MOM1_ARATH
ID MOM1_ARATH Reviewed; 2001 AA.
AC Q9M658; Q8GXZ0; Q9LN02; Q9M659;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Helicase protein MOM1;
DE EC=3.6.4.-;
DE AltName: Full=Protein MAINTENANCE OF METHYLATION;
DE AltName: Full=Protein MORPHEUS MOLECULE 1;
GN Name=MOM1; Synonyms=MOM; OrderedLocusNames=At1g08060; ORFNames=T6D22.14;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, DISRUPTION PHENOTYPE,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Zurich;
RX PubMed=10821279; DOI=10.1038/35012108;
RA Amedeo P., Habu Y., Afsar K., Mittelsten Scheid O., Paszkowski J.;
RT "Disruption of the plant gene MOM releases transcriptional silencing of
RT methylated genes.";
RL Nature 405:203-206(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1756-2001.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1769-2001.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10899982; DOI=10.2307/3871263;
RA Steimer A., Amedeo P., Afsar K., Fransz P., Mittelsten Scheid O.,
RA Paszkowski J.;
RT "Endogenous targets of transcriptional gene silencing in Arabidopsis.";
RL Plant Cell 12:1165-1178(2000).
RN [7]
RP REVIEW.
RX PubMed=10999407; DOI=10.1023/a:1006487529698;
RA Mittelsten Scheid O., Paszkowski J.;
RT "Transcriptional gene silencing mutants.";
RL Plant Mol. Biol. 43:235-241(2000).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12370435; DOI=10.1073/pnas.202380499;
RA Mittelsten Scheid O., Probst A.V., Afsar K., Paszkowski J.;
RT "Two regulatory levels of transcriptional gene silencing in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13659-13662(2002).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12609046; DOI=10.1046/j.1365-313x.2003.01667.x;
RA Probst A.V., Fransz P.F., Paszkowski J., Mittelsten Scheid O.;
RT "Two means of transcriptional reactivation within heterochromatin.";
RL Plant J. 33:743-749(2003).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17082821; DOI=10.1038/sj.embor.7400791;
RA Vaillant I., Schubert I., Tourmente S., Mathieu O.;
RT "MOM1 mediates DNA-methylation-independent silencing of repetitive
RT sequences in Arabidopsis.";
RL EMBO Rep. 7:1273-1278(2006).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17082818; DOI=10.1038/sj.embor.7400835;
RA Habu Y., Mathieu O., Tariq M., Probst A.V., Smathajitt C., Zhu T.,
RA Paszkowski J.;
RT "Epigenetic regulation of transcription in intermediate heterochromatin.";
RL EMBO Rep. 7:1279-1284(2006).
RN [12]
RP CMM REGIONS, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18725928; DOI=10.1371/journal.pgen.1000165;
RA Caikovski M., Yokthongwattana C., Habu Y., Nishimura T., Mathieu O.,
RA Paszkowski J.;
RT "Divergent evolution of CHD3 proteins resulted in MOM1 refining epigenetic
RT control in vascular plants.";
RL PLoS Genet. 4:E1000165-E1000165(2008).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19910926; DOI=10.1038/emboj.2009.328;
RA Yokthongwattana C., Bucher E., Caikovski M., Vaillant I., Nicolet J.,
RA Mittelsten Scheid O., Paszkowski J.;
RT "MOM1 and Pol-IV/V interactions regulate the intensity and specificity of
RT transcriptional gene silencing.";
RL EMBO J. 29:340-351(2010).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21070421; DOI=10.1111/j.1365-313x.2010.04358.x;
RA Mlotshwa S., Pruss G.J., Gao Z., Mgutshini N.L., Li J., Chen X.,
RA Bowman L.H., Vance V.;
RT "Transcriptional silencing induced by Arabidopsis T-DNA mutants is
RT associated with 35S promoter siRNAs and requires genes involved in siRNA-
RT mediated chromatin silencing.";
RL Plant J. 64:699-704(2010).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20826701; DOI=10.1104/pp.110.162131;
RA Zhou Y., Zhang J., Lin H., Guo G., Guo Y.;
RT "MORPHEUS' MOLECULE1 is required to prevent aberrant RNA transcriptional
RT read-through in Arabidopsis.";
RL Plant Physiol. 154:1272-1280(2010).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20404545; DOI=10.4161/psb.5.6.11663;
RA Habu Y., Yoshikawa M.;
RT "Locus-specific dependency of endogenous silent loci on MOM1 and non-CG
RT methylation in Arabidopsis thaliana.";
RL Plant Signal. Behav. 5:724-726(2010).
