279135; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279136; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279137; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279138; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279139; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279140; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279141; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279142; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279143; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279144; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279145; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279146; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279147; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279148; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279149; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AJ279150; CAC21448.1; JOINED; Genomic_DNA.
DR EMBL; AB033067; BAA86555.1; ALT_INIT; mRNA.
DR EMBL; AB051476; BAB21780.3; ALT_INIT; mRNA.
DR EMBL; BX641011; CAE46010.1; -; mRNA.
DR EMBL; CR749229; CAH18085.1; ALT_INIT; mRNA.
DR EMBL; CR749289; CAH18144.1; -; mRNA.
DR EMBL; AC138832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032146; AAH32146.1; ALT_SEQ; mRNA.
DR EMBL; BC146792; AAI46793.1; -; mRNA.
DR EMBL; AF176695; AAG09268.1; ALT_FRAME; mRNA.
DR EMBL; AK057871; BAB71602.1; -; mRNA.
DR CCDS; CCDS43328.1; -. [A6H8Y1-1]
DR RefSeq; NP_060899.2; NM_018429.2. [A6H8Y1-1]
DR PDB; 5N9G; X-ray; 2.70 A; C/H=241-396.
DR PDBsum; 5N9G; -.
DR AlphaFoldDB; A6H8Y1; -.
DR SMR; A6H8Y1; -.
DR BioGRID; 120924; 53.
DR CORUM; A6H8Y1; -.
DR DIP; DIP-62076N; -.
DR IntAct; A6H8Y1; 21.
DR STRING; 9606.ENSP00000351575; -.
DR iPTMnet; A6H8Y1; -.
DR PhosphoSitePlus; A6H8Y1; -.
DR BioMuta; BDP1; -.
DR EPD; A6H8Y1; -.
DR jPOST; A6H8Y1; -.
DR MassIVE; A6H8Y1; -.
DR MaxQB; A6H8Y1; -.
DR PaxDb; A6H8Y1; -.
DR PeptideAtlas; A6H8Y1; -.
DR PRIDE; A6H8Y1; -.
DR ProteomicsDB; 777; -. [A6H8Y1-1]
DR ProteomicsDB; 778; -. [A6H8Y1-2]
DR ProteomicsDB; 779; -. [A6H8Y1-3]
DR ProteomicsDB; 780; -. [A6H8Y1-4]
DR ProteomicsDB; 781; -. [A6H8Y1-5]
DR ProteomicsDB; 782; -. [A6H8Y1-6]
DR ProteomicsDB; 783; -. [A6H8Y1-7]
DR ProteomicsDB; 784; -. [A6H8Y1-8]
DR Antibodypedia; 24108; 13 antibodies from 5 providers.
DR DNASU; 55814; -.
DR Ensembl; ENST00000358731.9; ENSP00000351575.4; ENSG00000145734.20. [A6H8Y1-1]
DR Ensembl; ENST00000617085.4; ENSP00000482469.1; ENSG00000273873.4. [A6H8Y1-1]
DR GeneID; 55814; -.
DR KEGG; hsa:55814; -.
DR MANE-Select; ENST00000358731.9; ENSP00000351575.4; NM_018429.3; NP_060899.2.
DR UCSC; uc003kbp.2; human. [A6H8Y1-1]
DR CTD; 55814; -.
DR DisGeNET; 55814; -.
DR GeneCards; BDP1; -.
DR HGNC; HGNC:13652; BDP1.
DR HPA; ENSG00000145734; Low tissue specificity.
DR MalaCards; BDP1; -.
DR MIM; 607012; gene.
DR MIM; 618257; phenotype.
DR neXtProt; NX_A6H8Y1; -.
DR OpenTargets; ENSG00000145734; -.
DR Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR PharmGKB; PA25336; -.
DR VEuPathDB; HostDB:ENSG00000145734; -.
DR eggNOG; KOG2009; Eukaryota.
DR GeneTree; ENSGT00390000012762; -.
DR HOGENOM; CLU_000736_0_0_1; -.
DR OMA; MKESVIQ; -.
DR OrthoDB; 156866at2759; -.
DR PhylomeDB; A6H8Y1; -.
DR TreeFam; TF328878; -.
DR PathwayCommons; A6H8Y1; -.
DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
DR Reactome; R-HSA-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-HSA-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR Reactome; R-HSA-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
DR SignaLink; A6H8Y1; -.
DR SIGNOR; A6H8Y1; -.
DR BioGRID-ORCS; 55814; 479 hits in 1082 CRISPR screens.
DR ChiTaRS; BDP1; human.
DR GeneWiki; BDP1; -.
DR GenomeRNAi; 55814; -.
DR Pharos; A6H8Y1; Tbio.
DR PRO; PR:A6H8Y1; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; A6H8Y1; protein.
DR Bgee; ENSG00000145734; Expressed in sural nerve and 102 other tissues.
DR ExpressionAtlas; A6H8Y1; baseline and differential.
DR Genevisible; A6H8Y1; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000126; C:transcription factor TFIIIB complex; IBA:GO_Central.
DR GO; GO:0001156; F:TFIIIC-class transcription factor complex binding; IBA:GO_Central.
DR GO; GO:0070898; P:RNA polymerase III preinitiation complex assembly; IBA:GO_Central.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR039467; TFIIIB_B''_Myb.
DR Pfam; PF15963; Myb_DNA-bind_7; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Coiled coil; Deafness;
KW Non-syndromic deafness; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation.
FT CHAIN 1..2624
FT /note="Transcription factor TFIIIB component B'' homolog"
FT /id="PRO_0000333863"
FT DOMAIN 295..345
FT /note="Myb-like"
FT REPEAT 823..877
FT /note="1; approximate"
FT REPEAT 878..932
FT /note="2"
FT REPEAT 933..987
FT /note="3"
FT REPEAT 988..1040
FT /note="4"
FT REPEAT 1041..1094
FT /note="5"
FT REPEAT 1095..1148
FT /note="6"
FT REPEAT 1149..1203
FT /note="7"
FT REPEAT 1204..1257
FT /note="8; approximate"
FT REPEAT 1258..1327
FT /note="9; approximate"
FT REGION 1..299
FT /note="Interaction with ZBTB43"
FT /evidence="ECO:0000269|PubMed:16542149"
FT REGION 1..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..470
FT /note="Required for phosphorylation by CSNK2A1"
FT REGION 379..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..1327
FT /note="9 X 55 AA repeats of G-R-R-X-I-S-P-X-E-N-G-X-E-E-V-
FT K-P-X-X-E-M-E-T-D-L-K-X-T-G-R-E-X-X-X-R-E-K-T-X-E-X-X-D-A-
FT X-E-E-I-D-X-D-L-E-E-T"
FT REGION 930..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1306..1348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1365..1440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1519..1543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1684..1722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1819..1863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2130..2164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2181..2200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2207..2241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2444..2501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2519..2566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 144..177
FT /evidence="ECO:0000255"
FT COILED 1078..1103
FT /evidence="ECO:0000255"
FT COILED 1223..1284
FT /evidence="ECO:0000255"
FT COMPBIAS 67..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..953
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..1031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1083
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1330..1348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1365..1392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1393..1421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1690..1718
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1830..1855
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2133..2147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2148..2164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2468..2482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2483..2498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2543..2557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 915
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..1863
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_033567"
FT VAR_SEQ 1..610
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:10574462"
FT /id="VSP_033568"
FT VAR_SEQ 24..43
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033569"
FT VAR_SEQ 1354..1388
