ID SMBT1_HUMAN Reviewed; 866 AA. AC Q9UHJ3; Q402F7; Q96C73; Q9Y4Q9; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2005, sequence version 2. DT 27-MAR-2024, entry version 173. DE RecName: Full=Scm-like with four MBT domains protein 1; DE Short=hSFMBT; DE AltName: Full=Renal ubiquitous protein 1; GN Name=SFMBT1; Synonyms=RU1; 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] (ISOFORM 1), AND TISSUE SPECIFICITY. RX PubMed=10661410; DOI=10.1016/s1074-7613(00)80163-6; RA Morel S., Levy F., Burlet-Schiltz O., Brasseur F., Probst-Kepper M., RA Peitrequin A.L., Monsarrat B., Van Velthoven R., Cerottini J.C., Boon T., RA Gairin J.E., Van den Eynde B.J.; RT "Processing of some antigens by the standard proteasome but not by the RT immunoproteasome results in poor presentation by dendritic cells."; RL Immunity 12:107-117(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Usui H., Ichikawa T., Kobayashi K., Kumanishi T.; RT "SFMBT and H-L(3)MBT interact with each other and regulate HOX expression RT and cell proliferation."; RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Muscle; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 113-866 (ISOFORM 2). 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 [8] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HISTONES. RX PubMed=17599839; DOI=10.1016/j.febslet.2007.06.025; RA Wu S., Trievel R.C., Rice J.C.; RT "Human SFMBT is a transcriptional repressor protein that selectively binds RT the N-terminal tail of histone H3."; RL FEBS Lett. 581:3289-3296(2007). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-775, 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 [10] RP FUNCTION, INTERACTION WITH KDM1A AND RCOR1, IDENTIFICATION IN THE SLC RP COMPLEX, AND MUTAGENESIS OF PHE-173; TRP-180 AND TYR-196. RX PubMed=23592795; DOI=10.1101/gad.210963.112; RA Zhang J., Bonasio R., Strino F., Kluger Y., Holloway J.K., RA Modzelewski A.J., Cohen P.E., Reinberg D.; RT "SFMBT1 functions with LSD1 to regulate expression of canonical histone RT genes and chromatin-related factors."; RL Genes Dev. 27:749-766(2013). RN [11] RP FUNCTION, AND IDENTIFICATION IN VARIOUS COREPRESSOR COMPLEX. RX PubMed=23349461; DOI=10.1074/jbc.m112.429605; RA Lin S., Shen H., Li J.L., Tang S., Gu Y., Chen Z., Hu C., Rice J.C., Lu J., RA Wu L.; RT "Proteomic and functional analyses reveal the role of chromatin reader RT SFMBT1 in regulating epigenetic silencing and the myogenic gene program."; RL J. Biol. Chem. 288:6238-6247(2013). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-767 AND SER-775, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). CC -!- FUNCTION: Histone-binding protein, which is part of various corepressor CC complexes. Mediates the recruitment of corepressor complexes to target CC genes, followed by chromatin compaction and repression of CC transcription. Plays a role during myogenesis: required for the CC maintenance of undifferentiated states of myogenic progenitor cells via CC interaction with MYOD1. Interaction with MYOD1 leads to the recruitment CC of associated corepressors and silencing of MYOD1 target genes. Part of CC the SLC complex in germ cells, where it may play a role during CC spermatogenesis. {ECO:0000269|PubMed:17599839, CC ECO:0000269|PubMed:23349461, ECO:0000269|PubMed:23592795}. CC -!- SUBUNIT: Interacts with MYOD1 (By similarity). Component of the SLC CC (SFMBT1-LSD1-CoREST) corepressor complex, which also contains CC KDM1A/LSD1 and RCOR1/CoREST. Interacts with KDM1A/LSD1 and CC RCOR1/CoREST. Interacts with L3MBTL3 (By similarity). {ECO:0000250, CC ECO:0000250|UniProtKB:Q9JMD1, ECO:0000269|PubMed:17599839, CC ECO:0000269|PubMed:23349461, ECO:0000269|PubMed:23592795}. CC -!