CC -!- FUNCTION: Required for the heritable maintenance of transcriptional
CC gene silencing (TGS) in heterochromatin, and particularly in the
CC intermediate bivalent heterochromatin, characterized by an unsual
CC methylation pattern consisting in hypermethylated DNA and histone H3
CC 'Lys-4' methylation (H3K4me) together with depletion of histone H3
CC 'Lys-9' methylation (H3K9me), in a chromatin methylation-independent
CC manner, in a non-CG methylation context. May play a role in the RNA
CC polymerase IV/V (Pol-IV/V)-mediated RNA-directed DNA methylation (RdDM)
CC leading to TGS (also called siRNA-mediated TGS pathway), probably by
CC modulating small interfering RNA (siRNA) accumulation. Especially
CC involved in the gene silencing of the transcriptionally silent
CC information region (TSI), 5S ribosomal RNA genes (localized in the
CC pericentromeric heterochromatin of chromosomes 3, 4, and 5) and of 180-
CC bp satellite repeats and 106B long terminal repeat (LTR)-like repeats
CC of the chromocenters. Prevents the aberrant mRNA transcriptional read-
CC through. {ECO:0000269|PubMed:10821279, ECO:0000269|PubMed:10899982,
CC ECO:0000269|PubMed:12370435, ECO:0000269|PubMed:12609046,
CC ECO:0000269|PubMed:17082818, ECO:0000269|PubMed:17082821,
CC ECO:0000269|PubMed:18725928, ECO:0000269|PubMed:19910926,
CC ECO:0000269|PubMed:20404545, ECO:0000269|PubMed:20826701,
CC ECO:0000269|PubMed:21070421}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10821279}.
CC -!- DISRUPTION PHENOTYPE: Reactivated transcription of heavily methylated
CC silent loci, independently of chromatin demethylation. Releases TSI, 5S
CC ribosomal RNA genes as well as 180-bp and 106B repeats of chromocenters
CC silencing independently of chromatin properties. Partial derepression
CC of 35S promoter homology-dependent TGS in transgenic plants. Abnormal
CC aberrant mRNA transcriptional read-through. Increased expression of
CC minor 5S rRNA species. No nuclear organization alteration.
CC {ECO:0000269|PubMed:10821279, ECO:0000269|PubMed:10899982,
CC ECO:0000269|PubMed:12370435, ECO:0000269|PubMed:12609046,
CC ECO:0000269|PubMed:17082818, ECO:0000269|PubMed:17082821,
CC ECO:0000269|PubMed:18725928, ECO:0000269|PubMed:19910926,
CC ECO:0000269|PubMed:20404545, ECO:0000269|PubMed:20826701,
CC ECO:0000269|PubMed:21070421}.
CC -!- MISCELLANEOUS: Requires for the complete maintenance of the 35S
CC promoter homology-dependent TGS induced by T-DNA construct insertion.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79839.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC42596.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF213627; AAF73380.1; -; mRNA.
DR EMBL; AF213628; AAF73381.1; -; Genomic_DNA.
DR EMBL; AC026875; AAF79839.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28236.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28237.1; -; Genomic_DNA.
DR EMBL; AK117959; BAC42596.1; ALT_INIT; mRNA.
DR EMBL; BT006219; AAP12868.1; -; mRNA.
DR PIR; D86215; D86215.
DR RefSeq; NP_563806.1; NM_100680.4.
DR RefSeq; NP_849608.1; NM_179277.1.
DR PDB; 3VEM; X-ray; 3.20 A; A/B/C/D=1700-1814.
DR PDBsum; 3VEM; -.
DR AlphaFoldDB; Q9M658; -.
DR SMR; Q9M658; -.
