DDX4_MOUSE
ID DDX4_MOUSE Reviewed; 702 AA.
AC Q61496; Q9D5X7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=ATP-dependent RNA helicase DDX4 {ECO:0000305|PubMed:28633017};
DE EC=3.6.4.13 {ECO:0000305|PubMed:28633017};
DE AltName: Full=DEAD box protein 4;
DE AltName: Full=Mvh {ECO:0000303|PubMed:28254886, ECO:0000303|PubMed:7991615};
DE AltName: Full=Vasa homolog {ECO:0000303|PubMed:7991615};
GN Name=Ddx4 {ECO:0000312|MGI:MGI:102670};
GN Synonyms=Mvh {ECO:0000303|PubMed:28254886}, Vasa;
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 STRAIN=C57BL/6J; TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 60-702, AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=7991615; DOI=10.1073/pnas.91.25.12258;
RA Fujiwara Y., Komiya T., Kawabata H., Sato M., Fujimoto H., Furusawa M.,
RA Noce T.;
RT "Isolation of a DEAD-family protein gene that encodes a murine homolog of
RT Drosophila vasa and its specific expression in germ cell lineage.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:12258-12262(1994).
RN [3]
RP INTERACTION WITH PIWIL2.
RX PubMed=14736746; DOI=10.1242/dev.00973;
RA Kuramochi-Miyagawa S., Kimura T., Ijiri T.W., Isobe T., Asada N.,
RA Fujita Y., Ikawa M., Iwai N., Okabe M., Deng W., Lin H., Matsuda Y.,
RA Nakano T.;
RT "Mili, a mammalian member of piwi family gene, is essential for
RT spermatogenesis.";
RL Development 131:839-849(2004).
RN [4]
RP INTERACTION WITH RANBP9.
RC TISSUE=Testis;
RX PubMed=14648869; DOI=10.1002/mrd.20009;
RA Shibata N., Tsunekawa N., Okamoto-Ito S., Akasu R., Tokumasu A., Noce T.;
RT "Mouse RanBPM is a partner gene to a germline specific RNA helicase, mouse
RT vasa homolog protein.";
RL Mol. Reprod. Dev. 67:1-7(2004).
RN [5]
RP INTERACTION WITH MAEL.
RX PubMed=16787967; DOI=10.1093/hmg/ddl158;
RA Costa Y., Speed R.M., Gautier P., Semple C.A., Maratou K., Turner J.M.A.,
RA Cooke H.J.;
RT "Mouse MAELSTROM: the link between meiotic silencing of unsynapsed
RT chromatin and microRNA pathway?";
RL Hum. Mol. Genet. 15:2324-2334(2006).
RN [6]
RP IDENTIFICATION IN A MRNP COMPLEX.
RX PubMed=17141210; DOI=10.1016/j.ydbio.2006.10.046;
RA Hosokawa M., Shoji M., Kitamura K., Tanaka T., Noce T., Chuma S.,
RA Nakatsuji N.;
RT "Tudor-related proteins TDRD1/MTR-1, TDRD6 and TDRD7/TRAP: domain
RT composition, intracellular localization, and function in male germ cells in
RT mice.";
RL Dev. Biol. 301:38-52(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND SER-700, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20439430; DOI=10.1101/gad.1902110;
RA Kuramochi-Miyagawa S., Watanabe T., Gotoh K., Takamatsu K., Chuma S.,
RA Kojima-Kita K., Shiromoto Y., Asada N., Toyoda A., Fujiyama A., Totoki Y.,
RA Shibata T., Kimura T., Nakatsuji N., Noce T., Sasaki H., Nakano T.;
RT "MVH in piRNA processing and gene silencing of retrotransposons.";
RL Genes Dev. 24:887-892(2010).
RN [9]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH CLOCK AND
RP ARNTL/BMAL1.