FT /note="NISSEVLSMMHTPVEEKRNSEKEVSSHFSHFKISS -> VCIFLSFKSFLNA
FT FSEEINNSMIILSLSPTTLKNL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11040218"
FT /id="VSP_033570"
FT VAR_SEQ 1354..1388
FT /note="NISSEVLSMMHTPVEEKRNSEKEVSSHFSHFKISS -> VCIFLSFKSFLNA
FT FSEEINNSMIILSLSPTTFKNL (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:10574462"
FT /id="VSP_033571"
FT VAR_SEQ 1354..1372
FT /note="NISSEVLSMMHTPVEEKRN -> VCIFLSFKSFLNAFFRGNK (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:11040218"
FT /id="VSP_033572"
FT VAR_SEQ 1373..2624
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11040218"
FT /id="VSP_033573"
FT VAR_SEQ 1389..2624
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10574462,
FT ECO:0000303|PubMed:11040218"
FT /id="VSP_033574"
FT VAR_SEQ 1977..2008
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_033575"
FT VAR_SEQ 2008
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_033576"
FT VAR_SEQ 2249..2254
FT /note="YTPTSI -> VKECTV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11161782"
FT /id="VSP_033577"
FT VAR_SEQ 2255..2624
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11161782"
FT /id="VSP_033578"
FT VAR_SEQ 2271..2327
FT /note="NLVANVPQDGEDEQAFILTLVEIPANAVEEFTDATAQFMPNPLLPAPILVKS
FT VNTEE -> FVYQQLQLVKMPWVYLFLEEIILKSRLIIWILYLGRDFNAGLIKMTTFLL
FT PKNVHSL (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_033579"
FT VAR_SEQ 2328..2624
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_033580"
FT VAR_SEQ 2582..2584
FT /note="VSC -> RPF (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_033581"
FT VAR_SEQ 2585..2624
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_033582"
FT VARIANT 26
FT /note="N -> S (in dbSNP:rs3748042)"
FT /id="VAR_056743"
FT VARIANT 38
FT /note="D -> E (in dbSNP:rs3748043)"
FT /evidence="ECO:0000269|PubMed:11040218,
FT ECO:0000269|PubMed:11161782, ECO:0000269|PubMed:11214970,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_043312"
FT VARIANT 125
FT /note="A -> V (in dbSNP:rs9687593)"
FT /id="VAR_056744"
FT VARIANT 722
FT /note="K -> E (in dbSNP:rs36009281)"
FT /id="VAR_056745"
FT VARIANT 757
FT /note="R -> C (in dbSNP:rs3761966)"
FT /evidence="ECO:0000269|PubMed:10574462,
FT ECO:0000269|PubMed:11214970, ECO:0000269|PubMed:15489334"
FT /id="VAR_043313"
FT VARIANT 778
FT /note="V -> M (in dbSNP:rs3761967)"
FT /id="VAR_043314"
FT VARIANT 1180
FT /note="G -> S (in dbSNP:rs715748)"
FT /id="VAR_056746"
FT VARIANT 1244
FT /note="F -> I (in dbSNP:rs1961760)"
FT /evidence="ECO:0000269|PubMed:11214970,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_056747"
FT VARIANT 1264
FT /note="I -> M (in dbSNP:rs715747)"
FT /evidence="ECO:0000269|PubMed:10574462,
FT ECO:0000269|PubMed:11214970, ECO:0000269|PubMed:15489334"
FT /id="VAR_043315"
FT VARIANT 1347
FT /note="V -> M (in dbSNP:rs6886336)"
FT /evidence="ECO:0000269|PubMed:10574462,
FT ECO:0000269|PubMed:11040218, ECO:0000269|PubMed:11161782,
FT ECO:0000269|PubMed:11214970, ECO:0000269|PubMed:15489334"
FT /id="VAR_043316"
FT VARIANT 1469
FT /note="K -> E (in dbSNP:rs1698063)"
FT /evidence="ECO:0000269|PubMed:11214970,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_043317"
FT VARIANT 1676
FT /note="Q -> E (in dbSNP:rs12187098)"
FT /id="VAR_056748"
FT VARIANT 2013
FT /note="I -> L (in dbSNP:rs6453014)"
FT /evidence="ECO:0000269|PubMed:11161782,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_043318"
FT VARIANT 2555
FT /note="N -> S (in dbSNP:rs17276250)"
FT /id="VAR_056749"
FT MUTAGEN 390
FT /note="S->A: Not phosphorylated by CSNK2A1; when associated
FT with A-426; A-431; A-437 and A-446. CK2 treatment
FT constitutively activates for U6 transcription; when
FT associated with A-426; A-431; A-437 and A-446."
FT /evidence="ECO:0000269|PubMed:15469824"
FT MUTAGEN 426
FT /note="S->A: Not phosphorylated by CSNK2A1; when associated
FT with A-390; A-431; A-437 and A-446. CK2 treatment
FT constitutively activates for U6 transcription; when
FT associated with A-390; A-431; A-437 and A-446."
FT /evidence="ECO:0000269|PubMed:15469824"
FT MUTAGEN 431
FT /note="S->A: Not phosphorylated by CSNK2A1; when associated
FT with A-390; A-426; A-437 and A-446. CK2 treatment
FT constitutively activates for U6 transcription; when
FT associated with A-390; A-426; A-437 and A-446."
