ID DDX5_MOUSE Reviewed; 614 AA. AC Q61656; E9Q105; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 24-JAN-2024, entry version 194. DE RecName: Full=Probable ATP-dependent RNA helicase DDX5; DE EC=3.6.4.13; DE AltName: Full=DEAD box RNA helicase DEAD1; DE Short=mDEAD1; DE AltName: Full=DEAD box protein 5; DE AltName: Full=RNA helicase p68; GN Name=Ddx5; Synonyms=Tnz2; 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]. RC STRAIN=C57BL/6J; TISSUE=Testis; RX PubMed=8445986; DOI=10.1016/0024-3205(93)90526-9; RA Lemaire L., Heinlein U.A.O.; RT "High-level expression in male germ cells of murine P68 RNA helicase RT mRNA."; RL Life Sci. 52:917-926(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP FUNCTION. RX PubMed=17011493; DOI=10.1016/j.devcel.2006.08.003; RA Caretti G., Schiltz R.L., Dilworth F.J., Di Padova M., Zhao P., Ogryzko V., RA Fuller-Pace F.V., Hoffman E.P., Tapscott S.J., Sartorelli V.; RT "The RNA helicases p68/p72 and the noncoding RNA SRA are coregulators of RT MyoD and skeletal muscle differentiation."; RL Dev. Cell 11:547-560(2006). RN [4] RP FUNCTION. RX PubMed=17960593; DOI=10.1002/jcb.21526; RA Jensen E.D., Niu L., Caretti G., Nicol S.M., Teplyuk N., Stein G.S., RA Sartorelli V., van Wijnen A.J., Fuller-Pace F.V., Westendorf J.J.; RT "p68 (Ddx5) interacts with Runx2 and regulates osteoblast RT differentiation."; RL J. Cell. Biochem. 103:1438-1451(2008). RN [5] RP INTERACTION WITH NUPR1. RX PubMed=19723804; DOI=10.1242/jcs.048678; RA Sambasivan R., Cheedipudi S., Pasupuleti N., Saleh A., Pavlath G.K., RA Dhawan J.; RT "The small chromatin-binding protein p8 coordinates the association of RT anti-proliferative and pro-myogenic proteins at the myogenin promoter."; RL J. Cell Sci. 122:3481-3491(2009). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC 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 [7] RP INTERACTION WITH BRDT. RX PubMed=22570411; DOI=10.1093/nar/gks342; RA Berkovits B.D., Wang L., Guarnieri P., Wolgemuth D.J.; RT "The testis-specific double bromodomain-containing protein BRDT forms a RT complex with multiple spliceosome components and is required for mRNA RT splicing and 3'-UTR truncation in round spermatids."; RL Nucleic Acids Res. 40:7162-7175(2012). RN [8] RP FUNCTION IN CIRCADIAN RHYTHMS, IDENTIFICATION IN A LARGE PER COMPLEX, AND RP SUBCELLULAR LOCATION. RX PubMed=22767893; DOI=10.1126/science.1221592; RA Padmanabhan K., Robles M.S., Westerling T., Weitz C.J.; RT "Feedback regulation of transcriptional termination by the mammalian RT circadian clock PERIOD complex."; RL Science 337:599-602(2012). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-40 AND LYS-236, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Involved in the alternative regulation of pre-mRNA splicing; CC its RNA helicase activity is necessary for increasing tau exon 10 CC inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre- CC mRNA in the stem-loop region downstream of exon 10. The rate of ATP CC hydrolysis is highly stimulated by single-stranded RNA. Involved in CC transcriptional regulation; the function is independent of the RNA CC helicase activity. Transcriptional coactivator for androgen receptor AR CC but probably not ESR1. Synergizes with DDX17 and SRA1 RNA to activate CC MYOD1 transcriptional activity and involved in skeletal muscle CC differentiation. Transcriptional coactivator for p53/TP53 and involved CC in p53/TP53 transcriptional response to DNA damage and p53/TP53- CC dependent apoptosis. Transcriptional coactivator for RUNX2 and involved CC in regulation of osteoblast differentiation. Acts as a transcriptional CC repressor in a promoter-specific manner; the function probably involves CC association with histone deacetylases, such as HDAC1. As component of a CC large PER complex is involved in the inhibition of 3' transcriptional CC termination of circadian target genes such as PER1 and NR1D1 and the CC control of the circadian rhythms. {ECO:0000269|PubMed:17011493, CC ECO:0000269|PubMed:17960593, ECO:0000269|PubMed:22767893}. 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 -!- SUBUNIT: Identified in the spliceosome C complex. Component of a CC ribonucleoprotein complex containing mRNAs and RNA-binding proteins CC including DDX5, HNRNPH2 and SRSF1 as well as splicing regulator ARVCF CC (By similarity). Interacts with RBM4; the interaction occurs in an RNA- CC independent manner. Interacts with AGO1 and AGO2. Interacts with ESR1, CC AR, EP300, CREBBP, POLR2A, TP53, RUNX2 and HDAC1. Self-associates. CC Interacts with DDX17. Interacts with BRDT. The large PER complex CC involved in the repression of transcriptional termination is composed CC of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active). CC Interacts with DHX36; this interaction occurs in a RNA-dependent manner CC (By similarity). Interacts with NUPR1 (PubMed:19723804). Interacts with CC ERCC6 (By similarity). Interacts with DDX3X in the cytoplasm; this CC interaction may be more efficient when both proteins are CC unphosphorylated (By similarity). {ECO:0000250|UniProtKB:P17844, CC ECO:0000269|PubMed:19723804, ECO:0000269|PubMed:22570411, CC ECO:0000269|PubMed:22767893}. CC -!