RX PubMed=22900038; DOI=10.1371/journal.pone.0042695;
RA Peruquetti R.L., de Mateo S., Sassone-Corsi P.;
RT "Circadian proteins CLOCK and BMAL1 in the chromatoid body, a RNA
RT processing granule of male germ cells.";
RL PLoS ONE 7:E42695-E42695(2012).
RN [10]
RP INTERACTION WITH RANBP9 AND RANBP10.
RX PubMed=27622290; DOI=10.1016/j.jmb.2016.09.004;
RA Hong S.K., Kim K.H., Song E.J., Kim E.E.;
RT "Structural Basis for the Interaction between the IUS-SPRY Domain of RanBPM
RT and DDX-4 in Germ Cell Development.";
RL J. Mol. Biol. 428:4330-4344(2016).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-446.
RX PubMed=28633017; DOI=10.1016/j.devcel.2017.05.021;
RA Wenda J.M., Homolka D., Yang Z., Spinelli P., Sachidanandam R.,
RA Pandey R.R., Pillai R.S.;
RT "Distinct roles of RNA helicases MVH and TDRD9 in PIWI slicing-triggered
RT mammalian piRNA biogenesis and function.";
RL Dev. Cell 41:623-637(2017).
RN [12]
RP INTERACTION WITH TEX19.1.
RX PubMed=28254886; DOI=10.1242/jcs.188763;
RA Tarabay Y., Achour M., Teletin M., Ye T., Teissandier A., Mark M.,
RA Bourc'his D., Viville S.;
RT "Tex19 paralogs are new members of the piRNA pathway controlling
RT retrotransposon suppression.";
RL J. Cell Sci. 130:1463-1474(2017).
CC -!- FUNCTION: ATP-dependent RNA helicase required during spermatogenesis to
CC repress transposable elements and preventing their mobilization, which
CC is essential for the germline integrity (PubMed:20439430,
CC PubMed:28633017). Acts via the piRNA metabolic process, which mediates
CC the repression of transposable elements during meiosis by forming
CC complexes composed of piRNAs and Piwi proteins and governs the
CC methylation and subsequent repression of transposons (PubMed:20439430,
CC PubMed:28633017). Involved in the secondary piRNAs metabolic process,
CC the production of piRNAs in fetal male germ cells through a ping-pong
CC amplification cycle (PubMed:20439430, PubMed:28633017). Required for
CC PIWIL2 slicing-triggered piRNA biogenesis: helicase activity enables
CC utilization of one of the slice cleavage fragments generated by PIWIL2
CC and processing these pre-piRNAs into piRNAs (PubMed:28633017).
CC {ECO:0000269|PubMed:20439430, ECO:0000269|PubMed:28633017}.
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:0000305|PubMed:28633017};
CC -!- SUBUNIT: Found in a mRNP complex, at least composed of TDRD1, TDRD6,
CC TDRD7 and DDX4 (PubMed:17141210). Interacts with RANBP9
CC (PubMed:14648869, PubMed:27622290). Interacts with RANBP10
CC (PubMed:27622290). Interacts with PIWIL2 and MAEL (PubMed:14736746,
CC PubMed:16787967). Interacts with ARNTL/BMAL1 and CLOCK
CC (PubMed:22900038). Interacts with Tex19.1 and, probably, Tex19.2
CC (PubMed:28254886). {ECO:0000269|PubMed:14648869,
CC ECO:0000269|PubMed:14736746, ECO:0000269|PubMed:16787967,
CC ECO:0000269|PubMed:17141210, ECO:0000269|PubMed:22900038,
CC ECO:0000269|PubMed:27622290, ECO:0000269|PubMed:28254886}.
CC -!- INTERACTION:
CC Q61496; Q9UPY3-1: DICER1; Xeno; NbExp=3; IntAct=EBI-15569589, EBI-15569571;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20439430,
CC ECO:0000269|PubMed:22900038}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:22900038}. Note=Component of the meiotic nuage,
CC also named P granule, a germ-cell-specific organelle required to
CC repress transposon activity during meiosis.