DR BioGRID; 22563; 7.
DR IntAct; Q9M658; 4.
DR STRING; 3702.AT1G08060.1; -.
DR iPTMnet; Q9M658; -.
DR PaxDb; Q9M658; -.
DR PRIDE; Q9M658; -.
DR ProteomicsDB; 238300; -.
DR EnsemblPlants; AT1G08060.1; AT1G08060.1; AT1G08060.
DR EnsemblPlants; AT1G08060.2; AT1G08060.2; AT1G08060.
DR GeneID; 837322; -.
DR Gramene; AT1G08060.1; AT1G08060.1; AT1G08060.
DR Gramene; AT1G08060.2; AT1G08060.2; AT1G08060.
DR KEGG; ath:AT1G08060; -.
DR Araport; AT1G08060; -.
DR TAIR; locus:2205205; AT1G08060.
DR eggNOG; KOG0384; Eukaryota.
DR HOGENOM; CLU_001778_0_0_1; -.
DR InParanoid; Q9M658; -.
DR OMA; SPNIFWT; -.
DR PhylomeDB; Q9M658; -.
DR PRO; PR:Q9M658; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9M658; baseline and differential.
DR Genevisible; Q9M658; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:TAIR.
DR GO; GO:0032183; F:SUMO binding; IPI:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0031507; P:heterochromatin assembly; IEA:InterPro.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IMP:TAIR.
DR GO; GO:0010468; P:regulation of gene expression; IMP:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR039322; MOM1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR35116; PTHR35116; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; ATP-binding; Coiled coil; Helicase; Hydrolase; Iron;
KW Iron-sulfur; Metal-binding; Nucleotide-binding; Nucleus;
KW Reference proteome; RNA-mediated gene silencing; Transcription;
KW Transcription regulation.
FT CHAIN 1..2001
FT /note="Helicase protein MOM1"
FT /id="PRO_0000405275"
FT DOMAIN 357..448
FT /note="2Fe-2S ferredoxin-type"
FT DOMAIN 563..722
FT /note="Helicase C-terminal"
FT REGION 19..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..1044
FT /note="Conserved MOM1 Motif 1 (CMM1)"
FT REGION 1466..1517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1528..1547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1624..1644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1734..1815
FT /note="Conserved MOM1 Motif 2 (CMM2), required to mediates
FT gene silencing maintenance"
FT REGION 1915..2001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1993..2001
FT /note="Conserved MOM1 Motif 3 (CMM3)"
FT COILED 693..722
FT /evidence="ECO:0000255"
FT COILED 1130..1168
FT /evidence="ECO:0000255"
FT COILED 1194..1217
FT /evidence="ECO:0000255"
FT COILED 1736..1785
FT /evidence="ECO:0000255"
FT COMPBIAS 19..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1488..1517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1915..1931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1940..1995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 400
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 409