- INTERACTION: CC Q61656; Q63014: Akap8; Xeno; NbExp=4; IntAct=EBI-643076, EBI-11617845; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P17844}. Nucleus, CC nucleolus {ECO:0000250|UniProtKB:P17844}. Cytoplasm CC {ECO:0000250|UniProtKB:P17844}. Note=During the G0 phase, predominantly CC located in the nucleus. Cytoplasmic levels increase during the G1/S CC phase. During the M phase, located at the vicinity of the condensed CC chromosomes. At G1, localizes in the cytoplasm. CC {ECO:0000250|UniProtKB:P17844}. CC -!- PTM: Sumoylated; sumoylation, promoted by PIAS1, promotes interaction CC with HDAC1 and transcriptional repression activity. Sumoylation also CC significantly increases stability, and reduces polyubiquitination (By CC similarity). {ECO:0000250|UniProtKB:P17844}. CC -!- PTM: Polyubiquitinated, leading to proteasomal degradation. CC {ECO:0000250|UniProtKB:P17844}. CC -!- PTM: Weakly phosphorylated in the G1/S phase of the cell cycle and much CC more at G2/M, especially at Thr and Tyr residues. CC {ECO:0000250|UniProtKB:P17844}. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX5/DBP2 CC subfamily. {ECO:0000305}. CC -!- CAUTION: Silenced gene expression via RNA interference in CC PubMed:17011493 and PubMed:17960593 was simultaneously performed with CC DDX5 and DDX17; siRNA-resistant DDX5 expression was able to rescue the CC effect in muscle differentiation. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X65627; CAA46581.1; -; mRNA. DR EMBL; AL603664; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; I48385; I48385. DR AlphaFoldDB; Q61656; -. DR SMR; Q61656; -. DR CORUM; Q61656; -. DR DIP; DIP-32293N; -. DR IntAct; Q61656; 22. DR MINT; Q61656; -. DR STRING; 10090.ENSMUSP00000021062; -. DR GlyGen; Q61656; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q61656; -. DR PhosphoSitePlus; Q61656; -. DR SwissPalm; Q61656; -. DR EPD; Q61656; -. DR jPOST; Q61656; -. DR MaxQB; Q61656; -. DR PaxDb; 10090-ENSMUSP00000021062; -. DR ProteomicsDB; 277972; -. DR Pumba; Q61656; -. DR AGR; MGI:105037; -. DR MGI; MGI:105037; Ddx5. DR eggNOG; KOG0331; Eukaryota. DR InParanoid; Q61656; -. DR BRENDA; 3.6.4.13; 3474. DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors. DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway. DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression. DR ChiTaRS; Ddx5; mouse. DR PRO; PR:Q61656; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q61656; Protein. DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB. DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI. DR GO; GO:0005516; F:calmodulin binding; ISO:MGI. DR GO; GO:0019899; F:enzyme binding; ISO:MGI. DR GO; GO:0035500; F:MH2 domain binding; ISO:MGI. DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB. DR GO; GO:0050681; F:nuclear androgen receptor binding; ISS:UniProtKB. DR GO; GO:0036002; F:pre-mRNA binding; ISO:MGI. DR GO; GO:0070878; F:primary miRNA binding; ISO:MGI. DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB. DR GO; GO:0070412; F:R-SMAD binding; ISO:MGI. DR GO; GO:0043021; F:ribonucleoprotein complex binding; ISS:UniProtKB. DR GO; GO:0003723; F:RNA binding; IDA:MGI. DR GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB. DR GO; GO:0046332; F:SMAD binding; ISO:MGI. DR GO; GO:0003712; F:transcription coregulator activity; IDA:MGI. DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IMP:UniProtKB. DR GO; GO:0030521; P:androgen receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0030509; P:BMP signaling pathway; ISO:MGI. DR GO; GO:0007623; P:circadian rhythm; IMP:MGI. DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:UniProtKB. DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; ISS:UniProtKB. DR GO; GO:0061614; P:miRNA transcription; IMP:UniProtKB. DR GO; GO:0009299; P:mRNA transcription; ISO:MGI. DR GO; GO:0045445; P:myoblast differentiation; IMP:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; ISS:UniProtKB. DR GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0031053; P:primary miRNA processing; ISO:MGI. DR GO; GO:0006606; P:protein import into