ID THOC1_HUMAN Reviewed; 657 AA. AC Q96FV9; B2RBP6; Q15219; Q64I72; Q64I73; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 02-MAR-2010, entry version 78. DE RecName: Full=THO complex subunit 1; DE Short=Tho1; DE AltName: Full=Nuclear matrix protein p84; DE Short=p84N5; DE AltName: Full=hTREX84; GN Name=THOC1; Synonyms=HPR1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND RP INTERACTION WITH RB1. RC TISSUE=Lymphocyte; RX MEDLINE=95050936; PubMed=7525595; DOI=10.1083/jcb.127.3.609; RA Durfee T., Mancini M.A., Jones D., Elledge S.J., Lee W.H.; RT "The amino-terminal region of the retinoblastoma gene product binds a RT novel nuclear matrix protein that co-localizes to centers for RNA RT processing."; RL J. Cell Biol. 127:609-622(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=15358532; DOI=10.1016/j.febslet.2004.07.074; RA Gasparri F., Sola F., Locatelli G., Muzio M.; RT "The death domain protein p84N5, but not the short isoform p84N5s, is RT cell cycle-regulated and shuttles between the nucleus and the RT cytoplasm."; RL FEBS Lett. 574:13-19(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Uterus; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16177791; DOI=10.1038/nature03983; RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., RA Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., RA FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., RA Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R., RA Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., RA Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., RA Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., RA O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.; RT "DNA sequence and analysis of human chromosome 18."; RL Nature 437:551-555(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Bone marrow; 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 [7] RP FUNCTION, PTM, DOMAIN, AND MUTAGENESIS OF LEU-617 AND TRP-620. RX PubMed=10512864; RA Doostzadeh-Cizeron J., Evans R., Yin S., Goodrich D.W.; RT "Apoptosis induced by the nuclear death domain protein p84N5 is RT inhibited by association with Rb protein."; RL Mol. Biol. Cell 10:3251-3261(1999). RN [8] RP FUNCTION. RX PubMed=10840029; DOI=10.1074/jbc.M000793200; RA Doostzadeh-Cizeron J., Yin S., Goodrich D.W.; RT "Apoptosis induced by the nuclear death domain protein p84N5 is RT associated with caspase-6 and NF-kappa B activation."; RL J. Biol. Chem. 275:25336-25341(2000). RN [9] RP FUNCTION. RX PubMed=11050087; DOI=10.1074/jbc.M006944200; RA Doostzadeh-Cizeron J., Terry N.H., Goodrich D.W.; RT "The nuclear death domain protein p84N5 activates a G2/M cell cycle RT checkpoint prior to the onset of apoptosis."; RL J. Biol. Chem. 276:1127-1132(2001). RN [10] RP FUNCTION, AND INTERACTION WITH THE TREX COMPLEX. RX MEDLINE=22010388; PubMed=11979277; DOI=10.1038/nature746; RA Straesser K., Masuda S., Mason P., Pfannstiel J., Oppizzi M., RA Rodriguez-Navarro S., Rondon A.G., Aguilera A., Struhl K., Reed R., RA Hurt E.; RT "TREX is a conserved complex coupling transcription with messenger RNA RT export."; RL Nature 417:304-308(2002). RN [11] RP SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION SIGNAL. RX PubMed=12096345; DOI=10.1038/sj.onc.1205583; RA Evans R.L., Poe B.S., Goodrich D.W.; RT "Nuclear localization is required for induction of apoptotic cell RT death by the Rb-associated p84N5 death domain protein."; RL Oncogene 21:4691-4695(2002). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560, AND MASS RP SPECTROMETRY. RC TISSUE=Epithelium; RX PubMed=15302935; DOI=10.1073/pnas.0404720101; RA Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., RA Li J., Cohn M.A., Cantley L.C., Gygi S.P.; RT "Large-scale characterization of HeLa cell nuclear phosphoproteins."; RL Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). RN [13] RP IDENTIFICATION IN THE TREX COMPLEX, FUNCTION OF THE TREX COMPLEX, MASS RP SPECTROMETRY, AND TISSUE SPECIFICITY. RX PubMed=15833825; DOI=10.1158/0008-5472.CAN-04-3624; RA Guo S., Hakimi M.A., Baillat D., Chen X., Farber M.J., RA Klein-Szanto A.J., Cooch N.S., Godwin A.K., Shiekhattar R.; RT "Linking transcriptional elongation and messenger RNA export to RT metastatic breast cancers."; RL Cancer Res. 65:3011-3016(2005). RN [14] RP IDENTIFICATION IN THE THO AND TREX COMPLEX, FUNCTION OF THE TREX RP COMPLEX, AND MASS SPECTROMETRY. RX PubMed=15998806; DOI=10.1101/gad.1302205; RA Masuda S., Das R., Cheng H., Hurt E., Dorman N., Reed R.; RT "Recruitment of the human TREX complex to mRNA during splicing."; RL Genes Dev. 19:1512-1517(2005). RN [15] RP FUNCTION, AND INTERACTION WITH THOC2; UAP56 AND RNA POLYMERASE II. RX PubMed=15870275; DOI=10.1128/MCB.25.10.4023-4033.2005; RA Li Y., Wang X., Zhang X., Goodrich D.W.; RT "Human hHpr1/p84/Thoc1 regulates transcriptional elongation and RT physically links RNA polymerase II and RNA processing factors."; RL Mol. Cell. Biol. 25:4023-4033(2005). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560, AND MASS RP SPECTROMETRY. RC TISSUE=Epithelium; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [17] RP FUNCTION OF THE TREX COMPLEX. RX PubMed=17190602; DOI=10.1016/j.cell.2006.10.044; RA Cheng H., Dufu K., Lee C.-S., Hsu J.L., Dias A., Reed R.; RT "Human mRNA export machinery recruited to the 5' end of mRNA."; RL Cell 127:1389-1400(2006). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS RP SPECTROMETRY. RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., RA Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for RT efficient phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [19] RP FUNCTION OF THE TREX COMPLEX. RX PubMed=18974867; DOI=10.1371/journal.ppat.1000194; RA Boyne J.R., Colgan K.J., Whitehouse A.; RT "Recruitment of the complete hTREX complex is required for Kaposi's RT sarcoma-associated herpesvirus intronless mRNA nuclear export and RT virus replication."; RL PLoS Pathog. 4:E1000194-E1000194(2008). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS RP SPECTROMETRY. 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 [21] RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [22] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-133 AND LYS-300, AND MASS RP SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [23] RP STRUCTURE BY NMR OF 561-657. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the death domain of nuclear matrix protein RT p84."; RL Submitted (JUL-2005) to the PDB data bank. CC -!- FUNCTION: Component of the THO subcomplex of the TREX complex. The CC TREX complex specifically associates with spliced mRNA and not CC with unspliced pre-mRNA. It is recruited to spliced mRNAs by a CC transcription-independent mechanism. Binds to mRNA upstream of the CC exon-junction complex (EJC) and is recruited in a splicing- and CC cap-dependent manner to a region near the 5' end of the mRNA where CC it functions in mRNA export. The recruitment occurs via an CC interaction between THOC4 and the cap-binding protein NCBP1. UAP56 CC functions as a bridge between THOC4 and the THO complex. The TREX CC complex is essential for the export of Kaposi's sarcoma-associated CC herpesvirus (KSHV) intronless mRNAs and infectious virus CC production. The recruitment of the TREX complex to the intronless CC viral mRNA occurs via an interaction between KSHV ORF57 protein CC and THOC4. CC -!