ID YTDC2_MOUSE Reviewed; 1445 AA.
AC B2RR83;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=3'-5' RNA helicase YTHDC2 {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000269|PubMed:29360036};
DE AltName: Full=Keen to exit meiosis leaving testes under-populated protein {ECO:0000303|PubMed:29360036};
DE Short=Ketu {ECO:0000303|PubMed:29360036};
DE AltName: Full=YTH domain-containing protein C2 {ECO:0000303|PubMed:28809393};
DE Short=mYTHDC2 {ECO:0000303|PubMed:29033321};
GN Name=Ythdc2 {ECO:0000303|PubMed:28809393, ECO:0000312|MGI:MGI:2448561};
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1278 AND SER-1282, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1104; SER-1105; SER-1107;
RP SER-1278; SER-1282 AND SER-1296, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Pancreas, 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).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=28809393; DOI=10.1038/cr.2017.99;
RA Hsu P.J., Zhu Y., Ma H., Guo Y., Shi X., Liu Y., Qi M., Lu Z., Shi H.,
RA Wang J., Cheng Y., Luo G., Dai Q., Liu M., Guo X., Sha J., Shen B., He C.;
RT "Ythdc2 is an N(6)-methyladenosine binding protein that regulates mammalian
RT spermatogenesis.";
RL Cell Res. 27:1115-1127(2017).
RN [5]
RP FUNCTION, AND INTERACTION WITH MEIOC.
RX PubMed=28380054; DOI=10.1371/journal.pgen.1006704;
RA Soh Y.Q.S., Mikedis M.M., Kojima M., Godfrey A.K., de Rooij D.G.,
RA Page D.C.;
RT "Meioc maintains an extended meiotic prophase I in mice.";
RL PLoS Genet. 13:E1006704-E1006704(2017).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP RNA-BINDING, AND INTERACTION WITH MEIOC.
RX PubMed=29087293; DOI=10.7554/elife.26116;
RA Bailey A.S., Batista P.J., Gold R.S., Chen Y.G., de Rooij D.G., Chang H.Y.,
RA Fuller M.T.;
RT "The conserved RNA helicase YTHDC2 regulates the transition from
RT proliferation to differentiation in the germline.";
RL Elife 6:0-0(2017).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND INTERACTION WITH XRN1 AND MEIOC.
RX PubMed=29033321; DOI=10.1016/j.molcel.2017.09.021;
RA Wojtas M.N., Pandey R.R., Mendel M., Homolka D., Sachidanandam R.,
RA Pillai R.S.;
RT "Regulation of m6A transcripts by the 3'-5' RNA helicase YTHDC2 is
RT essential for a successful meiotic program in the mammalian germline.";
RL Mol. Cell 68:374-387(2017).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF HIS-327.
RX PubMed=29360036; DOI=10.7554/elife.30919;
RA Jain D., Puno M.R., Meydan C., Lailler N., Mason C.E., Lima C.D.,
RA Anderson K.V., Keeney S.;
RT "Ketu mutant mice uncover an essential meiotic function for the ancient RNA
RT helicase YTHDC2.";
RL Elife 7:0-0(2018).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=32470506; DOI=10.1016/j.gene.2020.144810;
RA Zeng M., Dai X., Liang Z., Sun R., Huang S., Luo L., Li Z.;
RT "Critical roles of mRNA m6A modification and YTHDC2 expression for meiotic
RT initiation and progression in female germ cells.";
RL Gene 753:144810-144810(2020).
RN [10]
RP INTERACTION WITH RBM46.
RX PubMed=36001654; DOI=10.1126/sciadv.abq2945;
RA Qian B., Li Y., Yan R., Han S., Bu Z., Gong J., Zheng B., Yuan Z., Ren S.,
RA He Q., Zhang J., Xu C., Wang R., Sun Z., Lin M., Zhou J., Ye L.;
RT "RNA binding protein RBM46 regulates mitotic-to-meiotic transition in
RT spermatogenesis.";
RL Sci. Adv. 8:eabq2945-eabq2945(2022).
CC -!- FUNCTION: 3'-5' RNA helicase that plays a key role in the male and
CC female germline by promoting transition from mitotic to meiotic
CC divisions in stem cells (PubMed:28380054, PubMed:28809393,
CC PubMed:29033321, PubMed:29087293, PubMed:29360036, PubMed:32470506).
