DBP2_YEAST
ID DBP2_YEAST Reviewed; 546 AA.
AC P24783; D6W169; Q05456;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=ATP-dependent RNA helicase DBP2 {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000269|PubMed:22679025, ECO:0000269|PubMed:23721653};
DE AltName: Full=DEAD box protein 2 {ECO:0000303|PubMed:7641698};
DE AltName: Full=p68-like protein {ECO:0000303|PubMed:1996094};
GN Name=DBP2 {ECO:0000303|PubMed:7641698}; OrderedLocusNames=YNL112W;
GN ORFNames=N1945;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1996094; DOI=10.1128/mcb.11.3.1326-1333.1991;
RA Iggo R.D., Jamieson D.J., McNeill S.A., Southgate J., McPheat J.,
RA Lane D.P.;
RT "p68 RNA helicase: identification of a nucleolar form and cloning of
RT related genes containing a conserved intron in yeasts.";
RL Mol. Cell. Biol. 11:1326-1333(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9090055;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<261::aid-yea64>3.0.co;2-l;
RA de Antoni A., D'Angelo M., Dal Pero F., Sartorello F., Pandolfo D.,
RA Pallavicini A., Lanfranchi G., Valle G.;
RT "The DNA sequence of cosmid 14-13b from chromosome XIV of Saccharomyces
RT cerevisiae reveals an unusually high number of overlapping open reading
RT frames.";
RL Yeast 13:261-266(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
RX PubMed=1869554; DOI=10.1016/s0021-9258(18)98616-3;
RA Dequard-Chablat M., Riva M., Carles C., Sentenac A.;
RT "RPC19, the gene for a subunit common to yeast RNA polymerases A (I) and C
RT (III).";
RL J. Biol. Chem. 266:15300-15307(1991).
RN [6]
RP INDUCTION.
RX PubMed=7641698; DOI=10.1002/j.1460-2075.1995.tb00049.x;
RA Barta I., Iggo R.;
RT "Autoregulation of expression of the yeast Dbp2p 'DEAD-box' protein is
RT mediated by sequences in the conserved DBP2 intron.";
RL EMBO J. 14:3800-3808(1995).
RN [7]
RP FUNCTION, AND INTERACTION WITH UPF1.
RX PubMed=7883168; DOI=10.1101/gad.9.4.437;
RA He F., Jacobson A.;
RT "Identification of a novel component of the nonsense-mediated mRNA decay
RT pathway by use of an interacting protein screen.";
RL Genes Dev. 9:437-454(1995).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH UPF1, AND MUTAGENESIS OF
RP LYS-163; GLU-268; THR-300 AND ARG-447.
RX PubMed=11585918; DOI=10.1128/mcb.21.21.7366-7379.2001;
RA Bond A.T., Mangus D.A., He F., Jacobson A.;
RT "Absence of Dbp2p alters both nonsense-mediated mRNA decay and rRNA
RT processing.";
RL Mol. Cell. Biol. 21:7366-7379(2001).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88 AND SER-90, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88 AND SER-90, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-163 AND GLU-268.
RX PubMed=22679025; DOI=10.1074/jbc.m112.383075;
RA Cloutier S.C., Ma W.K., Nguyen L.T., Tran E.J.;
RT "The DEAD-box RNA helicase Dbp2 connects RNA quality control with
RT repression of aberrant transcription.";
RL J. Biol. Chem. 287:26155-26166(2012).
RN [16]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-474, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [17]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23721653; DOI=10.1016/j.jmb.2013.05.016;
RA Ma W.K., Cloutier S.C., Tran E.J.;
RT "The DEAD-box protein Dbp2 functions with the RNA-binding protein Yra1 to
RT promote mRNP assembly.";
RL J. Mol. Biol. 425:3824-3838(2013).
RN [18]
RP METHYLATION AT ARG-43; ARG-509; ARG-512; ARG-518 AND ARG-525.
RX PubMed=26046779; DOI=10.1002/pmic.201500032;
RA Plank M., Fischer R., Geoghegan V., Charles P.D., Konietzny R., Acuto O.,
RA Pears C., Schofield C.J., Kessler B.M.;
RT "Expanding the yeast protein arginine methylome.";
RL Proteomics 15:3232-3243(2015).
RN [19]
RP METHYLATION AT ARG-18; ARG-43; ARG-509; ARG-512; ARG-518 AND ARG-525.
RX PubMed=33856219; DOI=10.1021/acs.jproteome.0c00927;
RA Hamey J.J., Nguyen A., Wilkins M.R.;
RT "Discovery of arginine methylation, phosphorylation, and their co-
RT occurrence in condensate-associated proteins in Saccharomyces cerevisiae.";
RL J. Proteome Res. 20:2420-2434(2021).
CC -!- FUNCTION: ATP-dependent RNA helicase involved nonsense-mediated mRNA
CC decay and ribosome biogenesis through rRNA processing (PubMed:11585918,
CC PubMed:7883168). Associates directly with chromatin, correlating with
CC transcriptional activity (PubMed:22679025). Required for assembly of
CC mRNA-binding proteins YRA1, NAB2, and MEX67 onto poly(A)+ RNA
CC (PubMed:23721653). {ECO:0000269|PubMed:11585918,
CC ECO:0000269|PubMed:22679025, ECO:0000269|PubMed:23721653,
CC ECO:0000269|PubMed:7883168}.
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:0000269|PubMed:22679025, ECO:0000269|PubMed:23721653};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000269|PubMed:22679025};
CC -!- SUBUNIT: Interacts with UPF1. Associates with polysomes.
CC {ECO:0000269|PubMed:11585918, ECO:0000269|PubMed:7883168}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22679025}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- DISRUPTION PHENOTYPE: Results in defective assembly of nuclear mRNPs.
