M10L1_MOUSE
ID M10L1_MOUSE Reviewed; 1187 AA.
AC Q99MV5; Q7TPA9; Q8C3W0; Q924C2;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=RNA helicase Mov10l1 {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000305|PubMed:25762440};
DE AltName: Full=Cardiac helicase activated by MEF2 protein {ECO:0000303|PubMed:11397016};
DE AltName: Full=Cardiac-specific RNA helicase {ECO:0000303|PubMed:11397016};
DE AltName: Full=Moloney leukemia virus 10-like protein 1 homolog {ECO:0000305};
DE Short=MOV10-like protein 1 homolog {ECO:0000305};
GN Name=Mov10l1 {ECO:0000312|MGI:MGI:1891384};
GN Synonyms=Champ {ECO:0000303|PubMed:11397016};
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=11279525; DOI=10.1038/86927;
RA Wang P.J., McCarrey J.R., Yang F., Page D.C.;
RT "An abundance of X-linked genes expressed in spermatogonia.";
RL Nat. Genet. 27:422-426(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=NIH Swiss; TISSUE=Heart;
RX PubMed=11397016; DOI=10.1006/dbio.2001.0277;
RA Liu Z.-P., Nakagawa O., Nakagawa M., Yanagisawa H., Passier R.,
RA Richardson J.A., Srivastava D., Olson E.N.;
RT "CHAMP, a novel cardiac-specific helicase regulated by MEF2C.";
RL Dev. Biol. 234:497-509(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INDUCTION, AND TISSUE SPECIFICITY.
RC STRAIN=NIH Swiss;
RX PubMed=12754203; DOI=10.1074/jbc.m300014200;
RA Ueyama T., Kasahara H., Ishiwata T., Yamasaki N., Izumo S.;
RT "Csm, a cardiac-specific isoform of the RNA helicase Mov10l1, is regulated
RT by Nkx2.5 in embryonic heart.";
RL J. Biol. Chem. 278:28750-28757(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 769-1187.
RC STRAIN=C57BL/6J; TISSUE=Heart;
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 FUNCTION (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), MUTAGENESIS OF
RP 888-ASP--GLN-892, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11854500; DOI=10.1073/pnas.261708699;
RA Liu Z.-P., Olson E.N.;
RT "Suppression of proliferation and cardiomyocyte hypertrophy by CHAMP, a
RT cardiac-specific RNA helicase.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2043-2048(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND INTERACTION WITH PIWIL1; PIWIL2 AND PIWIL4.
RX PubMed=20534472; DOI=10.1073/pnas.1003953107;
RA Zheng K., Xiol J., Reuter M., Eckardt S., Leu N.A., McLaughlin K.J.,
RA Stark A., Sachidanandam R., Pillai R.S., Wang P.J.;
RT "Mouse MOV10L1 associates with Piwi proteins and is an essential component
RT of the Piwi-interacting RNA (piRNA) pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11841-11846(2010).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP HSPA2; PIWIL2 AND PIWIL4.
RX PubMed=20547853; DOI=10.1073/pnas.1007158107;
RA Frost R.J., Hamra F.K., Richardson J.A., Qi X., Bassel-Duby R., Olson E.N.;
RT "MOV10L1 is necessary for protection of spermatocytes against
RT retrotransposons by Piwi-interacting RNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11847-11852(2010).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=23166510; DOI=10.1371/journal.pgen.1003038;
RA Zheng K., Wang P.J.;
RT "Blockade of pachytene piRNA biogenesis reveals a novel requirement for
RT maintaining post-meiotic germline genome integrity.";
RL PLoS Genet. 8:E1003038-E1003038(2012).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, RNA-BINDING, INTERACTION WITH PLD6, AND
RP MUTAGENESIS OF LYS-778.
RX PubMed=25762440; DOI=10.1101/gad.254631.114;
RA Vourekas A., Zheng K., Fu Q., Maragkakis M., Alexiou P., Ma J.,
RA Pillai R.S., Mourelatos Z., Wang P.J.;
RT "The RNA helicase MOV10L1 binds piRNA precursors to initiate piRNA
RT processing.";
RL Genes Dev. 29:617-629(2015).
