BDP1_MOUSE
ID BDP1_MOUSE Reviewed; 2467 AA.
AC Q571C7; Q8BTI4; Q8K0U7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 113.
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, Tfnr;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 508-2467 (ISOFORM 1).
RC TISSUE=Pancreatic islet;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1852-2467 (ISOFORM 1).
RC TISSUE=Eye;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2047-2467 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP TISSUE SPECIFICITY.
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 (By
CC similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q571C7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q571C7-2; Sequence=VSP_033583;
CC -!- TISSUE SPECIFICITY: Expressed in the cochlea, particularly in the
CC spiral ligament, the capillaries of the stria vascularis and the
CC basilar membrane. {ECO:0000269|PubMed:24312468}.
CC -!- PTM: Phosphorylated by CSNK2A1 during mitosis, resulting in its release
CC from chromatin and suppression of polymerase III transcription.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH30359.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
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DR EMBL; CT025569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT030167; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK220262; BAD90187.1; -; mRNA.
DR EMBL; BC030359; AAH30359.1; ALT_SEQ; mRNA.
DR EMBL; AK090184; BAC41127.1; -; mRNA.
DR CCDS; CCDS49343.1; -. [Q571C7-1]
DR RefSeq; NP_001074530.1; NM_001081061.1. [Q571C7-1]
DR RefSeq; XP_006517788.1; XM_006517725.3. [Q571C7-2]
DR AlphaFoldDB; Q571C7; -.
DR SMR; Q571C7; -.
DR BioGRID; 243826; 4.
DR STRING; 10090.ENSMUSP00000038321; -.
DR iPTMnet; Q571C7; -.
DR PhosphoSitePlus; Q571C7; -.
DR EPD; Q571C7; -.
DR jPOST; Q571C7; -.
DR MaxQB; Q571C7; -.
DR PaxDb; Q571C7; -.
DR PeptideAtlas; Q571C7; -.
DR PRIDE; Q571C7; -.
DR ProteomicsDB; 273552; -. [Q571C7-1]
DR ProteomicsDB; 273553; -. [Q571C7-2]
DR Antibodypedia; 24108; 13 antibodies from 5 providers.
DR Ensembl; ENSMUST00000038104; ENSMUSP00000038321; ENSMUSG00000049658. [Q571C7-1]
DR Ensembl; ENSMUST00000109379; ENSMUSP00000105005; ENSMUSG00000049658. [Q571C7-2]
DR GeneID; 544971; -.
DR KEGG; mmu:544971; -.
DR UCSC; uc007rqc.1; mouse. [Q571C7-1]
DR CTD; 55814; -.
DR MGI; MGI:1347077; Bdp1.
DR VEuPathDB; HostDB:ENSMUSG00000049658; -.
DR eggNOG; KOG2009; Eukaryota.
DR GeneTree; ENSGT00390000012762; -.
DR HOGENOM; CLU_000736_0_0_1; -.
DR InParanoid; Q571C7; -.
DR OMA; MKESVIQ; -.
DR OrthoDB; 156866at2759; -.
DR PhylomeDB; Q571C7; -.
DR TreeFam; TF328878; -.
DR Reactome; R-MMU-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-MMU-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR Reactome; R-MMU-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
DR BioGRID-ORCS; 544971; 13 hits in 75 CRISPR screens.
DR ChiTaRS; Bdp1; mouse.
DR PRO; PR:Q571C7; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q571C7; protein.
DR Bgee; ENSMUSG00000049658; Expressed in humerus cartilage element and 231 other tissues.
DR ExpressionAtlas; Q571C7; baseline and differential.
DR Genevisible; Q571C7; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
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:0006355; P:regulation of transcription, DNA-templated; ISA:MGI.
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 2: Evidence at transcript level;
KW Activator; Alternative splicing; Coiled coil; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..2467
FT /note="Transcription factor TFIIIB component B'' homolog"
FT /id="PRO_0000333864"
FT DOMAIN 297..347
FT /note="Myb-like"
FT REGION 1..301
FT /note="Interaction with ZBTB43"
FT /evidence="ECO:0000250"
FT REGION 1..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..472
FT /note="Required for phosphorylation by CSNK2A1"
FT /evidence="ECO:0000250"
FT REGION 380..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1318..1388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1409..1448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1527..1561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1592..1706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1902..1926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1977..2014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2058..2083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2179..2206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2260..2290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2304..2449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 144..177
