EWS_MOUSE
ID EWS_MOUSE Reviewed; 655 AA.
AC Q61545; Q9D2P0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=RNA-binding protein EWS;
GN Name=Ewsr1; Synonyms=Ews, Ewsh;
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 TISSUE=Testis;
RX PubMed=7829090; DOI=10.1006/geno.1994.1495;
RA Plougastel B., Mattei M.-G., Thomas G., Delattre O.;
RT "Cloning and chromosome localization of the mouse Ews gene.";
RL Genomics 23:278-281(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Placenta;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-438, AND IDENTIFICATION BY MASS
RP 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).
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-470; ARG-485; ARG-502; ARG-505
RP AND ARG-614, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [8]
RP INTERACTION WITH PRDM9; REC8; SYCP3 AND SYCP1.
RX PubMed=27932493; DOI=10.1091/mbc.e16-09-0686;
RA Parvanov E.D., Tian H., Billings T., Saxl R.L., Spruce C., Aithal R.,
RA Krejci L., Paigen K., Petkov P.M.;
RT "PRDM9 interactions with other proteins provide a link between
RT recombination hotspots and the chromosomal axis in meiosis.";
RL Mol. Biol. Cell 28:488-499(2017).
CC -!- FUNCTION: Might function as a transcriptional repressor. {ECO:0000250}.
CC -!- SUBUNIT: Binds RNA, POLR2C, SF1 and calmodulin. Interacts with PTK2B
CC and TDRD3 (By similarity). Forms a complex with REC8, PRDM9, SYCP3 and
CC SYCP1; complex formation is dependent of phosphorylated form of REC8
CC and requires PRDM9 bound to hotspot DNA; EWSR1 joins PRDM9 with the
CC chromosomal axis through REC8 (PubMed:27932493). {ECO:0000250,
CC ECO:0000269|PubMed:27932493}.
CC -!- INTERACTION:
CC Q61545; P20263: Pou5f1; NbExp=13; IntAct=EBI-1606991, EBI-1606219;
CC Q61545; Q64012: Raly; NbExp=2; IntAct=EBI-1606991, EBI-6878379;
CC Q61545; Q8C7B8: Zswim4; NbExp=2; IntAct=EBI-1606991, EBI-26673088;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cell membrane {ECO:0000250}. Note=Relocates from cytoplasm to ribosomes
CC upon PTK2B/FAK2 activation. {ECO:0000250}.
CC -!- PTM: Phosphorylated; calmodulin-binding inhibits phosphorylation of
CC Ser-266. {ECO:0000250}.
CC -!- PTM: Highly methylated on arginine residues. Methylation is mediated by
CC PRMT1 and, at lower level by PRMT8 (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Binds calmodulin in the presence, but not in the
CC absence, of calcium ion. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRM TET family. {ECO:0000305}.
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DR EMBL; X79233; CAA55815.1; -; mRNA.
DR EMBL; AK019460; BAB31732.1; -; mRNA.
DR EMBL; AK151625; BAE30560.1; -; mRNA.
DR EMBL; AL645845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466574; EDL40519.1; -; Genomic_DNA.
DR CCDS; CCDS24396.1; -.
DR PIR; A55726; A55726.
DR RefSeq; NP_031994.2; NM_007968.3.
DR AlphaFoldDB; Q61545; -.
DR BMRB; Q61545; -.
DR SMR; Q61545; -.
DR BioGRID; 199551; 123.
DR IntAct; Q61545; 70.
DR MINT; Q61545; -.
DR STRING; 10090.ENSMUSP00000078867; -.
DR iPTMnet; Q61545; -.
DR PhosphoSitePlus; Q61545; -.
DR SwissPalm; Q61545; -.
DR EPD; Q61545; -.
DR jPOST; Q61545; -.
DR MaxQB; Q61545; -.
DR PaxDb; Q61545; -.
DR PRIDE; Q61545; -.
DR ProteomicsDB; 271509; -.
DR Antibodypedia; 3786; 577 antibodies from 41 providers.
DR DNASU; 14030; -.
DR Ensembl; ENSMUST00000079949; ENSMUSP00000078867; ENSMUSG00000009079.
DR GeneID; 14030; -.
DR KEGG; mmu:14030; -.
DR UCSC; uc007hvw.2; mouse.
DR CTD; 2130; -.
DR MGI; MGI:99960; Ewsr1.
DR VEuPathDB; HostDB:ENSMUSG00000009079; -.
DR eggNOG; KOG1995; Eukaryota.
DR GeneTree; ENSGT00940000154191; -.
DR InParanoid; Q61545; -.
DR OrthoDB; 1539664at2759; -.
DR TreeFam; TF322599; -.
DR BioGRID-ORCS; 14030; 15 hits in 76 CRISPR screens.
DR ChiTaRS; Ewsr1; mouse.
DR PRO; PR:Q61545; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q61545; protein.
DR Bgee; ENSMUSG00000009079; Expressed in yolk sac and 253 other tissues.
DR ExpressionAtlas; Q61545; baseline and differential.
DR Genevisible; Q61545; MM.
DR GO; GO:0015030; C:Cajal body; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR CDD; cd12533; RRM_EWS; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR034869; EWS_RRM.