CC -!- FUNCTION: [Isoform 1]: ATP-dependent RNA helicase required during
CC spermatogenesis to repress transposable elements and prevent their
CC mobilization, which is essential for germline integrity
CC (PubMed:20534472, PubMed:20547853, PubMed:23166510, PubMed:25762440).
CC Acts via the piRNA metabolic process, which mediates the repression of
CC transposable elements during meiosis by forming complexes composed of
CC piRNAs and Piwi proteins and governs the methylation and subsequent
CC repression of transposons (PubMed:20534472, PubMed:20547853,
CC PubMed:23166510, PubMed:25762440). Involved in the primary piRNA
CC metabolic process (PubMed:20534472, PubMed:20547853, PubMed:23166510,
CC PubMed:25762440). Specifically binds to piRNA precursors and promotes
CC the generation of intermediate piRNA processing fragments that are
CC subsequently loaded to Piwi proteins (PubMed:25762440). Acts via its
CC ATP-dependent RNA helicase activity: displays 5'-3' RNA unwinding
CC activity and probably mediates unwinding and funneling of single-
CC stranded piRNA precursor transcripts to the endonuclease that catalyzes
CC the first cleavage step of piRNA processing to generate piRNA
CC intermediate fragments that are subsequently loaded to Piwi proteins
CC (PubMed:25762440). {ECO:0000269|PubMed:20534472,
CC ECO:0000269|PubMed:20547853, ECO:0000269|PubMed:23166510,
CC ECO:0000269|PubMed:25762440}.
CC -!- FUNCTION: [Isoform 2]: May act downstream of MEF2C during heart
CC formation. Acts as a cardiac-specific suppressor of cardiomyocyte
CC hypertrophy and cell cycle progression, suggesting that it may suppress
CC these processes through the regulation of CDKN1A. Such results however
CC require additional evidence. {ECO:0000305|PubMed:11854500}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000305|PubMed:25762440};
CC -!- SUBUNIT: Interacts with PIWIL1 (PubMed:20534472). Interacts with PIWIL2
CC (PubMed:20534472, PubMed:20547853). Interacts with PIWIL4
CC (PubMed:20534472, PubMed:20547853). Interacts with HSPA2
CC (PubMed:20547853). Interacts with PLD6 (PubMed:25762440).
CC {ECO:0000269|PubMed:20534472, ECO:0000269|PubMed:20547853,
CC ECO:0000269|PubMed:25762440}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:20534472, ECO:0000269|PubMed:23166510}.
CC Note=Component of the meiotic nuage, also named P granule, a germ-cell-
CC specific organelle required to repress transposon activity during
CC meiosis (PubMed:20534472, PubMed:23166510).
CC {ECO:0000269|PubMed:23166510, ECO:0000305|PubMed:20534472}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:11854500}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q99MV5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99MV5-2; Sequence=VSP_003392;
CC Name=3; Synonyms=Csm {ECO:0000303|PubMed:12754203}, Cardiac-specific
CC isoform of Mov10l1 {ECO:0000303|PubMed:12754203};
CC IsoId=Q99MV5-3; Sequence=VSP_010949;
CC -!- TISSUE SPECIFICITY: Isoform 1: Specifically expressed in testis
CC (PubMed:12754203). Isoform 1: In testis, present in pachytene
CC spermatocytes but absent in postmeiotic spermatids (at protein level)
CC (PubMed:20534472, PubMed:20547853). Isoform 2: Present in
CC cardiomyocytes (at protein level) (PubMed:11279525). Isoform 2: Heart
CC specific (PubMed:11854500). Isoform 3: Heart specific and is
CC specifically expressed in cardiac myocytes (PubMed:12754203).
CC {ECO:0000269|PubMed:11279525, ECO:0000269|PubMed:11854500,
CC ECO:0000269|PubMed:12754203, ECO:0000269|PubMed:20547853}.
