HNRPD_MOUSE
ID HNRPD_MOUSE Reviewed; 355 AA.
AC Q60668; Q60667; Q80ZJ0; Q91X94;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 04-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein D0;
DE Short=hnRNP D0;
DE AltName: Full=AU-rich element RNA-binding protein 1;
GN Name=Hnrnpd; Synonyms=Auf1, Hnrpd;
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] OF 1-228 (ISOFORMS 2/4), AND NUCLEOTIDE SEQUENCE
RP [MRNA] OF 25-355 (ISOFORM 3).
RC STRAIN=BALB/cJ; TISSUE=Embryo;
RX PubMed=7959009; DOI=10.1016/0378-1119(94)90168-6;
RA Ehrenman K., Long L., Wagner B.J., Brewer G.;
RT "Characterization of cDNAs encoding the murine A+U-rich RNA-binding protein
RT AUF1.";
RL Gene 149:315-319(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 5-355 (ISOFORM 1).
RC TISSUE=Brain, and Salivary gland;
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 [3]
RP PROTEIN SEQUENCE OF 184-197, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-83; SER-190 AND
RP THR-193, AND 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-243, 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-272; ARG-278; ARG-282 AND
RP ARG-345, METHYLATION [LARGE SCALE ANALYSIS] AT ARG-280 AND ARG-282 (ISOFORM
RP 3), METHYLATION [LARGE SCALE ANALYSIS] AT ARG-261 AND ARG-263 (ISOFORM 4),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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).
CC -!- FUNCTION: Binds with high affinity to RNA molecules that contain AU-
CC rich elements (AREs) found within the 3'-UTR of many proto-oncogenes
CC and cytokine mRNAs. Also binds to double- and single-stranded DNA
CC sequences in a specific manner and functions a transcription factor.
CC Each of the RNA-binding domains specifically can bind solely to a
CC single-stranded non-monotonous 5'-UUAG-3' sequence and also weaker to
CC the single-stranded 5'-TTAGGG-3' telomeric DNA repeat. Binds RNA
CC oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the
CC telomeric single-stranded DNA 5'-TTAGGG-3' repeats. Binding of RRM1 to
CC DNA inhibits the formation of DNA quadruplex structure which may play a
CC role in telomere elongation. May be involved in translationally coupled
CC mRNA turnover. Implicated with other RNA-binding proteins in the
CC cytoplasmic deadenylation/translational and decay interplay of the FOS
CC mRNA mediated by the major coding-region determinant of instability
CC (mCRD) domain. May play a role in the regulation of the rhythmic
CC expression of circadian clock core genes. Directly binds to the 3'UTR
CC of CRY1 mRNA and induces CRY1 rhythmic translation. May also be
CC involved in the regulation of PER2 translation.
CC {ECO:0000250|UniProtKB:Q14103}.
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Part of a complex associated with the
CC FOS mCRD domain and consisting of PABPC1, PAIP1, CSDE1/UNR and SYNCRIP.
CC Interacts with IGF2BP2. Interacts with GTPBP1. Interacts with EIF4G1;
CC the interaction requires RNA. Interacts with EIF3B and RPS3.
CC {ECO:0000250|UniProtKB:Q14103}.
CC -!- INTERACTION:
CC Q60668; P06151: Ldha; NbExp=2; IntAct=EBI-299932, EBI-444940;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q14103}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q14103}. Note=Localized in cytoplasmic mRNP
CC granules containing untranslated mRNAs. Component of ribonucleosomes.
CC Cytoplasmic localization oscillates diurnally.
CC {ECO:0000250|UniProtKB:Q14103}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q60668-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q60668-2; Sequence=VSP_007940;
CC Name=3; Synonyms=muAUF1-3;
CC IsoId=Q60668-3; Sequence=VSP_007941;
CC Name=4;
CC IsoId=Q60668-4; Sequence=VSP_007940, VSP_007941;
CC -!- PTM: Methylated by PRMT1, in an insulin-dependent manner. The PRMT1-
CC mediated methylation regulates its phosphorylation (By similarity).