FT /evidence="ECO:0000269|PubMed:15469824"
FT MUTAGEN 437
FT /note="T->A: Not phosphorylated by CSNK2A1; when associated
FT with A-390; A-426; A-431 and A-446. CK2 treatment
FT constitutively activates for U6 transcription; when
FT associated with A-390; A-426; A-431 and A-446."
FT /evidence="ECO:0000269|PubMed:15469824"
FT MUTAGEN 446
FT /note="S->A: Not phosphorylated by CSNK2A1; when associated
FT with A-390; A-426; A-431 and A-437. CK2 treatment
FT constitutively activates for U6 transcription; when
FT associated with A-390; A-426; A-431 and A-437."
FT /evidence="ECO:0000269|PubMed:15469824"
FT CONFLICT 8
FT /note="S -> N (in Ref. 9; AAG09268)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="E -> G (in Ref. 1; AAG30221/AAG30220)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="R -> K (in Ref. 10; BAB71602)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="V -> D (in Ref. 2; CAC21448)"
FT /evidence="ECO:0000305"
FT CONFLICT 881
FT /note="A -> T (in Ref. 9; AAG09268)"
FT /evidence="ECO:0000305"
FT CONFLICT 973
FT /note="V -> G (in Ref. 2; CAC21448/CAC04245)"
FT /evidence="ECO:0000305"
FT CONFLICT 1009
FT /note="E -> G (in Ref. 1; AAG30221/AAG30220)"
FT /evidence="ECO:0000305"
FT CONFLICT 2580
FT /note="T -> A (in Ref. 6; CAE46010)"
FT /evidence="ECO:0000305"
FT HELIX 305..317
FT /evidence="ECO:0007829|PDB:5N9G"
FT HELIX 322..328
FT /evidence="ECO:0007829|PDB:5N9G"
FT HELIX 334..347
FT /evidence="ECO:0007829|PDB:5N9G"
FT HELIX 349..357
FT /evidence="ECO:0007829|PDB:5N9G"
FT HELIX 364..381
FT /evidence="ECO:0007829|PDB:5N9G"
SQ SEQUENCE 2624 AA; 293885 MW; CB7B80EBBF06B557 CRC64;
MFRRARLSVK PNVRPGVGAR GSTASNPQRG RESPRPPDPA TDSASKPAEP TDVPTVDFGG
AEPQEKAPRS STEKTGGDND VEESSRSSST VSQRRKRISS TSSLVKSSVS VPSESHPLST
INQEAPQPTA TSTKEKQPCS DRYRIYKAQK LREMLKEELR KEKKQWKNKY AINESQRPPD
RSKMTMRDFI YYLPDNNPMT SSLEQEKKTE KPSTPVQTRE QEGKSTPNAE DNEMEEETDD
GPLLVPRVKV AEDGSIILDE ESLTVEVLRT KGPCVVEEND PIFERGSTTT YSSFRKNYYS
KPWSNKETDM FFLAISMVGT DFSMIGQLFP HRARIEIKNK FKREEKTNGW RIDKAFQEKR
PFDFDFFAHL LQKVLAEEEK RKQKSVKNHS LKEKKSTKPR KNVKVKKVAC EGVNNDPDES
MSSRISDTER SQKDAQTVEE ESLTLSREDA EQVALEVDLN QKKRRRKKQD GANELGVNNL
LENATVQAGP SKGEKHKNKC QAIRPELKEG ECSKEQMLSC TQNIDGIVGF ASTEKVEKRT
DPILSLSNQQ DATSVATESS ESSTSDLPSF EVGIRALCEV NNAEGSCIEE RNVDLKNNSL
