SMBT1_HUMAN
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 03-AUG-2022, entry version 164.
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. {ECO:0000250, ECO:0000269|PubMed:17599839,
CC ECO:0000269|PubMed:23349461, ECO:0000269|PubMed:23592795}.
CC -!- INTERACTION:
CC Q9UHJ3; Q7L5A3: FAM214B; 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}.
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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. [Q9UHJ3-1]
DR RefSeq; XP_006713266.1; XM_006713203.3. [Q9UHJ3-1]
DR RefSeq; XP_006713267.1; XM_006713204.3. [Q9UHJ3-1]
DR RefSeq; XP_011532126.1; XM_011533824.2. [Q9UHJ3-1]
DR RefSeq; XP_011532127.1; XM_011533825.2. [Q9UHJ3-1]
DR AlphaFoldDB; Q9UHJ3; -.
DR SMR; Q9UHJ3; -.
DR BioGRID; 119553; 46.
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; Q9UHJ3; -.
DR PeptideAtlas; Q9UHJ3; -.
DR PRIDE; Q9UHJ3; -.
DR ProteomicsDB; 84362; -. [Q9UHJ3-1]
DR ProteomicsDB; 84363; -. [Q9UHJ3-2]
DR ABCD; Q9UHJ3; 1 sequenced antibody.
DR Antibodypedia; 31362; 144 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 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; HQVGWAS; -.
DR PhylomeDB; Q9UHJ3; -.
DR TreeFam; TF316498; -.
DR PathwayCommons; Q9UHJ3; -.
DR SignaLink; Q9UHJ3; -.
DR BioGRID-ORCS; 51460; 9 hits in 1078 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 169 other tissues.
DR ExpressionAtlas; Q9UHJ3; baseline and differential.
DR Genevisible; Q9UHJ3; HS.
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:0048635; P:negative regulation of muscle organ development; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR CDD; cd09581; SAM_Scm-like-4MBT1_2; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 3.90.1150.190; -; 1.
DR InterPro; IPR004092; Mbt.
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 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; SSF47769; 1.
DR PROSITE; PS51079; MBT; 4.
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