CC {ECO:0000250|UniProtKB:Q14103}.
CC -!- PTM: Arg-345 is dimethylated, probably to asymmetric dimethylarginine.
CC {ECO:0000250|UniProtKB:Q14103}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA64653.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA64653.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
CC Sequence=AAA64654.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA64654.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
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DR EMBL; U11273; AAA64653.1; ALT_SEQ; mRNA.
DR EMBL; U11274; AAA64654.1; ALT_SEQ; mRNA.
DR EMBL; BC011172; AAH11172.2; -; mRNA.
DR EMBL; BC049098; AAH49098.1; -; mRNA.
DR CCDS; CCDS39180.1; -. [Q60668-2]
DR CCDS; CCDS39181.1; -. [Q60668-3]
DR CCDS; CCDS39182.1; -. [Q60668-1]
DR CCDS; CCDS51571.1; -. [Q60668-4]
DR PIR; I49069; I49069.
DR PIR; I49070; I49070.
DR RefSeq; NP_001070733.1; NM_001077265.2. [Q60668-1]
DR RefSeq; NP_001070734.1; NM_001077266.2.
DR RefSeq; NP_001070735.1; NM_001077267.2.
DR RefSeq; NP_031542.2; NM_007516.3. [Q60668-3]
DR RefSeq; XP_006534798.1; XM_006534735.3. [Q60668-1]
DR AlphaFoldDB; Q60668; -.
DR SMR; Q60668; -.
DR BioGRID; 198279; 51.
DR ComplexPortal; CPX-1078; mCRD-poly(A)-bridging complex.
DR DIP; DIP-31411N; -.
DR IntAct; Q60668; 14.
DR MINT; Q60668; -.
DR STRING; 10090.ENSMUSP00000132735; -.
DR iPTMnet; Q60668; -.
DR PhosphoSitePlus; Q60668; -.
DR SwissPalm; Q60668; -.
DR EPD; Q60668; -.
DR jPOST; Q60668; -.
DR MaxQB; Q60668; -.
DR PaxDb; Q60668; -.
DR PeptideAtlas; Q60668; -.
DR PRIDE; Q60668; -.
DR ProteomicsDB; 269614; -. [Q60668-1]
DR ProteomicsDB; 269615; -. [Q60668-2]
DR ProteomicsDB; 269616; -. [Q60668-3]
DR ProteomicsDB; 269617; -. [Q60668-4]
DR Antibodypedia; 1448; 455 antibodies from 33 providers.
DR DNASU; 11991; -.
DR Ensembl; ENSMUST00000019128; ENSMUSP00000019128; ENSMUSG00000000568. [Q60668-3]
DR Ensembl; ENSMUST00000172361; ENSMUSP00000132735; ENSMUSG00000000568. [Q60668-1]
DR GeneID; 11991; -.
DR KEGG; mmu:11991; -.
DR UCSC; uc008ygt.2; mouse. [Q60668-1]
DR UCSC; uc008ygu.2; mouse. [Q60668-3]
DR CTD; 3184; -.
DR MGI; MGI:101947; Hnrnpd.
DR VEuPathDB; HostDB:ENSMUSG00000000568; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000158010; -.
DR InParanoid; Q60668; -.
DR OMA; GPNQSWN; -.
DR OrthoDB; 1055256at2759; -.
DR PhylomeDB; Q60668; -.
DR TreeFam; TF314808; -.
DR Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR BioGRID-ORCS; 11991; 10 hits in 75 CRISPR screens.
DR ChiTaRS; Hnrnpd; mouse.
DR PRO; PR:Q60668; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q60668; protein.
DR Bgee; ENSMUSG00000000568; Expressed in embryonic post-anal tail and 263 other tissues.
DR ExpressionAtlas; Q60668; baseline and differential.
DR Genevisible; Q60668; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0106002; C:mCRD-mediated mRNA stability complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; ISO:MGI.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0042162; F:telomeric DNA binding; ISS:UniProtKB.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISO:MGI.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
DR GO; GO:0071732; P:cellular response to nitric oxide; ISO:MGI.