EIDQTENVKP MLRGRFQRPK PNLSRAGKKS VLSQGKTESE SKNSHSKTSV EKNHVEKDKM
NTLDILRMET TERENPEAET VSVLGEKNCL QEGSQLKALR PVQVRGRLQK PKPNAGKAAE
RKEILISQEE IGANVEKNEN ESCADRDTPQ HMEDQSRKDF EEEDVILQPE KNDSFQNVQP
DEPKVLNECL SVQENNKANK LNQVPILRTR FQKPKPNIGR GTGRREISSK EEVLEKILVS
GEMAAALRET VRLDTSPKEM VPAEINTKEM QSDLKETGRR AISPREKILD VIDDTIEMET
GLKAMGREIC LREKTPEVID ATEEIDKDLE EAGRREISPQ KNGPEEVKPL GEVETDLKAT
GNESSPREKT PEVTDATEEI DKNLEETGRR KISPRENGPE EVKPVDEMET DLNATGRESS
PREKTPEVID ATEEIDLEET EREVSPQENG LEEVKPLGEM ETDLKATGRD SFPRGKTPEV
IDAIEEIEID LEETEREISP QENGLEEVKP LGEMQTDLKA TGREISPREK TPEVIDATEE
IDKDLEETGR REISPEENGP EEVKPVDEME TDLKTTGREG SSREKTREVI DAAEVIETDL
EETEREISPQ ENGPEEVKPV GKMETDLKEI REEISQREKV LAEFSAIREK EIDLKETGKR
DIPIMEKVSG KMAVVEEMEA DLKETGKENF RERGSEEICV TEEKVAELKQ TGKTDISPRE
NELEETSTSR QTDTHLMQSG SNDFSAVPSL DIQNISSEVL SMMHTPVEEK RNSEKEVSSH
FSHFKISSQT HESDKTEVQG IQSPDVPEQF SDINLSKSLP QEQKPLEIKP APFVRSRFKR
PKPNLARAAL KRETTESEKY IYEKKSETKK METIVMQENN EQTDTLPSQH DEASLMISRE
KDTLGHRNEE AVILPCTQTE RNLSPSNSCE PKEESQSAPV QKNDSVVSVG TNNVNTFQQE
MKESVIQTAR QVRGRLQRPR PNIRKTGQRQ IVDKGEAKGI IKEGRTILPK DETEKKVLTV
SNSQIETEIE VPSSAVPEHR MYENQSQVVL VENLHVNKTN ETIRHENKPY VPSSAQMTRR
KFQKAKPNLG RAHSKKEEPV LEKVTTDQSK EGKPEDHLLQ KGASNTQLLL KEKAELLTSL
EVSARKDCVG SKESALAKID AELEEVGPSR RVGEETVGDN SPSSVVEEQY LNKLTSCPQP
LNETSYSKIA LDGKTTISST SEYERNRGER RSHKKFKPNV TRGRGSKRVR GKTSKKEPRA
SKAMLVTLRA SQEEDDDADD FESDYEEESY HLAPEEVNKA PVFVPVGLRS PEPVSAQIEE
TMEELEITVN VPDVGCIAVV EHELPNTDVT TEEMKQEENL SVPFEMTTSE HIQDEPGTND
GSTEAAITLL TMGDLVLQSE ISSEQGDVGV CIIPHVHSKD KSHIPSSLDN VNHKIVHECQ
ELSSPVITTS PASFEENKIV LEEQSSREEI SLMEKVKENA TPTRNTISKV TSNLRIRSRL
AKPKPNLEKT LGTNRLDDYQ EVSSLCVTKG AEMETQRETE KNASKATELE NKNLGPVTTA
ENKDQSKLAC VHGIKGTSIS SEVNLTERNE NQEESSQEVH MLSVAPVASS ETGPCTLGLD
RGLGENSVEE PQIKDSKGDS VLTLPVPEYT PTSIPEVQQE NIINPQDLTV NLVANVPQDG
EDEQAFILTL VEIPANAVEE FTDATAQFMP NPLLPAPILV KSVNTEERGD MSICLPATSV
GQDAMGLSIS GRDNSKKPPD NLDLVSRKRF QCRLDKNDHI PPAKKRSLTL RDDCQEYTTE
VHSKELTNVF EETGESHKGQ DIFLTSGSTL TTPEPQRQQV EAAFQSRGSR SPDACMDKNV
PQLPQDEMIV SDKEERTDAA PKSQQMDSRT SSSKASLSRP GRRPLGFLSL ICSKNSLESD
EPMQVHSKKR LKPLIPGLRK KLKRSNPFNE SQEKNRESSD LLPSPSVITT QSENISSSAT
QVSCDQPLLK EGYKSAQKRA PQGEATTVSE YFFNDIFIEV DETE
