ID DI3L1_HUMAN Reviewed; 1054 AA. AC Q8TF46; Q8N1N8; Q8WTU9; Q96CM7; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 2. DT 27-MAR-2024, entry version 143. DE RecName: Full=DIS3-like exonuclease 1; DE EC=3.1.13.1 {ECO:0000269|PubMed:20531386, ECO:0000269|PubMed:20531389, ECO:0000269|PubMed:37602378}; GN Name=DIS3L; Synonyms=DIS3L1, KIAA1955; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=11853319; DOI=10.1093/dnares/8.6.319; RA Nagase T., Kikuno R., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XXII. The RT complete sequences of 50 new cDNA clones which code for large proteins."; RL DNA Res. 8:319-327(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT GLY-614. RC TISSUE=Tongue; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16572171; DOI=10.1038/nature04601; RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.; RT "Analysis of the DNA sequence and duplication history of human chromosome RT 15."; RL Nature 440:671-675(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT GLY-614. RC TISSUE=Kidney, and Muscle; 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 [6] RP ASSOCIATION WITH THE RNA EXOSOME COMPLEX, IDENTIFICATION BY MASS RP SPECTROMETRY, FUNCTION, COFACTOR, SUBCELLULAR LOCATION, MUTAGENESIS OF RP ASP-486, AND CATALYTIC ACTIVITY. RX PubMed=20531386; DOI=10.1038/emboj.2010.121; RA Tomecki R., Kristiansen M.S., Lykke-Andersen S., Chlebowski A., RA Larsen K.M., Szczesny R.J., Drazkowska K., Pastula A., Andersen J.S., RA Stepien P.P., Dziembowski A., Jensen T.H.; RT "The human core exosome interacts with differentially localized processive RT RNases: hDIS3 and hDIS3L."; RL EMBO J. 29:2342-2357(2010). RN [7] RP FUNCTION, COFACTOR, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-62; ASP-166 RP AND ASP-486, ASSOCIATION WITH THE RNA EXOSOME COMPLEX, AND CATALYTIC RP ACTIVITY. RX PubMed=20531389; DOI=10.1038/emboj.2010.122; RA Staals R.H., Bronkhorst A.W., Schilders G., Slomovic S., Schuster G., RA Heck A.J., Raijmakers R., Pruijn G.J.; RT "Dis3-like 1: a novel exoribonuclease associated with the human exosome."; RL EMBO J. 29:2358-2367(2010). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-989, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [10] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=37602378; DOI=10.1093/nar/gkad673; RA Huntzinger E., Sinteff J., Morlet B., Seraphin B.; RT "HELZ2: a new, interferon-regulated, human 3'-5' exoribonuclease of the RNB RT family is expressed from a non-canonical initiation codon."; RL Nucleic Acids Res. 0:0-0(2023). CC -!- FUNCTION: Catalytic component of the RNA exosome complex which has CC 3'->5' exoribonuclease activity and participates in a multitude of CC cellular RNA processing and degradation events (PubMed:20531386, CC PubMed:20531389, PubMed:37602378). In the cytoplasm, the RNA exosome CC complex is involved in general mRNA turnover and specifically degrades CC inherently unstable mRNAs containing AU-rich elements (AREs) within CC their 3' untranslated regions, and in RNA surveillance pathways, CC preventing translation of aberrant mRNAs. It seems to be involved in CC degradation of histone mRNA (PubMed:20531386, PubMed:20531389). CC {ECO:0000269|PubMed:20531386, ECO:0000269|PubMed:20531389, CC ECO:0000269|PubMed:37602378}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield CC nucleoside 5'-phosphates.; EC=3.1.13.1; CC Evidence={ECO:0000269|PubMed:20531386, ECO:0000269|PubMed:20531389, CC ECO:0000269|PubMed:37602378}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:20531386, ECO:0000269|PubMed:20531389}; CC -!- SUBUNIT: Component of the RNA exosome complex. The catalytically CC inactive RNA exosome core (Exo-9) complex is believed to associate with CC catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and CC nuclear-specific RNA exosome complex forms. CC {ECO:0000269|PubMed:20531386, ECO:0000269|PubMed:20531389}. CC -!