CC Specifically recognizes and binds N6-methyladenosine (m6A)-containing
CC RNAs, a modification present at internal sites of mRNAs and some non-
CC coding RNAs that plays a role in the efficiency of RNA processing and
CC stability (PubMed:29360036). Essential for ensuring a successful
CC progression of the meiotic program in the germline by regulating the
CC level of m6A-containing RNAs (PubMed:29033321). Acts by binding and
CC promoting degradation of m6A-containing mRNAs: the 3'-5' RNA helicase
CC activity is required for this process and RNA degradation may be
CC mediated by XRN1 exoribonuclease (PubMed:29033321). Required for both
CC spermatogenesis and oogenesis (PubMed:28809393, PubMed:29033321).
CC {ECO:0000269|PubMed:28380054, ECO:0000269|PubMed:28809393,
CC ECO:0000269|PubMed:29033321, ECO:0000269|PubMed:29087293,
CC ECO:0000269|PubMed:29360036, ECO:0000269|PubMed:32470506}.
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:0000269|PubMed:29360036};
CC -!- SUBUNIT: Interacts with MEIOC; binds transcripts that regulate the
CC mitotic cell cycle inhibiting progression into metaphase, thereby
CC allowing meiotic prophase to proceed normally (PubMed:28380054,
CC PubMed:29087293). Interacts (via ANK repeats) with XRN1 (By
CC similarity). Interacts with ZCCHC4 (By similarity). Associates with the
CC small ribosomal subunit (By similarity). Interacts with RBM46
CC (PubMed:36001654). {ECO:0000250|UniProtKB:Q9H6S0,
CC ECO:0000269|PubMed:28380054, ECO:0000269|PubMed:29087293,
CC ECO:0000269|PubMed:36001654}.
CC -!- INTERACTION:
CC B2RR83; A2AG06: Meioc; NbExp=4; IntAct=EBI-8572369, EBI-11664020;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29033321,
CC ECO:0000269|PubMed:29087293, ECO:0000269|PubMed:29360036}. Cytoplasm,
CC perinuclear region {ECO:0000250|UniProtKB:Q9H6S0}.
CC -!- TISSUE SPECIFICITY: Present in male and female germ cells (at protein
CC level) (PubMed:29033321, PubMed:32470506). Highly expressed in testis
CC (PubMed:28809393, PubMed:29033321, PubMed:29087293, PubMed:29360036).
CC Not detected in spermatogonia next to the tubule wall but is strongly
CC expressed in spermatocytes, suggesting that it is up-regulated in germ
CC cells upon entry into meiosis (at protein level) (PubMed:29087293).
CC {ECO:0000269|PubMed:28809393, ECO:0000269|PubMed:29033321,
CC ECO:0000269|PubMed:29087293, ECO:0000269|PubMed:29360036,
CC ECO:0000269|PubMed:32470506}.
CC -!- DEVELOPMENTAL STAGE: Expression rises between 7 and 12 d.p.p. and
CC remains steady through adulthood. {ECO:0000269|PubMed:28809393}.
CC -!- DOMAIN: The YTH domain mediates RNA-binding. It recognizes and binds
CC N6-methyladenosine (m6A)-containing RNAs.
CC {ECO:0000250|UniProtKB:Q9H6S0}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and reach adulthood
CC (PubMed:28809393, PubMed:29087293, PubMed:29033321). However, both male
CC and female mice are infertile; male mice have smaller testes, and
CC female mice have smaller ovaries and show progressive loss of germ
CC cells (PubMed:28809393, PubMed:29087293, PubMed:29033321). Mutant germ
CC cells enter meiosis but proceed prematurely to aberrant metaphase and
CC apoptosis, and display defects in transitioning from spermatogonial to
CC meiotic gene expression programs (PubMed:29087293, PubMed:29033321).
CC Mutant testes reveal an up-regulation of N6-methyladenosine (m6A)-
CC enriched transcripts (PubMed:29033321). {ECO:0000269|PubMed:28809393,
CC ECO:0000269|PubMed:29033321, ECO:0000269|PubMed:29087293,
CC ECO:0000269|PubMed:29360036}.
CC -!- MISCELLANEOUS: 'Ketu' is a harbinger of misfortune in Vedic mythology
CC (PubMed:29360036). {ECO:0000303|PubMed:29360036}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
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DR EMBL; BC138263; AAI38264.1; -; mRNA.
DR EMBL; BC171951; AAI71951.1; -; mRNA.
DR CCDS; CCDS50278.1; -.
DR RefSeq; NP_001156485.1; NM_001163013.1.
DR AlphaFoldDB; B2RR83; -.
DR SMR; B2RR83; -.
DR BioGRID; 232185; 8.
DR IntAct; B2RR83; 4.
DR MINT; B2RR83; -.
DR STRING; 10090.ENSMUSP00000048340; -.