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 412
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT CONFLICT 705
FT /note="K -> M (in Ref. 1; AAF73380)"
FT /evidence="ECO:0000305"
FT CONFLICT 1219
FT /note="D -> E (in Ref. 1; AAF73380)"
FT /evidence="ECO:0000305"
FT HELIX 1735..1807
FT /evidence="ECO:0007829|PDB:3VEM"
FT TURN 1808..1812
FT /evidence="ECO:0007829|PDB:3VEM"
SQ SEQUENCE 2001 AA; 218569 MW; B9C85D4E62704441 CRC64;
MKKDEKIGLT GRTIYTRSLA ASIPASVEQE TPGLRRSSRG TPSTKVITPA SATRKSERLA
PSPASVSKKS GGIVKNSTPS SLRRSNRGKT EVSLQSSKGS DNSIRKGDTS PDIEQRKDSV
EESTDKIKPI MSARSYRALF RGKLKESEAL VDASPNEEEL VVVGCSRRIP AGNDDVQGKT
DCPPPADAGS KRLPVDETSL DKGTDFPLKS VTETEKIVLD ASPIVETGDD SVIGSPSENL
ETQKLQDGKT DCSPPANAES KTLPVGETSL EKEYPQKFQD DNTDCLPPAN AESKRLPVGE
TSLEKDTDFP LKSTTETGKM VLYASPIVET RDDSVICSPS TNLETQKLLV SKTGLETDIV
LPLKRKRDTA EIELDACATV ANGDDHVMSS DGVIPSPSGC KNDNRPEMCN TCKKRQKVNG
DCQNRSVCSC IVQPVEESDN VTQDMKETGP VTSREYEENG QIQHGKSSDP KFYSSVYPEY
WVPVQLSDVQ LEQYCQTLFS KSLSLSSLSK IDLGALEETL NSVRKTCDHP YVMDASLKQL
LTKNLELHEI LDVEIKASGK LHLLDKMLTH IKKNGLKAVV FYQATQTPEG LLLGNILEDF
VGQRFGPKSY EHGIYSSKKN SAINNFNKES QCCVLLLETR ACSQTIKLLR ADAFILFGSS
LNPSHDVKHV EKIKIESCSE RTKIFRLYSV CTVEEKALIL ARQNKRQNKA VENLNRSLTH
ALLMWGASYL FDKLDHFHSS ETPDSGVSFE QSIMDGVIHE FSSILSSKGG EENEVKLCLL
LEAKHAQGTY SSDSTLFGED HIKLSDEESP NIFWSKLLGG KNPMWKYPSD TPQRNRKRVQ
YFEGSEASPK TGDGGNAKKR KKASDDVTDP RVTDPPVDDD ERKASGKDHM GALESPKVIT
LQSSCKSSGT DGTLDGNDAF GLYSMGSHIS GIPEDMLASQ DWGKIPDESQ RRLHTVLKPK
MAKLCQVLHL SDACTSMVGN FLEYVIENHR IYEEPATTFQ AFQIALSWIA ALLVKQILSH
KESLVRANSE LAFKCSRVEV DYIYSILSCM KSLFLEHTQG LQFDCFGTNS KQSVVSTKLV
NESLSGATVR DEKINTKSMR NSSEDEECMT EKRCSHYSTA TRDIEKTISG IKKKYKKQVQ
KLVQEHEEKK MELLNMYADK KQKLETSKSV EAAVIRITCS RTSTQVGDLK LLDHNYERKF
DEIKSEKNEC LKSLEQMHDV AKKKLAEDEA CWINRIKSWA AKLKVCVPIQ SGNNKHFSGS
SNISQNAPDV QICNNANVEA TYADTNCMAS KVNQVPEAEN TLGTMSGGST QQVHEMVDVR
NDETMDVSAL SREQLTKSQS NEHASITVPE ILIPADCQEE FAALNVHLSE DQNCDRITSA
ASDEDVSSRV PEVSQSLENL SASPEFSLNR EEALVTTENR RTSHVGFDTD NILDQQNRED
CSLDQEIPDE LAMPVQHLAS VVETRGAAES DQYGQDICPM PSSLAGKQPD PAANTESENL
EEAIEPQSAG SETVETTDFA ASHQGDQVTC PLLSSPTGNQ PAPEANIEGQ NINTSAEPHV
AGPDAVESGD YAVIDQETMG AQDACSLPSG SVGTQSDLGA NIEGQNVTTV AQLPTDGSDA
VVTGGSPVSD QCAQDASPMP LSSPGNHPDT AVNIEGLDNT SVAEPHISGS DACEMEISEP
GPQVERSTFA NLFHEGGVEH SAGVTALVPS LLNNGTEQIA VQPVPQIPFP VFNDPFLHEL
EKLRRESENS KKTFEEKKSI LKAELERKMA EVQAEFRRKF HEVEAEHNTR TTKIEKDKNL
VIMNKLLANA FLSKCTDKKV SPSGAPRGKI QQLAQRAAQV SALRNYIAPQ QLQASSFPAP
ALVSAPLQLQ QSSFPAPGPA PLQPQASSFP SSVSRPSALL LNFAVCPMPQ PRQPLISNIA
PTPSVTPATN PGLRSPAPHL NSYRPSSSTP VATATPTSSV PPQALTYSAV SIQQQQEQQP
QQSLSSGLQS NNEVVCLSDD E