DR GO; GO:1904586; P:cellular response to putrescine; ISO:MGI.
DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR GO; GO:0097167; P:circadian regulation of translation; ISS:UniProtKB.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; ISO:MGI.
DR GO; GO:1990828; P:hepatocyte dedifferentiation; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0048255; P:mRNA stabilization; ISO:MGI.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISO:MGI.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:1905663; P:positive regulation of telomerase RNA reverse transcriptase activity; IMP:BHF-UCL.
DR GO; GO:1904355; P:positive regulation of telomere capping; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0043488; P:regulation of mRNA stability; IMP:MGI.
DR GO; GO:0032204; P:regulation of telomere maintenance; IMP:BHF-UCL.
DR GO; GO:0051592; P:response to calcium ion; ISO:MGI.
DR GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
DR GO; GO:1901355; P:response to rapamycin; ISO:MGI.
DR GO; GO:1904383; P:response to sodium phosphate; ISO:MGI.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012956; CARG-binding_factor_N.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF08143; CBFNT; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Biological rhythms; Cytoplasm;
KW Direct protein sequencing; DNA-binding; Isopeptide bond; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein;
KW RNA-binding; Transcription; Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14103"
FT CHAIN 2..355
FT /note="Heterogeneous nuclear ribonucleoprotein D0"
FT /id="PRO_0000081850"
FT DOMAIN 97..179
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 182..261
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q14103"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14103"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14103"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 119
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14103"
FT MOD_RES 127
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14103"
FT MOD_RES 165
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14103"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 193
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 243
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 251
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14103"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14103"
FT MOD_RES 272
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 278
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 280
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q14103"
FT MOD_RES 282
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 345
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 345
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14103"
FT MOD_RES 345
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 72
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14103"
FT CROSSLNK 129
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14103"
FT CROSSLNK 197
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14103"
FT VAR_SEQ 74..92
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_007940"
FT VAR_SEQ 285..334
FT /note="GPSQNWNQGYSNYWNQGYGNYGYNSQGYGGYGGYDYTGYNNYYGYGDYSN
FT -> D (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7959009"
FT /id="VSP_007941"
FT CONFLICT 22..23
FT /note="SA -> G (in Ref. 1; AAA64653)"
FT /evidence="ECO:0000305"
FT CONFLICT 35..38
FT /note="AQGP -> RRA (in Ref. 1; AAA64654)"
FT /evidence="ECO:0000305"
FT CONFLICT 35..37
FT /note="AQG -> RR (in Ref. 1; AAA64653)"
FT /evidence="ECO:0000305"
FT CONFLICT 50..53
FT /note="GSAA -> LCG (in Ref. 1; AAA64654)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="N -> K (in Ref. 1; AAA64654)"
FT /evidence="ECO:0000305"
FT CONFLICT 227..228
FT /note="FI -> ID (in Ref. 1; AAA64653)"
FT /evidence="ECO:0000305"
FT MOD_RES Q60668-3:280
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q60668-3:282
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q60668-4:261
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q60668-4:263
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 355 AA; 38354 MW; 5941DFC6F65B88DF CRC64;
MSEEQFGGDG AAAAATAAVG GSAGEQEGAM VAAAAQGPAA AAGSGSGGGG SAAGGTEGGS
AEAEGAKIDA SKNEEDEGHS NSSPRHTEAA AAQREEWKMF IGGLSWDTTK KDLKDYFSKF
GEVVDCTLKL DPITGRSRGF GFVLFKESES VDKVMDQKEH KLNGKVIDPK RAKAMKTKEP
VKKIFVGGLS PDTPEEKIRE YFGGFGEVES IELPMDNKTN KRRGFCFITF KEEEPVKKIM
EKKYHNVGLS KCEIKVAMSK EQYQQQQQWG SRGGFAGRAR GRGGGPSQNW NQGYSNYWNQ
GYGNYGYNSQ GYGGYGGYDY TGYNNYYGYG DYSNQQSGYG KVSRRGGHQN SYKPY
