NRDE2_HUMAN
ID NRDE2_HUMAN Reviewed; 1164 AA.
AC Q9H7Z3; B4DH71; Q4G0A7; Q9NWH6;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Nuclear exosome regulator NRDE2 {ECO:0000305|PubMed:30842217};
DE AltName: Full=Protein NRDE2 homolog {ECO:0000305};
GN Name=NRDE2 {ECO:0000312|HGNC:HGNC:20186};
GN Synonyms=C14orf102 {ECO:0000312|HGNC:HGNC:20186};
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], AND VARIANT SER-1118.
RC TISSUE=Brain, and Embryo;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-1118.
RC TISSUE=Chondrosarcoma;
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 [4]
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MTREX.
RX PubMed=29902117; DOI=10.1080/15476286.2018.1467180;
RA Richard P., Ogami K., Chen Y., Feng S., Moresco J.J., Yates J.R. III,
RA Manley J.L.;
RT "NRDE-2, the human homolog of fission yeast Nrl1, prevents DNA damage
RT accumulation in human cells.";
RL RNA Biol. 15:868-876(2018).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MTREX; EXOSC10; EFTUD2
RP AND EIF4A3.
RX PubMed=30538148; DOI=10.1261/rna.069773.118;
RA Jiao A.L., Perales R., Umbreit N.T., Haswell J.R., Piper M.E., Adams B.D.,
RA Pellman D., Kennedy S., Slack F.J.;
RT "Human nuclear RNAi-defective 2 (NRDE2) is an essential RNA splicing
RT factor.";
RL RNA 25:352-363(2019).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 163-266 IN COMPLEX WITH MTREX,
RP FUNCTION, INTERACTION WITH MTREX, SUBCELLULAR LOCATION, DOMAIN, AND
RP MUTAGENESIS OF PHE-163; ASP-166; TYR-187 AND ARG-189.
RX PubMed=30842217; DOI=10.1101/gad.322602.118;
RA Wang J., Chen J., Wu G., Zhang H., Du X., Chen S., Zhang L., Wang K.,
RA Fan J., Gao S., Wu X., Zhang S., Kuai B., Zhao P., Chi B., Wang L., Li G.,
RA Wong C.C.L., Zhou Y., Li J., Yun C., Cheng H.;
RT "NRDE2 negatively regulates exosome functions by inhibiting MTR4
RT recruitment and exosome interaction.";
RL Genes Dev. 33:536-549(2019).
CC -!- FUNCTION: Protein of the nuclear speckles that regulates RNA
CC degradation and export from the nucleus through its interaction with
CC MTREX an essential factor directing various RNAs to exosomal
CC degradation (PubMed:30842217). Changes the conformation of MTREX,
CC precluding its association with the nuclear exosome and interaction
CC with proteins required for its function in RNA exosomal degradation
CC (PubMed:30842217). Negatively regulates, for instance, the degradation
CC of mRNAs and lncRNAs by inhibiting their MTREX-mediated recruitment to
CC nuclear exosome (PubMed:30842217). By preventing the degradation of
CC RNAs in the nucleus, it promotes their export to the cytoplasm
CC (PubMed:30842217). U5 snRNP-associated RNA splicing factor which is
CC required for efficient splicing of CEP131 pre-mRNA and plays an
CC important role in centrosome maturation, integrity and function during
CC mitosis (PubMed:30538148). Suppresses intron retention in a subset of
CC pre-mRNAs containing short, GC-rich introns with relatively weak 5' and
CC 3' splice sites (PubMed:30538148). Plays a role in DNA damage response
CC (PubMed:29902117). {ECO:0000269|PubMed:29902117,
CC ECO:0000269|PubMed:30538148, ECO:0000269|PubMed:30842217}.
CC -!- SUBUNIT: Interacts with MTREX; the interaction is direct and stabilizes
CC NRDE2 (PubMed:30842217, PubMed:30538148, PubMed:29902117). Interacts
CC with EXOSC10, EFTUD2 and EIF4A3 (PubMed:30538148).
CC {ECO:0000269|PubMed:29902117, ECO:0000269|PubMed:30538148,
CC ECO:0000269|PubMed:30842217}.
CC -!- INTERACTION:
CC Q9H7Z3; P53365: ARFIP2; NbExp=3; IntAct=EBI-1042642, EBI-638194;
CC Q9H7Z3; G5E9W6: CCDC183; NbExp=3; IntAct=EBI-1042642, EBI-17212717;
CC Q9H7Z3; Q9BT25: HAUS8; NbExp=3; IntAct=EBI-1042642, EBI-2558143;
CC Q9H7Z3; Q13352: ITGB3BP; NbExp=3; IntAct=EBI-1042642, EBI-712105;
CC Q9H7Z3; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-1042642, EBI-12039345;
CC Q9H7Z3; Q9NX70: MED29; NbExp=3; IntAct=EBI-1042642, EBI-394656;
CC Q9H7Z3; Q14696: MESD; NbExp=3; IntAct=EBI-1042642, EBI-6165891;
CC Q9H7Z3; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-1042642, EBI-1504830;
CC Q9H7Z3; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-1042642, EBI-742688;
CC Q9H7Z3; Q9BRT2: UQCC2; NbExp=3; IntAct=EBI-1042642, EBI-1054584;
CC Q9H7Z3; Q9UK41-2: VPS28; NbExp=3; IntAct=EBI-1042642, EBI-12146727;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:30538148,
CC ECO:0000269|PubMed:30842217}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:30842217}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:30538148, ECO:0000269|PubMed:30842217}. Nucleus
CC {ECO:0000269|PubMed:29902117}.