CC {ECO:0000269|PubMed:20439430}.
CC -!- TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:22900038}.
CC -!- DEVELOPMENTAL STAGE: Expressed in spermatogenic cells from the
CC spermatocyte stage to the round spermatid stage.
CC {ECO:0000269|PubMed:7991615}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable but show male sterility due to
CC defects in spermatogenesis. Retrotransposons are derepressed due to DNA
CC demethylation. Defects are caused by impaired piRNA expression.
CC {ECO:0000269|PubMed:20439430}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX4/VASA
CC subfamily. {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; AK014844; BAB29578.1; -; mRNA.
DR EMBL; D14859; BAA03584.1; -; mRNA.
DR CCDS; CCDS26774.1; -.
DR RefSeq; NP_034159.1; NM_010029.2.
DR PDB; 5JIU; X-ray; 2.05 A; C/D=201-220.
DR PDBsum; 5JIU; -.
DR AlphaFoldDB; Q61496; -.
DR SMR; Q61496; -.
DR BioGRID; 199085; 7.
DR DIP; DIP-61113N; -.
DR IntAct; Q61496; 1.
DR STRING; 10090.ENSMUSP00000096769; -.
DR iPTMnet; Q61496; -.
DR PhosphoSitePlus; Q61496; -.
DR REPRODUCTION-2DPAGE; IPI00121394; -.
DR REPRODUCTION-2DPAGE; Q61496; -.
DR jPOST; Q61496; -.
DR MaxQB; Q61496; -.
DR PaxDb; Q61496; -.
DR PeptideAtlas; Q61496; -.
DR PRIDE; Q61496; -.
DR ProteomicsDB; 279854; -.
DR Antibodypedia; 23442; 391 antibodies from 38 providers.
DR DNASU; 13206; -.
DR Ensembl; ENSMUST00000075748; ENSMUSP00000075157; ENSMUSG00000021758.
DR GeneID; 13206; -.
DR KEGG; mmu:13206; -.
DR UCSC; uc007rwm.2; mouse.
DR CTD; 54514; -.
DR MGI; MGI:102670; Ddx4.
DR VEuPathDB; HostDB:ENSMUSG00000021758; -.
DR eggNOG; KOG0335; Eukaryota.
DR GeneTree; ENSGT00940000157507; -.
DR HOGENOM; CLU_003041_16_3_1; -.
DR InParanoid; Q61496; -.
DR OMA; GDEDWDT; -.
DR OrthoDB; 595675at2759; -.
DR PhylomeDB; Q61496; -.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR BioGRID-ORCS; 13206; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Ddx4; mouse.
DR PRO; PR:Q61496; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q61496; protein.
DR Bgee; ENSMUSG00000021758; Expressed in spermatocyte and 42 other tissues.
DR ExpressionAtlas; Q61496; baseline and differential.
DR Genevisible; Q61496; MM.
DR GO; GO:0033391; C:chromatoid body; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0043186; C:P granule; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0071546; C:pi-body; IDA:UniProtKB.
DR GO; GO:0071547; C:piP-body; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; IMP:UniProtKB.
DR GO; GO:0030317; P:flagellated sperm motility; ISO:MGI.
DR GO; GO:0007276; P:gamete generation; IBA:GO_Central.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0007141; P:male meiosis I; IMP:UniProtKB.
DR GO; GO:0007140; P:male meiotic nuclear division; IMP:UniProtKB.
DR GO; GO:0010529; P:negative regulation of transposition; IMP:UniProtKB.
DR GO; GO:1990511; P:piRNA biosynthetic process; IMP:UniProtKB.
DR GO; GO:0034587; P:piRNA metabolic process; IMP:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
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; 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 SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
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 3D-structure; ATP-binding; Cytoplasm; Developmental protein;
KW Differentiation; Helicase; Hydrolase; Meiosis; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; RNA-mediated gene silencing;
KW Spermatogenesis.