CC -!- DEVELOPMENTAL STAGE: [Isoform 2]: Expression is first observed in the
CC linear heart tube at 8 dpc. The highest expression is in the region
CC that will give rise to the ventricular segments. At 9.5 dpc, the
CC ventricular expression is maintained in the looped heart tube. In the
CC adult, expression is observed exclusively within myocardial cells.
CC {ECO:0000269|PubMed:11854500}.
CC -!- INDUCTION: Isoform 2: Activated by MEF2C. Isoform 3: Activated by Nkx2-
CC 5. {ECO:0000269|PubMed:12754203}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and healthy but show male
CC sterility due to defects in spermatogenesis at early prophase of
CC meiosis I (PubMed:20534472, PubMed:20547853, PubMed:23166510).
CC Retrotransposons are derepressed due to DNA demethylation
CC (PubMed:20534472). Defects are caused by impaired piRNA biogenesis
CC during pachytene (PubMed:20534472, PubMed:20547853). The absence of
CC pachytene piRNAs causes disruption of germ cell development and results
CC in defects in post-meiotic genome integrity (PubMed:23166510). Mice do
CC not show any cardiac abnormalities (PubMed:20547853).
CC {ECO:0000269|PubMed:20534472, ECO:0000269|PubMed:20547853,
CC ECO:0000269|PubMed:23166510}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. SDE3 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP60176.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF285587; AAK31966.1; -; mRNA.
DR EMBL; AF340211; AAK77049.1; -; mRNA.
DR EMBL; AY303754; AAP60176.1; ALT_INIT; mRNA.
DR EMBL; AK084786; BAC39279.1; -; mRNA.
DR CCDS; CCDS27737.1; -. [Q99MV5-1]
DR RefSeq; NP_112550.2; NM_031260.2.
DR RefSeq; XP_006521621.1; XM_006521558.3.
DR AlphaFoldDB; Q99MV5; -.
DR SMR; Q99MV5; -.
DR BioGRID; 219930; 2.
DR STRING; 10090.ENSMUSP00000118437; -.
DR iPTMnet; Q99MV5; -.
DR PhosphoSitePlus; Q99MV5; -.
DR PaxDb; Q99MV5; -.
DR PRIDE; Q99MV5; -.
DR ProteomicsDB; 292063; -. [Q99MV5-1]
DR ProteomicsDB; 292064; -. [Q99MV5-2]
DR ProteomicsDB; 292065; -. [Q99MV5-3]
DR DNASU; 83456; -.
DR GeneID; 83456; -.
DR KEGG; mmu:83456; -.
DR CTD; 54456; -.
DR MGI; MGI:1891384; Mov10l1.
DR eggNOG; KOG1804; Eukaryota.
DR InParanoid; Q99MV5; -.
DR BioGRID-ORCS; 83456; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Mov10l1; mouse.
DR PRO; PR:Q99MV5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q99MV5; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; IDA:UniProtKB.
DR GO; GO:0071546; C:pi-body; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0034584; F:piRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IMP:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; IMP:UniProtKB.
DR GO; GO:0007141; P:male meiosis I; IMP:UniProtKB.
DR GO; GO:0007140; P:male meiotic nuclear division; IMP:UniProtKB.
DR GO; GO:0045786; P:negative regulation of cell cycle; IDA:UniProtKB.
DR GO; GO:0034587; P:piRNA metabolic process; IMP:UniProtKB.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF13086; AAA_11; 2.
DR Pfam; PF13087; AAA_12; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Developmental protein;
KW Differentiation; Helicase; Hydrolase; Meiosis; Nucleotide-binding;
KW Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing;
KW Spermatogenesis.
