XRN2_YEAST
ID XRN2_YEAST Reviewed; 1006 AA.
AC Q02792; D6W2B4;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=5'-3' exoribonuclease 2;
DE EC=3.1.13.-;
DE AltName: Full=Ribonucleic acid-trafficking protein 1;
DE AltName: Full=p116;
GN Name=RAT1; Synonyms=HKE1, TAP1; OrderedLocusNames=YOR048C;
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=1628825; DOI=10.1101/gad.6.7.1173;
RA Amberg D.C., Goldstein A.L., Cole C.N.;
RT "Isolation and characterization of RAT1: an essential gene of Saccharomyces
RT cerevisiae required for the efficient nucleocytoplasmic trafficking of
RT mRNA.";
RL Genes Dev. 6:1173-1189(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COFACTOR, AND SUBCELLULAR
RP LOCATION.
RX PubMed=8417335; DOI=10.1128/mcb.13.1.341-350.1993;
RA Kenna M., Stevens A., McCammon M., Douglas M.G.;
RT "An essential yeast gene with homology to the exonuclease-encoding
RT XRN1/KEM1 gene also encodes a protein with exoribonuclease activity.";
RL Mol. Cell. Biol. 13:341-350(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8497260; DOI=10.1128/mcb.13.6.3434-3444.1993;
RA Aldrich T.L., di Segni G., McConaughy B.L., Keen N.J., Whelen S.,
RA Hall B.D.;
RT "Structure of the yeast TAP1 protein: dependence of transcription
RT activation on the DNA context of the target gene.";
RL Mol. Cell. Biol. 13:3434-3444(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 929-1006.
RC STRAIN=BJ1991;
RX PubMed=8497275; DOI=10.1128/mcb.13.6.3650-3659.1993;
RA Ganster R.W., Shen W., Schmidt M.C.;
RT "Isolation of STD1, a high-copy-number suppressor of a dominant negative
RT mutation in the yeast TATA-binding protein.";
RL Mol. Cell. Biol. 13:3650-3659(1993).
RN [7]
RP PROTEIN SEQUENCE OF 2-9, FUNCTION, COFACTOR, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=7608167; DOI=10.1074/jbc.270.27.16063;
RA Stevens A., Poole T.L.;
RT "5'-exonuclease-2 of Saccharomyces cerevisiae. Purification and features of
RT ribonuclease activity with comparison to 5'-exonuclease-1.";
RL J. Biol. Chem. 270:16063-16069(1995).
RN [8]
RP FUNCTION.
RX PubMed=9207242; DOI=10.1006/bbrc.1997.6877;
RA Poole T.L., Stevens A.;
RT "Structural modifications of RNA influence the 5' exoribonucleolytic
RT hydrolysis by XRN1 and HKE1 of Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 235:799-805(1997).
RN [9]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=9384595; DOI=10.1093/emboj/16.23.7184;
RA Dichtl B., Stevens A., Tollervey D.;
RT "Lithium toxicity in yeast is due to the inhibition of RNA processing
RT enzymes.";
RL EMBO J. 16:7184-7195(1997).
RN [10]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-518; LEU-520; LYS-534; LYS-535
RP AND LYS-537.
RX PubMed=9315672; DOI=10.1128/mcb.17.10.6122;
RA Johnson A.W.;
RT "Rat1p and Xrn1p are functionally interchangeable exoribonucleases that are
RT restricted to and required in the nucleus and cytoplasm, respectively.";
RL Mol. Cell. Biol. 17:6122-6130(1997).
RN [11]
RP FUNCTION.
RX PubMed=9488433; DOI=10.1128/mcb.18.3.1181;
RA Petfalski E., Dandekar T., Henry Y., Tollervey D.;
RT "Processing of the precursors to small nucleolar RNAs and rRNAs requires
RT common components.";
RL Mol. Cell. Biol. 18:1181-1189(1998).
RN [12]
RP FUNCTION.
RX PubMed=9584178; DOI=10.1128/mcb.18.6.3376;
RA Villa T., Ceradini F., Presutti C., Bozzoni I.;
RT "Processing of the intron-encoded U18 small nucleolar RNA in the yeast
RT Saccharomyces cerevisiae relies on both exo- and endonucleolytic
RT activities.";
RL Mol. Cell. Biol. 18:3376-3383(1998).
RN [13]
RP FUNCTION.
RX PubMed=9891049; DOI=10.1128/mcb.19.2.1144;
RA Qu L.-H., Henras A., Lu Y.-J., Zhou H., Zhou W.-X., Zhu Y.-Q., Zhao J.,
RA Henry Y., Caizergues-Ferrer M., Bachellerie J.-P.;
RT "Seven novel methylation guide small nucleolar RNAs are processed from a
RT common polycistronic transcript by Rat1p and RNase III in yeast.";
RL Mol. Cell. Biol. 19:1144-1158(1999).
RN [14]
RP FUNCTION.
RX PubMed=11030620; DOI=10.1016/s0092-8674(00)00065-9;
RA Bousquet-Antonelli C., Presutti C., Tollervey D.;
RT "Identification of a regulated pathway for nuclear pre-mRNA turnover.";
RL Cell 102:765-775(2000).
RN [15]
RP FUNCTION, AND INTERACTION WITH RAI1.
RX PubMed=10805743; DOI=10.1128/mcb.20.11.4006-4015.2000;
RA Xue Y., Bai X., Lee I., Kallstrom G., Ho J., Brown J., Stevens A.,
RA Johnson A.W.;
RT "Saccharomyces cerevisiae RAI1 (YGL246c) is homologous to human DOM3Z and
RT encodes a protein that binds the nuclear exoribonuclease Rat1p.";
RL Mol. Cell. Biol. 20:4006-4015(2000).