FT /evidence="ECO:0000255"
FT COILED 458..487
FT /evidence="ECO:0000255"
FT COMPBIAS 29..44
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..774
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1043
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1099
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1338..1354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1359..1384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1426..1448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1532..1561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1624..1666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1678..1699
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1902..1922
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1977..2012
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2179..2201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2323..2337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2383..2402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2409..2428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 2426..2467
FT /note="SSDQPLLKEECKNGPKGAPEEEVTPVSEFVFSDIFIEVDETL -> CEHCCV
FT LLCMRYIYHLNEGRKSKFIFSWMSEIILVQLLFPTKMHLI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033583"
FT CONFLICT 788
FT /note="C -> F (in Ref. 2; BAD90187)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2467 AA; 270790 MW; C4B6BBCB266D47AA CRC64;
MFRRARLSVK PNVRPGVGTR GSAAPNPQRG PEAPRPPEPA TESAPKPAEP TDVPAVDSGG
AEPQEQAPGS SDEKTGDKNN AAESSTLSSA SSQRRKRVSS TSSLVQPSGS APSQSRPLST
VDHDAPQPNP TPAKEKQPCS DRYRIYKARK LREMLKEELR KEKKQWKNKF STNESQRPPD
RSKMTMRDFI YYLPDNNPMT SSVEQEKKPE KSLAPTPTRD RQENQSTQDA NDNEDVEEEV
DDGPLLVPRV KVAEDGSIIL DEESLTVEVL RTKGPCVVEE NDPIFERGST TTYSSFRKNY
YSKPWSNKET DMFFLAISMV GTDFSMIGQL FPHRARIEIK NKFKREEKTN GWRIDKAFQE
KRPFDFDFFA HLLQKVLAEE EKRKQKSTKC QSLKEKASKP RKNLKAKTVT SEEVNDDPDE
SVNSNISDPE RSQNDAETVN EEESPSSSGQ HLEQAMLEQD QNQEKKRRRN QGEANKQEAT
NLLERVLVHS SPPAAEIHKN TCPSEENESE CNKEQIPSLT QNIDDIAGLA PSEETEMRMD
PIPSTCNQQD IMPLARESSE SCAVALPVWE PGNTASADMA HAESSCSEGR GADLKTAAPE
TEQTENVKPK SRSRLQRPKP NLARAVGKKS AVSQDRQDER NKNSPSETAA EKNHMEKETM
NESETSVAKN TDGESPGAKT VSDLSEKSCV QQDSQAKVLR PTRLMRSRMQ RPKPNVVKAA
ERKEILTSQE KFGAHVEKSE DESCVVIPPQ TENESHKNLQ CEDTVSEPGR KDPFENIQPD
QPQVLSDCPS IHEGNKENKR KQVPVLRTRF QKPKPNTGRR RRRISSKEGI PEETPISGEI
PATWEEIPSL DTSLREEVLS VPLAPLTATA STKDSESDVK DSGRNDTASN AEMSEMTDVT
MEMETGLETI GRDTCPGEMG AEMIDIPMET EAGLKASLNE TSCMEKVPEL IDTTGEICTN
LGETGRKEVF LQENGPKEVG PVSEPETGLQ ETGKDLAMKE STPDTTDSTE EREAYSEETE
RQEKISALIK DAEEAKARGE METPLEEIGG GTSQRGKAAG APVEQSASEE EPQGSACREE
VAVESSTAEG KELNLRETGE DDVSSMVVVL GEKTDIEETN GDPKETERES SVSWERGSGE
IQVGEEMVED LGKPEKIDVA PREREPEEHS SGQPEADVIL SSSDGSTGSP QDKVNISSKI
SVMPTLVEEK ETTDKDISSH LGHVESCSQN LGRHETDQGM PLPDALERFS DTNLSKPLPQ
EQQPLQVKPA PFLRSRFKKP KPNLSRAALK RATIEAEHCV PGKKSEACKV EAAMLQQDSD
QAALSPQHNV PSLMASREND KSGHEEEEEA AILPCTQTEK DASPPNSSEP KEGSQLTPNQ
ENGLLVPIGT PMMNTVTQET RQNVVQTTLP VRGRLQRPRP NVQKARQRQI VEKGEARDIA
KNEGPELQKD ETRTCLTVAN SSHIESGVAV DMSSRVSECQ VSESQGHADP VENLSVNKAS
VVHEQMRHEN KPYVPSPALL IRRRFQKAKP NLGGARRKDE QPGVEKGRTD ESTALTAEDH
LLQKEDCDTQ LSLQAREKAD MPLEVSVRKE CIHSEESGSD RNDAQPNAGP SEGSRDETAK
EQPTSLGLEE QSLSKQIRSS CPQLWKESSY PKTVSSRRTP LSSASECEIE HSWKRTQRKT
KPNLTKGRGS KRIRGKTAKK EPRASKSVLV TLRASQKEDE DDAEDFDSDY EEETYHLAPE
ELSKAPVFVP VGLRSPEPVS AQIEETMEEL EITMDVADMT VVEHQLSHMD TTAQAVQAEK
AVYPPSFEMD VGEQTQEEPG PSDGSTEAAI TLLTMGDIVL QSEIIPGQGD VGVCVFPDVH
SEDKSHAPFS PDNVNQKVVH DYPEVCSPVI STSHASFEEN RIVSKEQSNR DAAVEEEAVE
ETLPTRNTTS TMSTHLRMES MVVTPELNSE KTLEISESHG HQEVASFCIT KETEVEIQRE
TEGDDSKAVE LEDKSHAPVT AAETKEEEQS QCVGDVEGAS VSQEAILPAR IEDHEETLQE
VQESGTAVAS SEIGQQTLDS GQSFGESAAK EALKETPKGS DVPVLHGPES VPSHIPEAQQ
ENTGPQAVTV NPFADGQQDG EDEQAFILTL VEIPTHATEG FTDAAMQLMP SSLLPAPILV
RSGNAAERGD LSGSLQTSLV VQDAPSLSPS RSGSSEKPPA NLDLTSRKRF CCSPDESIHV
PPAKKSSLVP GIDYQECTSE VCSEELNVFE KTAESCMGQG IFPTSESTHA TSKPQKEHSE
PTDTGSSGSL DEIKDACVEN MAQLPQSEIV SDKEEKTEPA SNSEQRDIVT SSSKPPLTRP
GRRPLGFLSL LCPKNSLESD EVTQTHSKKR LKPQIPVSRR NLRKPNLHNT SQKKNQDSSA
PPPSPSVTAP LSGTAGSPES SAAQVSSDQP LLKEECKNGP KGAPEEEVTP VSEFVFSDIF
IEVDETL