DR InterPro; IPR033109; EWSR1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034870; TET_fam.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR23238; PTHR23238; 1.
DR PANTHER; PTHR23238:SF3; PTHR23238:SF3; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Calmodulin-binding; Cell membrane; Cytoplasm; Membrane;
KW Metal-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; RNA-binding; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..655
FT /note="RNA-binding protein EWS"
FT /id="PRO_0000081587"
FT REPEAT 8..16
FT /note="1"
FT REPEAT 17..27
FT /note="2"
FT REPEAT 28..34
FT /note="3"
FT REPEAT 35..42
FT /note="4"
FT REPEAT 43..50
FT /note="5"
FT REPEAT 51..59
FT /note="6"
FT REPEAT 60..68
FT /note="7"
FT REPEAT 69..75
FT /note="8"
FT REPEAT 76..84
FT /note="9"
FT REPEAT 85..91
FT /note="10"
FT REPEAT 92..110
FT /note="11"
FT REPEAT 111..116
FT /note="12"
FT REPEAT 117..125
FT /note="13"
FT REPEAT 126..156
FT /note="14"
FT REPEAT 157..163
FT /note="15"
FT REPEAT 164..170
FT /note="16"
FT REPEAT 171..177
FT /note="17"
FT REPEAT 178..188
FT /note="18"
FT REPEAT 189..193
FT /note="19"
FT REPEAT 194..201
FT /note="20"
FT REPEAT 202..206
FT /note="21"
FT REPEAT 207..212
FT /note="22"
FT REPEAT 213..218
FT /note="23"
FT REPEAT 219..224
FT /note="24"
FT REPEAT 225..230
FT /note="25"
FT REPEAT 231..238
FT /note="26"
FT REPEAT 239..245
FT /note="27"
FT REPEAT 246..252
FT /note="28"
FT REPEAT 253..259
FT /note="29"
FT DOMAIN 256..285
FT /note="IQ"
FT REPEAT 260..276
FT /note="30"
FT REPEAT 277..285
FT /note="31"
FT DOMAIN 360..446
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 517..548
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 1..285
FT /note="EAD (Gln/Pro/Thr-rich)"
FT REGION 8..285
FT /note="31 X approximate tandem repeats"
FT REGION 121..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 638..655
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 121..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..194
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..475
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..561
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 266
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250"
FT MOD_RES 300
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 302
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 304
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 309
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 314
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 317
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 321
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 438
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 454
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 463
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 470
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 470
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 485
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 489
FT /note="Asymmetric dimethylarginine; by PRMT8"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 493
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 499
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 502
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 505
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 505
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 562
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 564
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 571
FT /note="Asymmetric dimethylarginine; alternate; by PRMT8"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 571
FT /note="Omega-N-methylarginine; alternate; by PRMT8"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 574
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 580
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 588
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 591
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 595
FT /note="Asymmetric dimethylarginine; alternate; by PRMT8"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 595
FT /note="Omega-N-methylarginine; alternate; by PRMT8"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 599
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 602
FT /note="Asymmetric dimethylarginine; by PRMT8"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 606
FT /note="Asymmetric dimethylarginine; alternate; by PRMT8"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 606
FT /note="Omega-N-methylarginine; alternate; by PRMT8"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 614
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 614
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 632
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT MOD_RES 635
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q01844"
FT CONFLICT 97
FT /note="T -> A (in Ref. 1; CAA55815)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="T -> S (in Ref. 1; CAA55815)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 655 AA; 68462 MW; 10C7F06A921668F3 CRC64;
MASTDYSTYS QAAAQQGYSA YTAQPTQGYA QTTQAYGQQS YGTYGQPTDV SYTQAQTTAT
YGQTAYATSY GQPPTGYSTP TAPQAYSQPV QGYGTGTYDS TTATVTTTQA SYAAQTAYGT
QPAYPTYGQQ PTATAPTRPQ DGNKPAETSQ PQSSTGGYNQ PSLGYGQSNY SYPQVPGSYP
MQPVTAPPSY PPTSYSSSQP TSYDQSSYSQ QNTYGQPSSY GQQSSYGQQS SYGQQPPTSY
PPQTGSYSQA PSQYSQQSSS YGQQSSFRQD HPSSMGVYGQ ESGGFSGPGE NRSLSGPDNR
GRGRGGFDRG GMSRGGRGGG RGGLGAGERG GFNKPGGPMD EGPDLDLGLP IDPDEDSDNS
AIYVQGLNDN VTLDDLADFF KQCGVVKMNK RTGQPMIHIY LDKETGKPKG DATVSYEDPP
TAKAAVEWFD GKDFQGSKLK VSLARKKPPM NSMRGGMPPR EGRGMPPPLR GGPGGPGGPG
GPMGRMGGRG GDRGGFPPRG PRGSRGNPSG GGNVQHRAGD WQCPNPGCGN QNFAWRTECN
QCKAPKPEGF LPPPFPPPGG DRGRGGPGGM RGGRGGLMDR GGPGGMFRGG RGGDRGGFRG
GRGMDRGGFG GGRRGGPGGP PGPLMEQMGG RRGGRGGPGK MDKGEHRQER RDRPY