DR iPTMnet; B2RR83; -.
DR PhosphoSitePlus; B2RR83; -.
DR SwissPalm; B2RR83; -.
DR EPD; B2RR83; -.
DR MaxQB; B2RR83; -.
DR PaxDb; 10090-ENSMUSP00000048340; -.
DR PeptideAtlas; B2RR83; -.
DR ProteomicsDB; 275234; -.
DR Pumba; B2RR83; -.
DR Antibodypedia; 48855; 58 antibodies from 16 providers.
DR Ensembl; ENSMUST00000037763.11; ENSMUSP00000048340.8; ENSMUSG00000034653.12.
DR GeneID; 240255; -.
DR KEGG; mmu:240255; -.
DR UCSC; uc008evb.2; mouse.
DR AGR; MGI:2448561; -.
DR CTD; 64848; -.
DR MGI; MGI:2448561; Ythdc2.
DR VEuPathDB; HostDB:ENSMUSG00000034653; -.
DR eggNOG; KOG0920; Eukaryota.
DR eggNOG; KOG0922; Eukaryota.
DR eggNOG; KOG1902; Eukaryota.
DR GeneTree; ENSGT00940000155826; -.
DR HOGENOM; CLU_001832_1_6_1; -.
DR InParanoid; B2RR83; -.
DR OMA; XDYRHSE; -.
DR OrthoDB; 1095660at2759; -.
DR PhylomeDB; B2RR83; -.
DR TreeFam; TF318311; -.
DR BioGRID-ORCS; 240255; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Ythdc2; mouse.
DR PRO; PR:B2RR83; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; B2RR83; Protein.
DR Bgee; ENSMUSG00000034653; Expressed in secondary oocyte and 225 other cell types or tissues.
DR ExpressionAtlas; B2RR83; baseline and differential.
DR Genevisible; B2RR83; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0035770; C:ribonucleoprotein granule; IDA:UniProtKB.
DR GO; GO:0034458; F:3'-5' RNA helicase activity; 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:0008186; F:ATP-dependent activity, acting on RNA; ISO:MGI.
DR GO; GO:0004386; F:helicase activity; IBA:GO_Central.
DR GO; GO:1990247; F:N6-methyladenosine-containing RNA reader activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0070063; F:RNA polymerase binding; ISO:MGI.
DR GO; GO:0051729; P:germline cell cycle switching, mitotic to meiotic cell cycle; IMP:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0048599; P:oocyte development; IMP:UniProtKB.
DR GO; GO:0044829; P:positive regulation by host of viral genome replication; ISO:MGI.
DR GO; GO:0070555; P:response to interleukin-1; ISO:MGI.
DR GO; GO:0034612; P:response to tumor necrosis factor; ISO:MGI.
DR GO; GO:0007286; P:spermatid development; IMP:UniProtKB.
DR CDD; cd17987; DEXHc_YTHDC2; 1.
DR CDD; cd06007; R3H_DEXH_helicase; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR CDD; cd21134; YTH; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.10.590.10; ph1033 like domains; 1.
DR Gene3D; 3.30.1370.50; R3H-like domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR034083; R3H_DEXH_helicase.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR InterPro; IPR007275; YTH_domain.
DR PANTHER; PTHR18934:SF213; 3'-5' RNA HELICASE YTHDC2; 1.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF01424; R3H; 1.
DR Pfam; PF04146; YTH; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00393; R3H; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF82708; R3H domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51061; R3H; 1.
DR PROSITE; PS50882; YTH; 1.
PE 1: Evidence at protein level;
KW ANK repeat; ATP-binding; Cytoplasm; Differentiation; Helicase; Hydrolase;
KW Meiosis; Nucleotide-binding; Oogenesis; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding; Spermatogenesis.