- INTERACTION: CC Q8TF46; Q9NQT5: EXOSC3; NbExp=5; IntAct=EBI-3672244, EBI-371866; CC Q8TF46-1; Q13868: EXOSC2; NbExp=2; IntAct=EBI-3895807, EBI-301735; CC Q8TF46-4; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-25933135, EBI-5235340; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20531386, CC ECO:0000269|PubMed:20531389}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q8TF46-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8TF46-2; Sequence=VSP_030366; CC Name=3; CC IsoId=Q8TF46-3; Sequence=VSP_030368, VSP_030369; CC Name=4; CC IsoId=Q8TF46-4; Sequence=VSP_030367; CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB85541.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AB075835; BAB85541.1; ALT_INIT; mRNA. DR EMBL; AK095407; BAC04542.1; -; mRNA. DR EMBL; AC055855; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471082; EAW77759.1; -; Genomic_DNA. DR EMBL; BC014124; AAH14124.2; -; mRNA. DR EMBL; BC022089; AAH22089.1; -; mRNA. DR CCDS; CCDS10214.1; -. [Q8TF46-4] DR CCDS; CCDS45286.1; -. [Q8TF46-1] DR RefSeq; NP_001137160.1; NM_001143688.2. [Q8TF46-1] DR RefSeq; NP_001310865.1; NM_001323936.1. [Q8TF46-4] DR RefSeq; NP_001310867.1; NM_001323938.1. [Q8TF46-2] DR RefSeq; NP_001310868.1; NM_001323939.1. [Q8TF46-2] DR RefSeq; NP_001310870.1; NM_001323941.1. [Q8TF46-2] DR RefSeq; NP_001310874.1; NM_001323945.1. [Q8TF46-4] DR RefSeq; NP_001310875.1; NM_001323946.1. [Q8TF46-2] DR RefSeq; NP_588616.1; NM_133375.4. [Q8TF46-4] DR AlphaFoldDB; Q8TF46; -. DR EMDB; EMD-7818; -. DR EMDB; EMD-7819; -. DR SMR; Q8TF46; -. DR BioGRID; 125453; 49. DR ComplexPortal; CPX-592; Cytoplasmic exosome complex, DIS3L variant. DR ComplexPortal; CPX-600; Cytoplasmic exosome complex, DIS3L-EXOSC10 variant. DR CORUM; Q8TF46; -. DR IntAct; Q8TF46; 29. DR MINT; Q8TF46; -. DR STRING; 9606.ENSP00000321711; -. DR GlyGen; Q8TF46; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8TF46; -. DR PhosphoSitePlus; Q8TF46; -. DR BioMuta; DIS3L; -. DR DMDM; 166201903; -. DR EPD; Q8TF46; -. DR jPOST; Q8TF46; -. DR MassIVE; Q8TF46; -. DR MaxQB; Q8TF46; -. DR PaxDb; 9606-ENSP00000321711; -. DR PeptideAtlas; Q8TF46; -. DR ProteomicsDB; 74555; -. [Q8TF46-1] DR ProteomicsDB; 74556; -. [Q8TF46-2] DR ProteomicsDB; 74557; -. [Q8TF46-3] DR ProteomicsDB; 74558; -. [Q8TF46-4] DR Pumba; Q8TF46; -. DR Antibodypedia; 26111; 161 antibodies from 22 providers. DR DNASU; 115752; -. DR Ensembl; ENST00000319194.9; ENSP00000321583.5; ENSG00000166938.13. [Q8TF46-4] DR Ensembl; ENST00000319212.9; ENSP00000321711.4; ENSG00000166938.13. [Q8TF46-1] DR GeneID; 115752; -. DR KEGG; hsa:115752; -. DR MANE-Select; ENST00000319212.9; ENSP00000321711.4; NM_001143688.3; NP_001137160.1. DR UCSC; uc002app.4; human. [Q8TF46-1] DR AGR; HGNC:28698; -. DR CTD; 115752; -. DR DisGeNET; 115752; -. DR GeneCards; DIS3L; -. DR HGNC; HGNC:28698; DIS3L. DR HPA; ENSG00000166938; Low tissue specificity. DR MIM; 614183; gene. DR neXtProt; NX_Q8TF46; -. DR OpenTargets; ENSG00000166938; -. DR PharmGKB; PA162383675; -. DR VEuPathDB; HostDB:ENSG00000166938; -. DR eggNOG; KOG2102; Eukaryota. DR GeneTree; ENSGT00530000063106; -. DR HOGENOM; CLU_002333_5_0_1; -. DR InParanoid; Q8TF46; -. DR OMA; LPLHEWK; -. DR OrthoDB; 945235at2759; -. DR PhylomeDB; Q8TF46; -. DR TreeFam; TF105755; -. DR PathwayCommons; Q8TF46; -. DR SignaLink; Q8TF46; -. DR SIGNOR; Q8TF46; -. DR BioGRID-ORCS; 115752; 23 hits in 1149 CRISPR screens. DR ChiTaRS; DIS3L; human. DR GeneWiki; DIS3L; -. DR GenomeRNAi; 115752; -. DR Pharos; Q8TF46; Tbio. DR PRO; PR:Q8TF46; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; Q8TF46; Protein. DR Bgee; ENSG00000166938; Expressed in left ventricle myocardium and 188 other