- INTERACTION: CC Q9UHJ3; Q7L5A3: ATOSB; NbExp=3; IntAct=EBI-747398, EBI-745689; CC Q9UHJ3; Q16695: H3-4; NbExp=4; IntAct=EBI-747398, EBI-358900; CC Q9UHJ3; P17482: HOXB9; NbExp=3; IntAct=EBI-747398, EBI-745290; CC Q9UHJ3; Q8IXK0: PHC2; NbExp=4; IntAct=EBI-747398, EBI-713786; CC Q9UHJ3; Q96GD3: SCMH1; NbExp=3; IntAct=EBI-747398, EBI-713793; CC Q9UHJ3; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-747398, EBI-12023934; CC Q9UHJ3; Q8TBK6: ZCCHC10; NbExp=6; IntAct=EBI-747398, EBI-597063; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17599839}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UHJ3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UHJ3-2; Sequence=VSP_013857; CC -!- TISSUE SPECIFICITY: Expressed in all cell lines and normal tissues CC tested, including the thymus. {ECO:0000269|PubMed:10661410}. CC -!- DOMAIN: The MBT repeats mediate binding to histones tails; however, in CC contrast to other MBT repeats, does not bind specific histone lysine CC modifications. The MBT repeats lack the conserved Asp and aromatic cage CC at conserved positions (PubMed:23592795). CC {ECO:0000269|PubMed:23592795}. 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; AF168132; AAF19794.1; -; mRNA. DR EMBL; AB189472; BAE43835.1; -; mRNA. DR EMBL; AK313965; BAG36680.1; -; mRNA. DR EMBL; AC099667; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471055; EAW65272.1; -; Genomic_DNA. DR EMBL; BC014614; AAH14614.1; -; mRNA. DR EMBL; AL080140; CAB45734.1; -; mRNA. DR CCDS; CCDS2867.1; -. [Q9UHJ3-1] DR PIR; T12525; T12525. DR RefSeq; NP_057413.2; NM_016329.3. [Q9UHJ3-1] DR RefSeq; XP_005265278.1; XM_005265221.3. DR RefSeq; XP_006713266.1; XM_006713203.3. DR RefSeq; XP_006713267.1; XM_006713204.3. DR RefSeq; XP_011532126.1; XM_011533824.2. DR RefSeq; XP_011532127.1; XM_011533825.2. DR AlphaFoldDB; Q9UHJ3; -. DR SMR; Q9UHJ3; -. DR BioGRID; 119553; 52. DR IntAct; Q9UHJ3; 48. DR MINT; Q9UHJ3; -. DR STRING; 9606.ENSP00000378235; -. DR BindingDB; Q9UHJ3; -. DR ChEMBL; CHEMBL1764944; -. DR GlyGen; Q9UHJ3; 1 site. DR iPTMnet; Q9UHJ3; -. DR PhosphoSitePlus; Q9UHJ3; -. DR BioMuta; SFMBT1; -. DR DMDM; 67461585; -. DR EPD; Q9UHJ3; -. DR jPOST; Q9UHJ3; -. DR MassIVE; Q9UHJ3; -. DR MaxQB; Q9UHJ3; -. DR PaxDb; 9606-ENSP00000378235; -. DR PeptideAtlas; Q9UHJ3; -. DR ProteomicsDB; 84362; -. [Q9UHJ3-1] DR ProteomicsDB; 84363; -. [Q9UHJ3-2] DR Pumba; Q9UHJ3; -. DR ABCD; Q9UHJ3; 1 sequenced antibody. DR Antibodypedia; 31362; 165 antibodies from 21 providers. DR DNASU; 51460; -. DR Ensembl; ENST00000394752.8; ENSP00000378235.2; ENSG00000163935.14. [Q9UHJ3-1] DR GeneID; 51460; -. DR KEGG; hsa:51460; -. DR MANE-Select; ENST00000394752.8; ENSP00000378235.2; NM_016329.4; NP_057413.2. DR UCSC; uc003dgh.4; human. [Q9UHJ3-1] DR AGR; HGNC:20255; -. DR CTD; 51460; -. DR DisGeNET; 51460; -. DR GeneCards; SFMBT1; -. DR HGNC; HGNC:20255; SFMBT1. DR HPA; ENSG00000163935; Tissue enhanced (testis). DR MIM; 607319; gene. DR neXtProt; NX_Q9UHJ3; -. DR OpenTargets; ENSG00000163935; -. DR PharmGKB; PA134898464; -. DR VEuPathDB; HostDB:ENSG00000163935; -. DR eggNOG; KOG3766; Eukaryota. DR GeneTree; ENSGT00940000157363; -. DR HOGENOM; CLU_005352_0_0_1; -. DR InParanoid; Q9UHJ3; -. DR OMA; HWSLKNG; -. DR OrthoDB; 5405166at2759; -. DR PhylomeDB; Q9UHJ3; -. DR TreeFam; TF316498; -. DR PathwayCommons; Q9UHJ3; -. DR SignaLink; Q9UHJ3; -. DR BioGRID-ORCS; 51460; 12 hits in 1157 CRISPR screens. DR ChiTaRS; SFMBT1; human. DR GenomeRNAi; 51460; -. DR Pharos; Q9UHJ3; Tbio. DR PRO; PR:Q9UHJ3; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q9UHJ3; Protein. DR Bgee; ENSG00000163935; Expressed in sperm and 171 other cell types or tissues. DR ExpressionAtlas; Q9UHJ3; baseline and differential. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central. DR GO; GO:0042393; F:histone binding; IDA:UniProtKB. DR GO; GO:0003714; F:transcription corepressor activity; TAS:UniProtKB. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0048635; P:negative regulation of muscle organ development; IMP:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW. DR CDD; cd20111; MBT_SFMBT1_rpt1; 1. DR CDD; cd20113; MBT_SFMBT1_rpt2; 1. DR CDD; cd20115; MBT_SFMBT1_rpt3; 1. DR CDD; cd20117; MBT_SFMBT1_rpt4; 1. DR CDD; cd09581; SAM_Scm-like-4MBT1_2; 1. DR Gene3D; 2.30.30.140; -; 4. DR Gene3D; 3.90.1150.190; SLED domain; 1. DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1. DR InterPro; IPR004092; Mbt. DR InterPro; IPR047352; MBT_SFMBT1_rpt2. DR InterPro; IPR047351; MBT_SFMBT1_rpt3. DR InterPro; IPR001660; SAM. DR InterPro; IPR013761; SAM/pointed_sf. DR InterPro; IPR037604; Scm-like-4MBT1/2_SAM. DR InterPro; IPR021987; SLED. DR InterPro; IPR038348; SLED_sf. DR PANTHER; PTHR12247; POLYCOMB GROUP PROTEIN; 1. DR PANTHER; PTHR12247:SF77; SCM-LIKE WITH FOUR MBT DOMAINS PROTEIN 1; 1. DR Pfam; PF02820; MBT; 4. DR Pfam; PF00536; SAM_1; 1. DR Pfam; PF12140; SLED; 1. DR SMART; SM00561; MBT; 4. DR SMART; SM00454; SAM; 1. DR SUPFAM; SSF47769; SAM/Pointed domain; 1. DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 4. DR PROSITE; PS51079; MBT; 4. DR Genevisible; Q9UHJ3; HS. PE 1: Evidence at protein level; KW Alternative splicing; Chromatin regulator; Differentiation; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Repressor; Spermatogenesis; KW Transcription; Transcription regulation. FT CHAIN 1..866 FT /note="Scm-like with four MBT domains protein 1" FT /id="PRO_0000071966" FT REPEAT 20..120 FT /note="MBT 1" FT REPEAT 128..232 FT /note="MBT 2" FT REPEAT 242..348 FT /note="MBT 3" FT REPEAT 356..453 FT /note="MBT 4" FT DOMAIN 796..864 FT /note="SAM" FT REGION 34..42 FT /note="Antigenic epitope" FT REGION 641..777 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 661..679 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 699..727 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 735..750 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 751..777 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 767 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 775 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 778..820 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_013857" FT MUTAGEN 173 FT /note="F->A: Reduced histone-binding." FT /evidence="ECO:0000269|PubMed:23592795" FT MUTAGEN 180 FT /note="W->A: Abolishes histone-binding." FT /evidence="ECO:0000269|PubMed:23592795" FT MUTAGEN 196 FT /note="Y->A: Reduced histone-binding." FT /evidence="ECO:0000269|PubMed:23592795" FT CONFLICT 642 FT /note="K -> R (in Ref. 1; AAF19794)" FT /evidence="ECO:0000305" FT CONFLICT 767 FT /note="S -> F (in Ref. 1; AAF19794)" FT /evidence="ECO:0000305" SQ SEQUENCE 866 AA; 98141 MW; DCE67BF35C413EB7 CRC64; MNGEQQLDAD AGSGMEEVEL SWEDYLEETG STAVPYGSFK HVDTRLQNGF APGMKLEVAV RTDPETYWVA TVITTCEQLL LLRYDGYGED RRADFWCDIR KADLYPIGWC EQNKKTLEAP EGIRDKVSDW DEFLRQTLIG ACSPPVPLLE GLRNGRNPLD LIAPGSRLEC QAFQDSLSTW IVTVVENIGG RLKLRYEGLE SSDNYEHWLY YLDPFLHHVG WAAQQGYELQ PPSAIRHLKN EAEWQEILAK VKEEEEEPLP SYLFKDKQVI GIHTFSVNMK LEAVDPWSPF GISPATVVKV FDEKYFLVEM DDLRPENHAR RSFVCHADSP GIFPVQWSLK NGLHISPPPG YPSQDFDWAD YLKQCGAEAA PQRCFPPLIS EHEFKENMKL EAVNPILPEE VCVATITAVR GSYLWLQLEG SKKPIPECIV SVESMDIFPL GWCETNGHPL STPRRARVYK QRKIAVVQPE KQVPSSRTVH EGLRNQELNS TESVMINGKY CCPKIYFNHR CFSGPYLNKG RIAELPQCVG PGNCVLVLRE VLTLLINAAY KPSRVLRELQ LDKDSVWHGC GEVLKAKYKG KSYRATVEIV KTADRVTEFC RQTCIKLECC PNLFGPRMVL DKCSENCSVL TKTKYTHYYG KKKNKRIGRP PGGHSNLACA LKKASKRRKR RKNVFVHKKK RSSASVDNTP AGSPQGSGGE DEDDPDEGDD DSLSEGSTSE QQDELQEESE MSEKKSCSSS PTQSEISTSL PPDRQRRKRE LRTFSFSDDE NKPPSPKEIR IEVAERLHLD SNPLKWSVAD VVRFIRSTDC APLARIFLDQ EIDGQALLLL TLPTVQECMD LKLGPAIKLC HHIERIKFAF YEQFAN //