CC {ECO:0000269|PubMed:23721653}.
CC -!- MISCELLANEOUS: Present with 33100 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: The gene for DBP2 has an unusual intron both because of
CC its size and because of its location near the 3' end of the gene. It
CC may have a function in an intron-mediated negative feedback loop
CC regulating DBP2 expression. {ECO:0000305|PubMed:7641698}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX5/DBP2
CC subfamily. {ECO:0000305}.
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DR EMBL; X52649; CAA36874.1; -; Genomic_DNA.
DR EMBL; Z71388; CAA95991.1; -; Genomic_DNA.
DR EMBL; Z69382; CAA93395.1; -; Genomic_DNA.
DR EMBL; M64991; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006947; DAA10435.1; -; Genomic_DNA.
DR PIR; S13757; S13757.
DR RefSeq; NP_014287.3; NM_001182950.3.
DR AlphaFoldDB; P24783; -.
DR SMR; P24783; -.
DR BioGRID; 35713; 244.
DR DIP; DIP-2438N; -.
DR IntAct; P24783; 42.
DR MINT; P24783; -.
DR STRING; 4932.YNL112W; -.
DR iPTMnet; P24783; -.
DR MaxQB; P24783; -.
DR PaxDb; P24783; -.
DR PRIDE; P24783; -.
DR EnsemblFungi; YNL112W_mRNA; YNL112W; YNL112W.
DR GeneID; 855611; -.
DR KEGG; sce:YNL112W; -.
DR SGD; S000005056; DBP2.
DR VEuPathDB; FungiDB:YNL112W; -.
DR eggNOG; KOG0331; Eukaryota.
DR GeneTree; ENSGT00940000160049; -.
DR HOGENOM; CLU_003041_16_9_1; -.
DR InParanoid; P24783; -.
DR OMA; STMPKFE; -.
DR BioCyc; YEAST:G3O-33136-MON; -.
DR Reactome; R-SCE-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-SCE-9018519; Estrogen-dependent gene expression.
DR PRO; PR:P24783; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P24783; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008186; F:ATP-dependent activity, acting on RNA; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IDA:SGD.
DR GO; GO:0030515; F:snoRNA binding; IDA:SGD.
DR GO; GO:1990120; P:messenger ribonucleoprotein complex assembly; IMP:SGD.
DR GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; IMP:SGD.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IPI:SGD.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IDA:SGD.
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; 1.
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 ATP-binding; Cytoplasm; Helicase; Hydrolase; Isopeptide bond; Methylation;
KW Nonsense-mediated mRNA decay; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing;
KW Ubl conjugation.
FT CHAIN 1..546
FT /note="ATP-dependent RNA helicase DBP2"
FT /id="PRO_0000055000"
FT DOMAIN 144..319
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 347..494
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..530
FT /note="RNA-binding RGG-box"
FT MOTIF 113..141
FT /note="Q motif"
FT MOTIF 267..270
FT /note="DEAD box"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 157..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 18
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 43
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:26046779,
FT ECO:0000269|PubMed:33856219"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 509
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 509
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:26046779,
FT ECO:0000269|PubMed:33856219"
FT MOD_RES 512
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 512
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:26046779,
FT ECO:0000269|PubMed:33856219"
FT MOD_RES 518
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 518
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:26046779,
FT ECO:0000269|PubMed:33856219"
FT MOD_RES 525
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 525
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:26046779,
FT ECO:0000269|PubMed:33856219"
FT CROSSLNK 474
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 163
FT /note="K->N: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:22679025"
FT MUTAGEN 163
FT /note="K->R: Decreases nonsense-mediated mRNA decay."
FT /evidence="ECO:0000269|PubMed:11585918"
FT MUTAGEN 268
FT /note="E->D: Decreases nonsense-mediated mRNA decay."
FT /evidence="ECO:0000269|PubMed:11585918"
FT MUTAGEN 268
FT /note="E->Q: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:22679025"
FT MUTAGEN 300
FT /note="T->A: Decreases nonsense-mediated mRNA decay."
FT /evidence="ECO:0000269|PubMed:11585918"
FT MUTAGEN 447
FT /note="R->K: Decreases nonsense-mediated mRNA decay."
FT /evidence="ECO:0000269|PubMed:11585918"
FT CONFLICT 425
FT /note="D -> GN (in Ref. 2; CAA93395)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 546 AA; 60999 MW; 30FE3D4C7E653120 CRC64;
MTYGGRDQQY NKTNYKSRGG DFRGGRNSDR NSYNDRPQGG NYRGGFGGRS NYNQPQELIK
PNWDEELPKL PTFEKNFYVE HESVRDRSDS EIAQFRKENE MTISGHDIPK PITTFDEAGF
PDYVLNEVKA EGFDKPTGIQ CQGWPMALSG RDMVGIAATG SGKTLSYCLP GIVHINAQPL
LAPGDGPIVL VLAPTRELAV QIQTECSKFG HSSRIRNTCV YGGVPKSQQI RDLSRGSEIV
IATPGRLIDM LEIGKTNLKR VTYLVLDEAD RMLDMGFEPQ IRKIVDQIRP DRQTLMWSAT
WPKEVKQLAA DYLNDPIQVQ VGSLELSASH NITQIVEVVS DFEKRDRLNK YLETASQDNE
YKTLIFASTK RMCDDITKYL REDGWPALAI HGDKDQRERD WVLQEFRNGR SPIMVATDVA
ARGIDVKGIN YVINYDMPGN IEDYVHRIGR TGRAGATGTA ISFFTEQNKG LGAKLISIMR
EANQNIPPEL LKYDRRSYGG GHPRYGGGRG GRGGYGRRGG YGGGRGGYGG NRQRDGGWGN
RGRSNY