cell types or tissues. DR ExpressionAtlas; Q8TF46; baseline and differential. DR GO; GO:0005813; C:centrosome; IDA:HPA. DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IDA:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0008859; F:exoribonuclease II activity; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0006401; P:RNA catabolic process; IDA:ComplexPortal. DR GO; GO:0006396; P:RNA processing; IDA:ComplexPortal. DR GO; GO:0016075; P:rRNA catabolic process; IDA:UniProtKB. DR CDD; cd09862; PIN_Rrp44-like; 1. DR Gene3D; 2.40.50.690; -; 1. DR Gene3D; 2.40.50.700; -; 1. DR Gene3D; 3.40.50.1010; 5'-nuclease; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR InterPro; IPR041505; Dis3_CSD2. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR001900; RNase_II/R. DR InterPro; IPR022966; RNase_II/R_CS. DR InterPro; IPR033771; Rrp44_CSD1. DR InterPro; IPR033770; RRP44_S1. DR PANTHER; PTHR23355:SF30; DIS3-LIKE EXONUCLEASE 1; 1. DR PANTHER; PTHR23355; RIBONUCLEASE; 1. DR Pfam; PF17849; OB_Dis3; 1. DR Pfam; PF00773; RNB; 1. DR Pfam; PF17216; Rrp44_CSD1; 1. DR Pfam; PF17215; Rrp44_S1; 1. DR SMART; SM00955; RNB; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 3. DR PROSITE; PS01175; RIBONUCLEASE_II; 1. DR Genevisible; Q8TF46; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasm; Exonuclease; Exosome; Hydrolase; KW Magnesium; Nuclease; Phosphoprotein; Reference proteome; RNA-binding. FT CHAIN 1..1054 FT /note="DIS3-like exonuclease 1" FT /id="PRO_0000314810" FT MOD_RES 989 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..134 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11853319" FT /id="VSP_030366" FT VAR_SEQ 1..83 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_030367" FT VAR_SEQ 735..750 FT /note="SNKTLADSLDNANDPH -> YSSFEGAEEWSGMLYI (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_030368" FT VAR_SEQ 751..1054 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_030369" FT VARIANT 518 FT /note="I -> V (in dbSNP:rs34668776)" FT /id="VAR_038056" FT VARIANT 614 FT /note="D -> G (in dbSNP:rs3803412)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_038057" FT VARIANT 747 FT /note="N -> S (in dbSNP:rs17258507)" FT /id="VAR_038058" FT MUTAGEN 62 FT /note="D->N: No change of exonuclease activity." FT /evidence="ECO:0000269|PubMed:20531389" FT MUTAGEN 166 FT /note="D->N: No change of exonuclease activity." FT /evidence="ECO:0000269|PubMed:20531389" FT MUTAGEN 486 FT /note="D->N: Complete loss of exonuclease activity." FT /evidence="ECO:0000269|PubMed:20531386, FT ECO:0000269|PubMed:20531389" SQ SEQUENCE 1054 AA; 120787 MW; B57B691CC25F65B8 CRC64; MLQKREKVLL LRTFQGRTLR IVREHYLRPC VPCHSPLCPQ PAACSHDGKL LSSDVTHYVI PDWKVVQDYL EILEFPELKG IIFMQTACQA VQHQRGRRQY NKLRNLLKDA RHDCILFANE FQQCCYLPRE RGESMEKWQT RSIYNAAVWY YHHCQDRMPI VMVTEDEEAI QQYGSETEGV FVITFKNYLD NFWPDLKAAH ELCDSILQSR RERENESQES HGKEYPEHLP LEVLEAGIKS GRYIQGILNV NKHRAQIEAF VRLQGASSKD SDLVSDILIH GMKARNRSIH GDVVVVELLP KNEWKGRTVA LCENDCDDKA SGESPSEPMP TGRVVGILQK NWRDYVVTFP SKEEVQSQGK NAQKILVTPW DYRIPKIRIS TQQAETLQDF RVVVRIDSWE STSVYPNGHF VRVLGRIGDL EGEIATILVE NSISVIPFSE AQMCEMPVNT PESPWKVSPE EEQKRKDLRK SHLVFSIDPK GCEDVDDTLS VRTLNNGNLE LGVHIADVTH FVAPNSYIDI EARTRATTYY LADRRYDMLP SVLSADLCSL LGGVDRYAVS IMWELDKASY EIKKVWYGRT IIRSAYKLFY EAAQELLDGN LSVVDDIPEF KDLDEKSRQA KLEELVWAIG KLTDIARHVR AKRDGCGALE LEGVEVCVQL DDKKNIHDLI PKQPLEVHET VAECMILANH WVAKKIWESF PHQALLRQHP PPHQEFFSEL RECAKAKGFF IDTRSNKTLA DSLDNANDPH DPIVNRLLRS MATQAMSNAL YFSTGSCAEE EFHHYGLALD KYTHFTSPIR RYSDIVVHRL LMAAISKDKK MEIKGNLFSN KDLEELCRHI NNRNQAAQHS QKQSTELFQC MYFKDKDPAT EERCISDGVI YSIRTNGVLL FIPRFGIKGA AYLKNKDGLV ISCGPDSCSE WKPGSLQRFQ NKITSTTTDG ESVTFHLFDH VTVRISIQAS RCHSDTIRLE IISNKPYKIP NTELIHQSSP LLKSELVKEV TKSVEEAQLA QEVKVNIIQE EYQEYRQTKG RSLYTLLEEI RDLALLDVSN NYGI //