ID   HELLS_MOUSE             Reviewed;         821 AA.
AC   Q60848; Q497T3; Q8VDZ1; Q9CYV7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 2.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=Lymphocyte-specific helicase;
DE            EC=3.6.4.-;
DE   AltName: Full=Proliferation-associated SNF2-like protein;
GN   Name=Hells {ECO:0000312|MGI:MGI:106209};
GN   Synonyms=Lsh {ECO:0000303|PubMed:8647447}, Pasg
GN   {ECO:0000312|EMBL:AAG43373.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAB08015.2}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, AND INDUCTION.
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAB08015.2};
RC   TISSUE=Fetal thymus {ECO:0000312|EMBL:AAB08015.2};
RX   PubMed=8647447; DOI=10.1016/0378-1119(95)00843-8;
RA   Jarvis C.D., Geiman T., Vila-Storm M.P., Osipovich O., Akella U.,
RA   Candeias S., Nathan I., Durum S.K., Muegge K.;
RT   "A novel putative helicase produced in early murine lymphocytes.";
RL   Gene 169:203-207(1996).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAG43373.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAG43373.1};
RX   PubMed=11357197; DOI=10.1002/dvdy.1128;
RA   Raabe E.H., Abdurrahman L., Behbehani G., Arececi R.J.;
RT   "An SNF2 factor involved in mammalian development and cellular
RT   proliferation.";
RL   Dev. Dyn. 221:92-105(2001).
RN   [3] {ECO:0000305, ECO:0000312|EMBL:BAE27697.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE27697.1};
RC   TISSUE=Embryo {ECO:0000312|EMBL:BAB28757.2}, and Heart
RC   {ECO:0000312|EMBL:BAE27697.1};
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   [4] {ECO:0000305, ECO:0000312|EMBL:AAI00395.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAI00395.1}, and FVB/N
RC   {ECO:0000312|EMBL:AAH20056.1};
RC   TISSUE=Egg {ECO:0000312|EMBL:AAI00395.1}, and Mammary gland
RC   {ECO:0000312|EMBL:AAH20056.1};
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   [5]
RP   PROTEIN SEQUENCE OF 31-38, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6] {ECO:0000305}
RP   TISSUE SPECIFICITY.
RX   PubMed=9878251; DOI=10.1006/geno.1998.5557;
RA   Geiman T.M., Durum S.K., Muegge K.;
RT   "Characterization of gene expression, genomic structure, and chromosomal
RT   localization of Hells (Lsh).";
RL   Genomics 54:477-483(1998).
RN   [7] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=10781083; DOI=10.1073/pnas.97.9.4772;
RA   Geiman T.M., Muegge K.;
RT   "Lsh, an SNF2/helicase family member, is required for proliferation of
RT   mature T lymphocytes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:4772-4777(2000).
RN   [8] {ECO:0000305}
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=11325543; DOI=10.1016/s0304-4165(01)00129-5;
RA   Geiman T.M., Tessarollo L., Anver M.R., Kopp J.B., Ward J.M., Muegge K.;
RT   "Lsh, a SNF2 family member, is required for normal murine development.";
RL   Biochim. Biophys. Acta 1526:211-220(2001).
RN   [9] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=11711429; DOI=10.1101/gad.929101;
RA   Dennis K., Fan T., Geiman T., Yan Q., Muegge K.;
RT   "Lsh, a member of the SNF2 family, is required for genome-wide
RT   methylation.";
RL   Genes Dev. 15:2940-2944(2001).
RN   [10] {ECO:0000305}
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=14517253; DOI=10.1093/emboj/cdg493;
RA   Yan Q., Huang J., Fan T., Zhu H., Muegge K.;
RT   "Lsh, a modulator of CpG methylation, is crucial for normal histone
RT   methylation.";
RL   EMBO J. 22:5154-5162(2003).
RN   [11] {ECO:0000305}
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=14612388; DOI=10.1128/mcb.23.23.8416-8428.2003;
RA   Yan Q., Cho E., Lockett S., Muegge K.;
RT   "Association of Lsh, a regulator of DNA methylation, with pericentromeric
RT   heterochromatin is dependent on intact heterochromatin.";
RL   Mol. Cell. Biol. 23:8416-8428(2003).
RN   [12] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=15105378; DOI=10.1101/gad.1176104;
RA   Sun L.-Q., Lee D.W., Zhang Q., Xiao W., Raabe E.H., Meeker A., Miao D.,
RA   Huso D.L., Arceci R.J.;
RT   "Growth retardation and premature aging phenotypes in mice with disruption
RT   of the SNF2-like gene, PASG.";
RL   Genes Dev. 18:1035-1046(2004).
RN   [13] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=15647320; DOI=10.1242/dev.01612;
RA   Fan T., Hagan J.P., Kozlov S.V., Stewart C.L., Muegge K.;
RT   "Lsh controls silencing of the imprinted Cdkn1c gene.";
RL   Development 132:635-644(2005).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung, Spleen, and 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).