CC -!- DOMAIN: The MID/MTR4-interacting domain is necessary and sufficient to
CC mediate interaction with MTREX. {ECO:0000269|PubMed:30842217}.
CC -!- SIMILARITY: Belongs to the NRDE2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14830.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK000870; BAA91404.1; -; mRNA.
DR EMBL; AK024113; BAB14830.1; ALT_INIT; mRNA.
DR EMBL; AK294958; BAG58032.1; -; mRNA.
DR EMBL; AL161662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC098568; AAH98568.1; -; mRNA.
DR CCDS; CCDS9890.1; -.
DR RefSeq; NP_060440.2; NM_017970.3.
DR PDB; 6IEH; X-ray; 2.89 A; A=163-266.
DR PDBsum; 6IEH; -.
DR AlphaFoldDB; Q9H7Z3; -.
DR SMR; Q9H7Z3; -.
DR BioGRID; 120373; 21.
DR IntAct; Q9H7Z3; 14.
DR STRING; 9606.ENSP00000346335; -.
DR iPTMnet; Q9H7Z3; -.
DR MetOSite; Q9H7Z3; -.
DR PhosphoSitePlus; Q9H7Z3; -.
DR BioMuta; NRDE2; -.
DR DMDM; 296439394; -.
DR EPD; Q9H7Z3; -.
DR jPOST; Q9H7Z3; -.
DR MassIVE; Q9H7Z3; -.
DR MaxQB; Q9H7Z3; -.
DR PaxDb; Q9H7Z3; -.
DR PeptideAtlas; Q9H7Z3; -.
DR PRIDE; Q9H7Z3; -.
DR ProteomicsDB; 81161; -.
DR Antibodypedia; 26518; 28 antibodies from 12 providers.
DR DNASU; 55051; -.
DR Ensembl; ENST00000354366.8; ENSP00000346335.3; ENSG00000119720.18.
DR GeneID; 55051; -.
DR KEGG; hsa:55051; -.
DR MANE-Select; ENST00000354366.8; ENSP00000346335.3; NM_017970.4; NP_060440.2.
DR UCSC; uc001xyi.3; human.
DR CTD; 55051; -.
DR DisGeNET; 55051; -.
DR GeneCards; NRDE2; -.
DR HGNC; HGNC:20186; NRDE2.
DR HPA; ENSG00000119720; Low tissue specificity.
DR MIM; 618631; gene.
DR neXtProt; NX_Q9H7Z3; -.
DR OpenTargets; ENSG00000119720; -.
DR PharmGKB; PA134926790; -.
DR VEuPathDB; HostDB:ENSG00000119720; -.
DR eggNOG; KOG1972; Eukaryota.
DR GeneTree; ENSGT00390000005524; -.
DR HOGENOM; CLU_007550_1_0_1; -.
DR InParanoid; Q9H7Z3; -.
DR OMA; VQVEFFE; -.
DR OrthoDB; 833360at2759; -.
DR PhylomeDB; Q9H7Z3; -.
DR TreeFam; TF323791; -.
DR PathwayCommons; Q9H7Z3; -.
DR SignaLink; Q9H7Z3; -.
DR BioGRID-ORCS; 55051; 749 hits in 1083 CRISPR screens.
DR ChiTaRS; NRDE2; human.
DR GenomeRNAi; 55051; -.
DR Pharos; Q9H7Z3; Tdark.
DR PRO; PR:Q9H7Z3; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9H7Z3; protein.
DR Bgee; ENSG00000119720; Expressed in sural nerve and 152 other tissues.
DR ExpressionAtlas; Q9H7Z3; baseline and differential.
DR Genevisible; Q9H7Z3; HS.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:1902369; P:negative regulation of RNA catabolic process; IMP:UniProtKB.
DR GO; GO:0046833; P:positive regulation of RNA export from nucleus; IMP:UniProtKB.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IMP:UniProtKB.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR013633; NRDE-2.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR13471; PTHR13471; 1.