FT CHAIN 1..1187
FT /note="RNA helicase Mov10l1"
FT /id="PRO_0000080707"
FT REPEAT 642..652
FT /note="1"
FT REPEAT 653..663
FT /note="2"
FT REPEAT 664..674
FT /note="3"
FT REPEAT 675..685
FT /note="4"
FT REPEAT 686..696
FT /note="5"
FT REGION 273..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..696
FT /note="5 X 11 AA tandem repeats of [TI]-R-N-[DN]-[GS]-Q-
FT [SP]-I-T-[NK]-[IVN]"
FT REGION 686..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 888..891
FT /note="DEAG box"
FT COMPBIAS 292..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..717
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 772..779
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..825
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12754203"
FT /id="VSP_010949"
FT VAR_SEQ 1..637
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11397016"
FT /id="VSP_003392"
FT MUTAGEN 778
FT /note="K->A: Catalytically inactive mutant. Homozygous
FT knockin male mice are sterile and display meiotic arrest at
FT the zygotene-like stage of prophase I. LINE1
FT retrotransposons are derepressed and piRNA biogenesis is
FT abolished."
FT /evidence="ECO:0000269|PubMed:25762440"
FT MUTAGEN 888..892
FT /note="DEAGQ->GGAAG: Isoform 2: Abolishes the suppressor of
FT cell proliferation activity."
FT /evidence="ECO:0000269|PubMed:11854500"
FT CONFLICT 821
FT /note="P -> L (in Ref. 2 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1187 AA; 132792 MW; 6A3A455DE3C0CB00 CRC64;
MIDDLIYFSN DAVTSTVLLN VGQEVIAVVE ENKVSNGLKA IRVEAVSDKW EDDSKNSSKG
LSDSSPRVLI GCVTSMLEGA GYISQTTYFS LESVCEGFHP CKGDWVEAEY WIRPGTWSSE
AISVKPLRYK RVDKVCISSL CGRNGVIEDS IFFSLDSLKL PEGYIPRRHD IVNAVVVESS
QSCYIWRALC MTPVKRDATL GEAPQEPYGA LLLKNKGDIE VTRMTSFGTL KEGESKSIVI
WIENKGKFSR ELVSCRLANW DKAHQFRFET QGRSKSCPGA AAGSVPEGEN VNSLNHHRED
KTDEIPESRL ANSTEISPDG CACKEESREK GNTPEKQEPE PGGLIPPGEK THIVVTCSAK
NPGRCKELLL LCFSDFLIGR HLEVSVVSSE EALIAVREPF SWKKPKSSQT LVSAKTTVVV
TTQKRNSRRQ LPSFLPQYPI PDRLKKCVEQ KIDILTFQPL LAELLNMSNY KEKFSTLLWL
EEIHAEIELK EYNMSRVVLK RKGDLLVLEV PGLAESRPSL YAGDKLILKS QEYNGHVIEY
IGYVMEIHEE DVTLKLNPGF EQMYNFEPMD VEFTYNRTTS RRCHYALEQV IHLGVKVLFP
EEIILQSPQV TGNWSLAQDT KNDGQSITNI TRNDGQSMTK VTRNDSQSIT NIIRNDGQSI
TNVTRNDGQP ITKVTRNNSQ SITNITRNDG QPITKNKKTV KDQTKHTTEE RHVGTTDQPE
KASSTAETMD EIQIPKARDK EFFNPVLNEN QKLAVRRILS GDCRPLPYIL FGPPGTGKTV
TIIEAVLQVH YALPDSRILV CAPSNSAADL VCLRLHESKV PKPAAMVRVN ATCRFEETII
DAIKPYCRDG EDIWRASRFR IIITTCSSAG LFYQIGVRVG YFTHVFVDEA GQASEPECLI
PLGLISDING QIVLAGDPMQ LGPVIKSRLA MAYGLNVSML ERLMSRPAYL RDENAFGACG
AYNPLLVTKL VKNYRSHSAL LALPSRLFYH RELEVCADPK VVTSLLGWEK LPRKGFPLIF
HGVRGNEARE GRSPSWFSPA EAVQVMRYCC LLARSVSSQV SSKDIGVITP YRKQVEKIKI
LLRNVDLTDI KVGSVEEFQG QEYLVIVIST VRSNEDRFED DRYFLGFLSN SKRFNVAITR
PKALLIILGN PHVLVRDPCF GALLEYSVSN GVYTGCDLPP ELQALQK