CC   -!- FUNCTION: Plays an essential role in normal development and survival.
CC       Involved in regulation of the expansion or survival of lymphoid cells.
CC       Required for de novo or maintenance DNA methylation. May control
CC       silencing of the imprinted CDKN1C gene through DNA methylation. May
CC       play a role in formation and organization of heterochromatin, implying
CC       a functional role in the regulation of transcription and mitosis.
CC       {ECO:0000269|PubMed:10781083, ECO:0000269|PubMed:11325543,
CC       ECO:0000269|PubMed:11357197, ECO:0000269|PubMed:11711429,
CC       ECO:0000269|PubMed:14517253, ECO:0000269|PubMed:14612388,
CC       ECO:0000269|PubMed:15105378, ECO:0000269|PubMed:15647320,
CC       ECO:0000269|PubMed:8647447}.
CC   -!- INTERACTION:
CC       Q60848; P25916: Bmi1; NbExp=2; IntAct=EBI-3043887, EBI-927401;
CC       Q60848; P30658: Cbx2; NbExp=2; IntAct=EBI-3043887, EBI-360174;
CC       Q60848; O88508: Dnmt3a; NbExp=4; IntAct=EBI-3043887, EBI-995154;
CC       Q60848; O88509: Dnmt3b; NbExp=4; IntAct=EBI-3043887, EBI-7987547;
CC       Q60848; P23798: Pcgf2; NbExp=2; IntAct=EBI-3043887, EBI-926857;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10781083,
CC       ECO:0000269|PubMed:14517253, ECO:0000269|PubMed:14612388}. Note=Closely
CC       associated with pericentric heterochromatin.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1 {ECO:0000269|PubMed:11357197, ECO:0000269|PubMed:8647447};
CC         IsoId=Q60848-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:16141072};
CC         IsoId=Q60848-2; Sequence=VSP_052235;
CC   -!- TISSUE SPECIFICITY: Highly expressed in thymus, bone marrow, and
CC       testis. Not detected in heart, brain, liver, kidney, skeletal muscle,
CC       spleen, peripheral blood lymphocytes, small intestine, colon, prostate
CC       or ovary. {ECO:0000269|PubMed:11325543, ECO:0000269|PubMed:11357197,
CC       ECO:0000269|PubMed:9878251}.
CC   -!- DEVELOPMENTAL STAGE: Differentially expressed during embryonic
CC       development, with highest expression in developing face, limbs,
CC       skeletal muscle, heart, and tail. Highly expressed in fetal thymocytes
CC       from day 14 to 16 of gestation, and expressed at much lower levels in
CC       adult thymus. {ECO:0000269|PubMed:10781083,
CC       ECO:0000269|PubMed:11357197, ECO:0000269|PubMed:8647447}.
CC   -!- INDUCTION: By concanavalin or lipopolysaccharide in unactivated
CC       splenocytes. {ECO:0000269|PubMed:10781083, ECO:0000269|PubMed:8647447}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH20056.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U25691; AAB08015.2; -; mRNA.
DR   EMBL; AF155210; AAG43373.1; -; mRNA.
DR   EMBL; AK013266; BAB28757.2; -; mRNA.
DR   EMBL; AK147126; BAE27697.1; -; mRNA.
DR   EMBL; BC020056; AAH20056.1; ALT_INIT; mRNA.
DR   EMBL; BC100394; AAI00395.1; -; mRNA.
DR   CCDS; CCDS29789.1; -. [Q60848-1]
DR   PIR; JC4666; JC4666.
DR   RefSeq; NP_032260.2; NM_008234.3. [Q60848-1]
DR   RefSeq; XP_006526762.1; XM_006526699.3. [Q60848-1]
DR   AlphaFoldDB; Q60848; -.
DR   SMR; Q60848; -.
DR   BioGRID; 200271; 13.
DR   DIP; DIP-43735N; -.
DR   IntAct; Q60848; 8.
DR   MINT; Q60848; -.
DR   STRING; 10090.ENSMUSP00000025965; -.
DR   GlyGen; Q60848; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q60848; -.
DR   PhosphoSitePlus; Q60848; -.
DR   SwissPalm; Q60848; -.
DR   EPD; Q60848; -.
DR   jPOST; Q60848; -.
DR   MaxQB; Q60848; -.
DR   PaxDb; 10090-ENSMUSP00000025965; -.
DR   PeptideAtlas; Q60848; -.
DR   ProteomicsDB; 269580; -. [Q60848-1]
DR   ProteomicsDB; 269581; -. [Q60848-2]
DR   Pumba; Q60848; -.
DR   Antibodypedia; 3852; 310 antibodies from 33 providers.
DR   DNASU; 15201; -.
DR   Ensembl; ENSMUST00000025965.12; ENSMUSP00000025965.6; ENSMUSG00000025001.12. [Q60848-1]
DR   GeneID; 15201; -.
DR   KEGG; mmu:15201; -.
DR   UCSC; uc008hjt.1; mouse. [Q60848-1]
DR   AGR; MGI:106209; -.