FT CHAIN 1..702
FT /note="ATP-dependent RNA helicase DDX4"
FT /id="PRO_0000054979"
FT DOMAIN 292..475
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 503..648
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 22..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..220
FT /note="Interaction with RANBP9"
FT /evidence="ECO:0000269|PubMed:27622290"
FT REGION 681..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 261..289
FT /note="Q motif"
FT MOTIF 419..422
FT /note="DEAD box"
FT /evidence="ECO:0000269|PubMed:28633017"
FT COMPBIAS 30..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 305..312
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64060"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 446
FT /note="E->Q: In Mvh(KI); heterozygous and homozygous
FT knockin male mice are infertile due to derepression of
FT transposable elements. Defects in piRNA biogenesis. Pre-
FT piRNAs fail to mature into piRNAs."
FT /evidence="ECO:0000269|PubMed:28633017"
FT CONFLICT 152
FT /note="R -> C (in Ref. 2; BAA03584)"
FT /evidence="ECO:0000305"
FT CONFLICT 156..160
FT /note="LFGSR -> FLVLG (in Ref. 2; BAA03584)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="A -> R (in Ref. 2; BAA03584)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="S -> T (in Ref. 2; BAA03584)"
FT /evidence="ECO:0000305"
FT CONFLICT 368..369
FT /note="RA -> IS (in Ref. 2; BAA03584)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="R -> S (in Ref. 2; BAA03584)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="G -> A (in Ref. 2; BAA03584)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="M -> I (in Ref. 2; BAA03584)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="R -> H (in Ref. 2; BAA03584)"
FT /evidence="ECO:0000305"
FT CONFLICT 472
FT /note="S -> N (in Ref. 2; BAA03584)"
FT /evidence="ECO:0000305"
FT CONFLICT 499..509
FT /note="SKREKLVEILR -> QKEKSLLRFYE (in Ref. 2; BAA03584)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="T -> S (in Ref. 2; BAA03584)"
FT /evidence="ECO:0000305"
FT CONFLICT 680..702
FT /note="HTLNTAGISSSQAPNPVDDESWD -> AHVEYSGDFFFTSSQSS (in
FT Ref. 2; BAA03584)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 702 AA; 76470 MW; 5D1E4CC0BDF39748 CRC64;
MGDEDWEAEI LKPHVSSYVP VFEKDKYSSG ANGDTFNRTS ASSDIGESSK KENTSTTGGF
GRGKGFGNRG FLNNKFEEGD SSGFWKESNN DCEDNQTRSR GFSKRGGCQD GNDSEASGPF
RRGGRGSFRG CRGGFGLGRP NSESDQDQGT QRGGGLFGSR KPAASDSGNG DTYQSRSGSG
RGGYKGLNEE VVTGSGKNSW KSETEGGESS DSQGPKVTYI PPPPPEDEDS IFAHYQTGIN
FDKYDTILVE VSGHDAPPAI LTFEEANLCQ TLNNNIAKAG YTKLTPVQKY SIPIVLAGRD
LMACAQTGSG KTAAFLLPIL AHMMRDGITA SRFKELQEPE CIIVAPTREL INQIYLEARK
FSFGTCVRAV VIYGGTQFGH SVRQIVQGCN ILCATPGRLM DIIGKEKIGL KQVKYLVLDE
ADRMLDMGFG PEMKKLISCP GMPSKEQRQT LLFSATFPEE IQRLAGDFLK SSYLFVAVGQ
VGGACRDVQQ TILQVGQYSK REKLVEILRN IGDERTMVFV ETKKKADFIA TFLCQEKIST
TSIHGDREQR EREQALGDFR CGKCPVLVAT SVAARGLDIE NVQHVINFDL PSTIDEYVHR
IGRTGRCGNT GRAISFFDTD SDNHLAQPLV KVLSDAQQDV PAWLEEIAFS TYVPPSFSSS
TRGGAVFASV DTRKNYQGKH TLNTAGISSS QAPNPVDDES WD