DR Pfam; PF08424; NRDE-2; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division; Coiled coil;
KW DNA damage; Mitosis; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..1164
FT /note="Nuclear exosome regulator NRDE2"
FT /id="PRO_0000089907"
FT REPEAT 305..337
FT /note="HAT 1"
FT REPEAT 395..427
FT /note="HAT 2"
FT REPEAT 758..792
FT /note="HAT 3"
FT REPEAT 978..1010
FT /note="HAT 4"
FT REPEAT 1067..1101
FT /note="HAT 5"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..266
FT /note="MID/MTR4-interacting domain"
FT /evidence="ECO:0000269|PubMed:30842217"
FT REGION 279..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 61..383
FT /evidence="ECO:0000255"
FT COMPBIAS 61..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..103
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT VARIANT 32
FT /note="C -> F (in dbSNP:rs7140914)"
FT /id="VAR_057813"
FT VARIANT 928
FT /note="E -> K (in dbSNP:rs59039343)"
FT /id="VAR_062239"
FT VARIANT 1118
FT /note="N -> S (in dbSNP:rs3737035)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_060343"
FT MUTAGEN 163
FT /note="F->A: Loss of interaction with MTREX associated with
FT decreased RNAs stability; when associated with R-166; A-187
FT and E-189."
FT /evidence="ECO:0000269|PubMed:30842217"
FT MUTAGEN 166
FT /note="D->R: Loss of interaction with MTREX associated with
FT decreased RNAs stability; when associated with A-163; A-187
FT and E-189."
FT /evidence="ECO:0000269|PubMed:30842217"
FT MUTAGEN 187
FT /note="Y->A: Loss of interaction with MTREX associated with
FT decreased RNAs stability; when associated with A-163; R-166
FT and E-189."
FT /evidence="ECO:0000269|PubMed:30842217"
FT MUTAGEN 189
FT /note="R->E: Loss of interaction with MTREX associated with
FT decreased RNAs stability; when associated with A-163; R-166
FT and A-187."
FT /evidence="ECO:0000269|PubMed:30842217"
FT CONFLICT 117
FT /note="E -> G (in Ref. 1; BAA91404)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="R -> G (in Ref. 1; BAA91404)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="D -> G (in Ref. 1; BAB14830)"
FT /evidence="ECO:0000305"
FT HELIX 172..176
FT /evidence="ECO:0007829|PDB:6IEH"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:6IEH"
FT HELIX 218..225
FT /evidence="ECO:0007829|PDB:6IEH"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:6IEH"
SQ SEQUENCE 1164 AA; 132673 MW; 343D0CF623AE2E83 CRC64;
MALFPAFAGL SEAPDGGSSR KELDWLSNPS FCVGSITSLS QQTEAAPAHV SEGLPLTRSH
LKSESSDESD TNKKLKQTSR KKKKEKKKKR KHQHHKKTKR KHGPSSSSRS ETDTDSEKDK
PSRGVGGSKK ESEEPNQGNN AAADTGHRFV WLEDIQAVTG ETFRTDKKPD PANWEYKSLY
RGDIARYKRK GDSCLGINPK KQCISWEGTS TEKKHSRKQV ERYFTKKSVG LMNIDGVAIS
SKTEPPSSEP ISFIPVKDLE DAAPVTTWLN PLGIYDQSTT HWLQGQGPPE QESKQPDAQP
DSESAALKAK VEEFNRRVRE NPRDTQLWMA FVAFQDEVMK SPGLYAIEEG EQEKRKRSLK
LILEKKLAIL ERAIESNQSS VDLKLAKLKL CTEFWEPSTL VKEWQKLIFL HPNNTALWQK
YLLFCQSQFS TFSISKIHSL YGKCLSTLSA VKDGSILSHP ALPGTEEAMF ALFLQQCHFL
RQAGHSEKAI SLFQAMVDFT FFKPDSVKDL PTKGQVEFFE PFWDSGEPRA GEKGARGWKA
WMHQQERGGW VVINPDEDDD EPEEDDQEIK DKTLPRWQIW LAAERSRDQR HWRPWRPDKT
KKQTEEDCED PERQVLFDDI GQSLIRLSSH DLQFQLVEAF LQFLGVPSGF TPPASCLYLA
MDENSIFDNG LYDEKPLTFF NPLFSGASCV GRMDRLGYPR WTRGQNREGE EFIRNVFHLV
MPLFSGKEKS QLCFSWLQYE IAKVIWCLHT KNKKRLKSQG KNCKKLAKNL LKEPENCNNF
CLWKQYAHLE WLLGNTEDAR KVFDTALGMA GSRELKDSDL CELSLLYAEL EVELSPEVRR
AATARAVHIL TKLTESSPYG PYTGQVLAVH ILKARKAYEH ALQDCLGDSC VSNPAPTDSC
SRLISLAKCF MLFQYLTIGI DAAVQIYEQV FAKLNSSVFP EGSGEGDSAS SQSWTSVLEA
ITLMHTSLLR FHMKVSVYPL APLREALSQA LKLYPGNQVL WRSYVQIQNK SHSASKTRRF
FDTITRSAKP LEPWLFAIEA EKLRKRLVET VQRLDGREIH ATIPETGLMH RIQALFENAM
RSDSGSQCPL LWRMYLNFLV SLGNKERSKG VFYKALQNCP WAKVLYLDAV EYFPDEMQEI
LDLMTEKELR VRLPLEELEL LLED
