HELLS_MOUSE
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 03-AUG-2022, entry version 163.
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},
GN Pasg {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
RC Heart {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
RC FVB/N {ECO:0000312|EMBL:AAH20056.1};
RC TISSUE=Egg {ECO:0000312|EMBL:AAI00395.1}, and
RC Mammary gland {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; 10.
DR DIP; DIP-43735N; -.
DR IntAct; Q60848; 8.
DR MINT; Q60848; -.
DR STRING; 10090.ENSMUSP00000025965; -.
DR iPTMnet; Q60848; -.
DR PhosphoSitePlus; Q60848; -.
DR EPD; Q60848; -.
DR jPOST; Q60848; -.
DR MaxQB; Q60848; -.
DR PaxDb; Q60848; -.
DR PeptideAtlas; Q60848; -.
DR PRIDE; Q60848; -.
DR ProteomicsDB; 269580; -. [Q60848-1]
DR ProteomicsDB; 269581; -. [Q60848-2]
DR Antibodypedia; 3852; 278 antibodies from 33 providers.
DR DNASU; 15201; -.
DR Ensembl; ENSMUST00000025965; ENSMUSP00000025965; ENSMUSG00000025001. [Q60848-1]
DR GeneID; 15201; -.
DR KEGG; mmu:15201; -.
DR UCSC; uc008hjt.1; mouse. [Q60848-1]
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; MNDRKYL; -.
DR OrthoDB; 61251at2759; -.
DR PhylomeDB; Q60848; -.
DR TreeFam; TF329077; -.
DR BioGRID-ORCS; 15201; 7 hits in 77 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 200 other tissues.
DR ExpressionAtlas; Q60848; baseline and differential.
DR Genevisible; Q60848; MM.
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 assembly; IMP:UniProtKB.
DR GO; GO:0031507; P:heterochromatin assembly; 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:0010216; P:maintenance of DNA methylation; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0031508; P:pericentric heterochromatin assembly; IMP:UniProtKB.
DR GO; GO:0001655; P:urogenital system development; IMP:MGI.
DR CDD; cd18009; DEXHc_HELLS_SMARCA6; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR000330; SNF2_N.
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; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
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