FT CHAIN 1..1445
FT /note="3'-5' RNA helicase YTHDC2"
FT /id="PRO_0000378275"
FT DOMAIN 53..121
FT /note="R3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
FT DOMAIN 218..384
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT REPEAT 521..553
FT /note="ANK 1"
FT REPEAT 554..586
FT /note="ANK 2"
FT DOMAIN 627..799
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1303..1433
FT /note="YTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00225"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 331..334
FT /note="DEAH box"
FT COMPBIAS 1179..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1203..1224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1247..1267
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 BINDING 1309..1311
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /ligand_part="N(6)-methyladenosine 5'-phosphate residue"
FT /ligand_part_id="ChEBI:CHEBI:74449"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5A9"
FT BINDING 1325
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /ligand_part="N(6)-methyladenosine 5'-phosphate residue"
FT /ligand_part_id="ChEBI:CHEBI:74449"
FT /evidence="ECO:0000250|UniProtKB:Q96MU7"
FT BINDING 1375
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /ligand_part="N(6)-methyladenosine 5'-phosphate residue"
FT /ligand_part_id="ChEBI:CHEBI:74449"
FT /evidence="ECO:0000250|UniProtKB:Q96MU7"
FT MOD_RES 1104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 327
FT /note="H->R: In ketu; homozygotes mice are both male- and
FT female-sterile. In the testis, mutant germ cells carry out
FT an abortive attempt at meiosis: They express hallmark
FT meiotic proteins and initiate recombination, but fail to
FT fully extinguish the spermatogonial mitotic division
FT program, proceed prematurely to an aberrant metaphase-like
FT state, and undergo apoptosis. The mutation probably causes
FT misfolding or protein aggregation. Slightly reduced
FT helicase activity."
FT /evidence="ECO:0000269|PubMed:29360036"
SQ SEQUENCE 1445 AA; 161092 MW; A693BF57FEAF7511 CRC64;
MSRPSSVSPR PPAPSGGGTG GGGGGSGGGG GGGGGGPASC GPGGGGRAKG LKDIRIDEEV
KIAVNIALER FRYGDQREME FPSSLTSTER AFIHRLSQSL GLVSKSKGKG ANRYLTVKKK
DGSETAHAMM TCNLTHNTKH AVRSLIQRFP VTNKERTELL PKTERGNVFA VEAENREMSK
TSGRLNNGIP QVPVKRGESE FDSFRQSLPV FEKQEEIVKI IKENKVVLIV GETGSGKTTQ
IPQFLLDDCF KNGIPCRIFC TQPRRLAAIA VAERVAAERR ERIGQTIGYQ IRLESRVSPK
TLLTFCTNGV LLRTLMAGDS TLSTVTHVIV DEVHERDRFS DFLLTKLRDL LQKHPTLKLI
LSSAALDVNL FIRYFGSCPV IYIQGRPFEV KEMFLEDILR TTGYTNKEML KYKKEKQREE
KQQTTLTEWY SAQENTFKPE SQRQRAVASV SEEYDLLDDG GDAVFSQLTE KDVNCLEPWL
IKEMDACLSD IWLHKDVDAF AQVFHLILTE NVSVDYRHSE TSATALMVAA GRGFTSQVEQ
LISMGANVHS KASNGWMALD WAKHFGQTEI VDLLESYSAS LEFGNLDESS LVQTNGNDLS
AEDRELLKAY HHSFDDEKVD LDLIMHLLYN ICHSCDAGAI LIFLPGYDEI VGLRDRILFD
DKRFADNTHR YQVFMLHSNM QTSDQKKVLK NPPAGVRKII LSTNIAETSI TVNDVVFVID
SGKVKEKSFD ALNFVTMLKM VWISKASAIQ RKGRAGRCRP GICFRLFSRL RFQNMLEFQT
PELLRMPLQE LCLHTKLLAP VNCTIADFLM KAPEPPPALI VRNAVQMLKT IDAMDAWEDL
TELGYHLADL PVEPHLGKMV LCAVVLKCLD PILTIACTLA YRDPFVLPTQ ASQKRAAMLC
RKRFTAGTFS DHMALLRAFQ AWQKARSDGW ERAFCEKNFL SQATMEIIIG MRTQLLGQLR
ASGFVRARGG GDIRDVNTNS ENWAVVKAAL VAGMYPNLVH VDRENVILTG PKEKKVRFHP
TSVLSQPQYK KIPPANGQAA AIQALPTDWL IYDEMTRAHR IANIRCCSAV TPVTVLVFCG
PARLASNALQ EPSSFRADGI PNDSSDSEME DRTTANLAAL KLDEWLNFKL EPEAASLLLQ
LRQKWHSLFL RRMRAPSKPW SQVDEATIRA IIAVLSTEEQ SAGLQQPSGI GQRPRPMSSE
ELPLASSWRS NNSRKSTADT EFADGSTTGE RVLMKSPSPA LHPPQKYKDR GILHPKRSTD
DRSDQSSVKS TDSSSYPSPC ASPSPPSSGK GSKSPSPRPN MPIRYFIMKS SNLRNLEISQ
QKGIWSTTPS NERKLNRAFW ESSMVYLVFS VQGSGHFQGF SRMSSEIGRE KSQDWGSAGL
GGVFKVEWIR KESLPFQFAH HLLNPWNDNK KVQISRDGQE LEPQVGEQLL QLWERLPLGE
KTTSD
//