DR   CTD; 3070; -.
DR   MGI; MGI:106209; Hells.
DR   VEuPathDB; HostDB:ENSMUSG00000025001; -.
DR   eggNOG; KOG0385; Eukaryota.
DR   GeneTree; ENSGT00740000115593; -.
DR   HOGENOM; CLU_000315_17_3_1; -.
DR   InParanoid; Q60848; -.
DR   OMA; PNIFTDW; -.
DR   OrthoDB; 5482994at2759; -.
DR   PhylomeDB; Q60848; -.
DR   TreeFam; TF329077; -.
DR   BioGRID-ORCS; 15201; 7 hits in 83 CRISPR screens.
DR   ChiTaRS; Hells; mouse.
DR   PRO; PR:Q60848; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q60848; Protein.
DR   Bgee; ENSMUSG00000025001; Expressed in epiblast (generic) and 204 other cell types or tissues.
DR   ExpressionAtlas; Q60848; baseline and differential.
DR   GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005721; C:pericentric heterochromatin; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR   GO; GO:0006306; P:DNA methylation; IMP:MGI.
DR   GO; GO:0006346; P:DNA methylation-dependent heterochromatin formation; IMP:UniProtKB.
DR   GO; GO:0031507; P:heterochromatin formation; IMP:MGI.
DR   GO; GO:0001822; P:kidney development; IMP:UniProtKB.
DR   GO; GO:0030098; P:lymphocyte differentiation; TAS:MGI.
DR   GO; GO:0046651; P:lymphocyte proliferation; IEP:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR   GO; GO:0044027; P:negative regulation of gene expression via CpG island methylation; IMP:UniProtKB.
DR   GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IMP:MGI.
DR   GO; GO:0031508; P:pericentric heterochromatin formation; IMP:UniProtKB.
DR   GO; GO:0001655; P:urogenital system development; IMP:MGI.
DR   CDD; cd18009; DEXHc_HELLS_SMARCA6; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR044753; HELLS_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR47161; LYMPHOID-SPECIFIC HELICASE; 1.
DR   PANTHER; PTHR47161:SF1; LYMPHOID-SPECIFIC HELICASE; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   Genevisible; Q60848; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell cycle; Cell division; Coiled coil;
KW   Developmental protein; Direct protein sequencing; Helicase; Hydrolase;
KW   Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..821
FT                   /note="Lymphocyte-specific helicase"
FT                   /id="PRO_0000260052"
FT   DOMAIN          218..386
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          586..736
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          78..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          14..96
FT                   /evidence="ECO:0000255"
FT   MOTIF           337..340
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        78..95
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..120
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         231..238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         486
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NRZ9"
FT   MOD_RES         498
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1..13
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_052235"
FT   CONFLICT        497
FT                   /note="K -> R (in Ref. 4; AAI00395)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        620
FT                   /note="L -> P (in Ref. 4; AAI00395)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   821 AA;  95126 MW;  8DEC2F2EEFBBD2F5 CRC64;
     MAEQTEPAVI TPAMLEEEEQ LEAAGLEKER KMLEEAQKSW DRESTEIRYR RLQHLLEKSN
     IYSKFLLTKM EQQQLEEQKK KEKLEKKKRS LKLTEGKSLV DGNGEKPVMK KKRGREDESY
     NISEVMSKEE ILSVAKKHKD NEDESSSTTS LCVEDIQKNK DSNSMIKDRL SQTVRQNSKF
     FFDPVRKCNG QPVPFQQPKH FTGGVMRWYQ VEGMEWLRML WENGINGILA DEMGLGKTVQ
     CIATIALMIQ RGVPGPFLVC GPLSTLPNWM AEFKRFTPEI PTLLYHGTRE DRRKLVKNIH
     KRQGTLQIHP VVVTSFEIAM RDQNALQHCY WKYLIVDEGH RIKNMKCRLI RELKRFNADN
     KLLLTGTPLQ NNLSELWSLL NFLLPDVFDD LKSFESWFDI TSLSETAEDI IAKEREQNVL
     HMLHQILTPF LLRRLKSDVA LEVPPKREVV VYAPLCNKQE IFYTAIVNRT IANMFGSCEK
     ETVELSPTGR PKRRSRKSIN YSELDQFPSE LEKLISQIQP EVNRERTVVE GNIPIESEVN
     LKLRNIMMLL RKCCNHPYMI EYPIDPVTQE FKIDEELVTN SGKFLILDRM LPELKKRGHK
     VLVFSQMTSM LDILMDYCHL RNFIFSRLDG SMSYSEREKN IYSFNTDPDV FLFLVSTRAG
     GLGINLTAAD TVIIYDSDWN PQSDLQAQDR CHRIGQTKPV VVYRLVTANT IDQKIVERAA
     AKRKLEKLII HKNHFKGGQS GLSQSKNFLD AKELMELLKS RDYEREVKGS REKVISDEDL
     ELLLDRSDLI DQMKASRPIK GKTGIFKILE NSEDSSAECL F
//