nucleus; IGI:MGI. DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0045667; P:regulation of osteoblast differentiation; IMP:UniProtKB. DR GO; GO:2001014; P:regulation of skeletal muscle cell differentiation; IMP:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0045069; P:regulation of viral genome replication; ISO:MGI. DR CDD; cd18049; DEADc_DDX5; 1. DR CDD; cd18787; SF2_C_DEAD; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR012587; P68_rpt. DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS. DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif. DR PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1. DR PANTHER; PTHR47958:SF90; ATP-DEPENDENT RNA HELICASE DDX5-RELATED; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF08061; P68HR; 2. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SMART; SM01414; P68HR; 2. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS51195; Q_MOTIF; 1. PE 1: Evidence at protein level; KW Acetylation; ATP-binding; Biological rhythms; Cytoplasm; Helicase; KW Hydrolase; Isopeptide bond; Methylation; mRNA processing; mRNA splicing; KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW RNA-binding; Spliceosome; Transcription; Transcription regulation; KW Ubl conjugation. FT CHAIN 1..614 FT /note="Probable ATP-dependent RNA helicase DDX5" FT /id="PRO_0000054992" FT DOMAIN 125..300 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 328..475 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT REGION 1..39 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 477..614 FT /note="Transactivation domain" FT /evidence="ECO:0000250" FT REGION 477..504 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 94..122 FT /note="Q motif" FT MOTIF 248..251 FT /note="DEAD box" FT COMPBIAS 1..16 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 114..116 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT BINDING 121 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 138..145 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT MOD_RES 24 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P17844" FT MOD_RES 32 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P17844" FT MOD_RES 33 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P17844" FT MOD_RES 40 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 236 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 297 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P17844" FT MOD_RES 480 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P17844" FT CROSSLNK 32 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P17844" FT CROSSLNK 45 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P17844" FT CROSSLNK 53 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT /evidence="ECO:0000250" FT CROSSLNK 53 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000250|UniProtKB:P17844" FT CROSSLNK 53 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P17844" FT CROSSLNK 340 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P17844" FT CROSSLNK 343 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P17844" FT CROSSLNK 388 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P17844" FT CROSSLNK 391 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P17844" FT CROSSLNK 411 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P17844" FT CROSSLNK 437 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P17844" FT CROSSLNK 451 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P17844" FT CROSSLNK 470 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P17844" FT CROSSLNK 523 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P17844" FT CONFLICT 112 FT /note="Q -> H (in Ref. 1; CAA46581)" FT /evidence="ECO:0000305" FT CONFLICT 159 FT /note="Q -> H (in Ref. 1; CAA46581)" FT /evidence="ECO:0000305" FT CONFLICT 597 FT /note="L -> V (in Ref. 1; CAA46581)" FT /evidence="ECO:0000305" FT CONFLICT 600 FT /note="A -> P (in Ref. 1; CAA46581)" FT /evidence="ECO:0000305" SQ SEQUENCE 614 AA; 69290 MW; A9BBB25D9B7B8819 CRC64; MSSYSSDRDR GRDRGFGAPR FGGSRTGPLS GKKFGNPGEK LVKKKWNLDE LPKFEKNFYQ EHPDLARRTA QEVDTYRRSK EITVRGHNCP KPVLNFYEAN FPANVMDVIA RQNFTEPTAI QAQGWPVALS GLDMVGVAQT GSGKTLSYLL PAIVHINHQP FLERGDGPIC LVLAPTRELA QQVQQVAAEY CRACRLKSTC IYGGAPKGPQ IRDLERGVEI CIATPGRLID FLECGKTNLR RTTYLVLDEA DRMLDMGFEP QIRKIVDQIR PDRQTLMWSA TWPKEVRQLA EDFLKDYIHI NIGALELSAN HNILQIVDVC HDVEKDEKLI RLMEEIMSEK ENKTIVFVET KRRCDELTRK MRRDGWPAMG IHGDKSQQER DWVLNEFKHG KAPILIATDV ASRGLDVEDV KFVINYDYPN SSEDYIHRIG RTARSTKTGT AYTFFTPNNI KQVSDLISVL REANQAINPK LLQLVEDRGS GRSRGRGGMK DDRRDRYSAG KRGGFNTFRD RENYDRGYSN LLKRDFGAKT QNGVYSAANY TNGSFGSNFV SAGIQTSFRT GNPTGTYQNG YDSTQQYGSN VANMHNGMNQ QAYAYPLPQA APMIGYPMPT GYSQ //