- FUNCTION: Regulates transcriptional elongation of a subset of CC genes. Participates in an apoptotic pathway which is characterized CC by activation of caspase-6, increases in the expression of BAK1 CC and BCL2L1 and activation of NF-kappa-B. This pathway does not CC require TP53/p53, nor does the presence of TP53/p53 affect the CC efficiency of cell killing. Activates a G2/M cell cycle checkpoint CC prior to the onset of apoptosis. Apoptosis is inhibited by CC association with RB1. CC -!- SUBUNIT: Component of the THO complex, which is composed of THOC1, CC THOC2, THOC5, THOC6 and THOC7. Together with THOC3, THOC4 and CC UAP56, THO forms the transcription/export (TREX) complex. Binds to CC the hypophosphorylated form of RB1. Interacts with THOC2, UAP56 CC and RNA polymerase II. CC -!- SUBCELLULAR LOCATION: Isoform 1: Nucleus speckle. Nucleus, CC nucleoplasm. Nucleus matrix. Cytoplasm. Note=Can shuttle between CC the nucleus and cytoplasm. Nuclear localization is required for CC induction of apoptotic cell death. Translocates to the cytoplasm CC during the early phase of apoptosis execution. CC -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q96FV9-1; Sequence=Displayed; CC Name=2; Synonyms=p84N5s; CC IsoId=Q96FV9-2; Sequence=VSP_038073, VSP_038074; CC Name=3; Synonyms=p84N5s2; CC IsoId=Q96FV9-3; Sequence=VSP_038071, VSP_038072; CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in various cancer cell CC lines. Expressed at very low levels in normal breast epithelial CC cells and highly expressed in breast tumors. Expression is CC strongly associated with an aggressive phenotype of breast tumors CC and expression correlates with tumor size and the metastatic state CC of the tumor progression. CC -!- INDUCTION: Up-regulated during cell proliferation. CC -!- DOMAIN: An intact death domain is needed for apoptosis. CC -!- PTM: Expression is altered specifically during apoptosis and is CC accompanied by the appearance of novel forms with smaller apparent CC molecular mass. CC -!- SIMILARITY: Contains 1 death domain. 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; L36529; AAA53571.1; -; mRNA. DR EMBL; AY573302; AAT81408.1; -; mRNA. DR EMBL; AY573303; AAT81409.1; -; mRNA. DR EMBL; AK314755; BAG37293.1; -; mRNA. DR EMBL; AP000845; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471113; EAX01732.1; -; Genomic_DNA. DR EMBL; BC010381; AAH10381.1; -; mRNA. DR IPI; IPI00305374; -. DR IPI; IPI00646620; -. DR IPI; IPI00944519; -. DR PIR; A53545; A53545. DR RefSeq; NP_005122.2; -. DR UniGene; Hs.712543; -. DR PDB; 1WXP; NMR; -; A=561-657. DR PDBsum; 1WXP; -. DR STRING; Q96FV9; -. DR PhosphoSite; Q96FV9; -. DR PRIDE; Q96FV9; -. DR Ensembl; ENST00000261600; ENSP00000261600; ENSG00000079134; Homo sapiens. DR GeneID; 9984; -. DR KEGG; hsa:9984; -. DR UCSC; uc002kkj.2; human. DR CTD; 9984; -. DR GeneCards; GC18M000204; -. DR H-InvDB; HIX0014291; -. DR HGNC; HGNC:19070; THOC1. DR HPA; HPA019096; -. DR HPA; HPA019687; -. DR MIM; 606930; gene. DR PharmGKB; PA134887435; -. DR eggNOG; prNOG18629; -. DR HOGENOM; HBG402972; -. DR HOVERGEN; HBG060294; -. DR InParanoid; Q96FV9; -. DR OMA; ILMGNEE; -. DR OrthoDB; EOG9W110J; -. DR NextBio; 37696; -. DR ArrayExpress; Q96FV9; -. DR Bgee; Q96FV9; -. DR CleanEx; HS_THOC1; -. DR Genevestigator; Q96FV9; -. DR GermOnline; ENSG00000079134; Homo sapiens. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell. DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell. DR GO; GO:0000445; C:THO complex part of transcription export co...; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0003711; F:transcription elongation regulator activity; IDA:UniProtKB. DR GO; GO:0006915; P:apoptosis; IDA:UniProtKB. DR GO; GO:0046784; P:intronless viral mRNA export from host nucleus; IDA:UniProtKB. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW. DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR GO; GO:0006350; P:transcription; IEA:UniProtKB-KW. DR InterPro; IPR000488; Death. DR InterPro; IPR011029; DEATH-like. DR InterPro; IPR021861; THO_THOC1. DR Gene3D; G3DSA:1.10.533.10; DEATH_like; 1. DR Pfam; PF00531; Death; 1. DR Pfam; PF11957; efThoc1; 1. DR SMART; SM00005; DEATH; 1. DR SUPFAM; SSF47986; DEATH_like; 1. DR PROSITE; PS50017; DEATH_DOMAIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; KW Complete proteome; Cytoplasm; DNA-binding; mRNA processing; KW mRNA splicing; mRNA transport; Nucleus; Phosphoprotein; RNA-binding; KW Transcription; Transcription regulation; Transport. FT CHAIN 1 657 THO complex subunit 1. FT /FTId=PRO_0000072520. FT DOMAIN 570 653 Death. FT MOTIF 414 430 Nuclear localization signal. FT MOD_RES 2 2 Phosphoserine. FT MOD_RES 133 133 N6-acetyllysine. FT MOD_RES 300 300 N6-acetyllysine. FT MOD_RES 560 560 Phosphoserine. FT VAR_SEQ 86 86 G -> A (in isoform 3). FT /FTId=VSP_038071. FT VAR_SEQ 87 657 Missing (in isoform 3). FT /FTId=VSP_038072. FT VAR_SEQ 363 377 LLSENPPDGERFSKM -> VSSTRNKPMIEKMEI (in FT isoform 2). FT /FTId=VSP_038073. FT VAR_SEQ 378 657 Missing (in isoform 2). FT /FTId=VSP_038074. FT MUTAGEN 617 617 L->P: Loss of ability to induce FT apoptosis. Interfere with normal response FT of SAOS-2 cells to radiation. FT MUTAGEN 620 620 W->P,R: Loss of ability to induce FT apoptosis. Interfere with normal response FT of SAOS-2 cells to radiation. FT CONFLICT 71 71 N -> H (in Ref. 2; AAT81408). FT CONFLICT 130 130 S -> A (in Ref. 1; AAA53571). FT CONFLICT 134 134 N -> S (in Ref. 3; BAG37293). FT CONFLICT 433 433 M -> T (in Ref. 1; AAA53571). FT CONFLICT 480 480 V -> A (in Ref. 1; AAA53571). FT CONFLICT 487 487 V -> M (in Ref. 1; AAA53571). FT CONFLICT 498 498 R -> K (in Ref. 1; AAA53571). FT CONFLICT 519 519 P -> Q (in Ref. 1; AAA53571). FT STRAND 565 567 FT HELIX 571 581 FT TURN 582 584 FT HELIX 585 588 FT TURN 589 593 FT HELIX 596 605 FT HELIX 609 624 FT HELIX 625 627 FT HELIX 630 639 FT HELIX 643 650 SQ SEQUENCE 657 AA; 75666 MW; DB7980BD0F252DAB CRC64; MSPTPPLFSL PEARTRFTKS TREALNNKNI KPLLSTFSQV PGSENEKKCT LDQAFRGILE EEIINHSSCE NVLAIISLAI GGVTEGICTA STPFVLLGDV LDCLPLDQCD TIFTFVEKNV ATWKSNTFYS AGKNYLLRMC NDLLRRLSKS QNTVFCGRIQ LFLARLFPLS EKSGLNLQSQ FNLENVTVFN TNEQESTLGQ KHTEDREEGM DVEEGEMGDE EAPTTCSIPI DYNLYRKFWS LQDYFRNPVQ CYEKISWKTF LKYSEEVLAV FKSYKLDDTQ ASRKKMEELK TGGEHVYFAK FLTSEKLMDL QLSDSNFRRH ILLQYLILFQ YLKGQVKFKS SNYVLTDEQS LWIEDTTKSV YQLLSENPPD GERFSKMVEH ILNTEENWNS WKNEGCPSFV KERTSDTKPT RIIRKRTAPE DFLGKGPTKK ILMGNEELTR LWNLCPDNME ACKSETREHM PTLEEFFEEA IEQADPENMV ENEYKAVNNS NYGWRALRLL ARRSPHFFQP TNQQFKSLPE YLENMVIKLA KELPPPSEEI KTGEDEDEED NDALLKENES PDVRRDKPVT GEQIEVFANK LGEQWKILAP YLEMKDSEIR QIECDSEDMK MRAKQLLVAW QDQEGVHATP ENLINALNKS GLSDLAESLT NDNETNS //