DDX5_MOUSE
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 03-AUG-2022, entry version 187.
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, Pancreas,
RC 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 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}.
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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 iPTMnet; Q61656; -.
DR PhosphoSitePlus; Q61656; -.
DR SwissPalm; Q61656; -.
DR EPD; Q61656; -.
DR jPOST; Q61656; -.
DR MaxQB; Q61656; -.
DR PaxDb; Q61656; -.
DR PRIDE; Q61656; -.
DR ProteomicsDB; 277972; -.
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; IEA:UniProtKB-SubCell.
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:1903800; P:positive regulation of miRNA maturation; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA: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 Gene3D; 3.40.50.300; -; 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 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; SSF52540; 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