RN [16]
RP FUNCTION.
RX PubMed=11142370; DOI=10.1017/s1355838200001540;
RA Geerlings T.H., Vos J.C., Raue H.A.;
RT "The final step in the formation of 25S rRNA in Saccharomyces cerevisiae is
RT performed by 5'->3' exonucleases.";
RL RNA 6:1698-1703(2000).
RN [17]
RP FUNCTION.
RX PubMed=11238889; DOI=10.1128/mcb.21.5.1515-1530.2001;
RA He F., Jacobson A.;
RT "Upf1p, Nmd2p, and Upf3p regulate the decapping and exonucleolytic
RT degradation of both nonsense-containing mRNAs and wild-type mRNAs.";
RL Mol. Cell. Biol. 21:1515-1530(2001).
RN [18]
RP FUNCTION.
RX PubMed=12769851; DOI=10.1016/s1097-2765(03)00137-0;
RA Danin-Kreiselman M., Lee C.Y., Chanfreau G.;
RT "RNase III-mediated degradation of unspliced pre-mRNAs and lariat
RT introns.";
RL Mol. Cell 11:1279-1289(2003).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RAI1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12612077; DOI=10.1128/mcb.23.6.2042-2054.2003;
RA Sydorskyy Y., Dilworth D.J., Yi E.C., Goodlett D.R., Wozniak R.W.,
RA Aitchison J.D.;
RT "Intersection of the Kap123p-mediated nuclear import and ribosome export
RT pathways.";
RL Mol. Cell. Biol. 23:2042-2054(2003).
RN [20]
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 [21]
RP FUNCTION.
RX PubMed=14561886; DOI=10.1261/rna.5126203;
RA Lee C.Y., Lee A., Chanfreau G.;
RT "The roles of endonucleolytic cleavage and exonucleolytic digestion in the
RT 5'-end processing of S. cerevisiae box C/D snoRNAs.";
RL RNA 9:1362-1370(2003).
RN [22]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX
RP WITH RTT103, AND MUTAGENESIS OF ASP-235.
RX PubMed=15565157; DOI=10.1038/nature03041;
RA Kim M., Krogan N.J., Vasiljeva L., Rando O.J., Nedea E., Greenblatt J.F.,
RA Buratowski S.;
RT "The yeast Rat1 exonuclease promotes transcription termination by RNA
RT polymerase II.";
RL Nature 432:517-522(2004).
RN [23]
RP ERRATUM OF PUBMED:15565157.
RA Kim M., Krogan N.J., Vasiljeva L., Rando O.J., Nedea E., Greenblatt J.F.,
RA Buratowski S.;
RL Nature 433:661-661(2005).
RN [24]
RP FUNCTION.
RX PubMed=16131592; DOI=10.1261/rna.2900205;
RA Fang F., Phillips S., Butler J.S.;
RT "Rat1p and Rai1p function with the nuclear exosome in the processing and
RT degradation of rRNA precursors.";
RL RNA 11:1571-1578(2005).
RN [25]
RP FUNCTION.
RX PubMed=16598041; DOI=10.1101/gad.1409106;
RA Luo W., Johnson A.W., Bentley D.L.;
RT "The role of Rat1 in coupling mRNA 3'-end processing to transcription
RT termination: implications for a unified allosteric-torpedo model.";
RL Genes Dev. 20:954-965(2006).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-574, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Possesses 5'->3' exoribonuclease activity. Required for the
CC processing of nuclear mRNA, rRNA and small nucleolar RNA (snoRNA)
CC precursors. May promote termination of transcription by RNA polymerase
CC II via the recruitment of 3'-end processing factors to the poly(A) site
CC and by the degradation of nascent RNA downstream of the poly(A) site.
CC {ECO:0000269|PubMed:10805743, ECO:0000269|PubMed:11030620,
CC ECO:0000269|PubMed:11142370, ECO:0000269|PubMed:11238889,
CC ECO:0000269|PubMed:12769851, ECO:0000269|PubMed:14561886,
CC ECO:0000269|PubMed:15565157, ECO:0000269|PubMed:16131592,
CC ECO:0000269|PubMed:16598041, ECO:0000269|PubMed:7608167,
CC ECO:0000269|PubMed:8417335, ECO:0000269|PubMed:9207242,
CC ECO:0000269|PubMed:9384595, ECO:0000269|PubMed:9488433,
CC ECO:0000269|PubMed:9584178, ECO:0000269|PubMed:9891049}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:7608167, ECO:0000269|PubMed:8417335};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:7608167, ECO:0000269|PubMed:8417335};
CC -!- ACTIVITY REGULATION: Inhibited by nucleoside 3', 5'-bisphosphates.
CC {ECO:0000269|PubMed:9384595}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0-8.8. {ECO:0000269|PubMed:7608167};
CC -!- SUBUNIT: Interacts with RAI1 and RTT103. {ECO:0000269|PubMed:10805743,
CC ECO:0000269|PubMed:12612077, ECO:0000269|PubMed:15565157}.
CC -!- INTERACTION:
CC Q02792; P53063: RAI1; NbExp=4; IntAct=EBI-14845, EBI-24206;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12612077,
CC ECO:0000269|PubMed:8417335, ECO:0000269|PubMed:9315672}.
CC -!- MISCELLANEOUS: Present with 623 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the 5'-3' exonuclease family. XRN2/RAT1
CC subfamily. {ECO:0000305}.
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DR EMBL; M95626; AAA34960.1; -; Genomic_DNA.
DR EMBL; Z11746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S61567; AAB26818.1; -; Genomic_DNA.
DR EMBL; Z74956; CAA99240.1; -; Genomic_DNA.
DR EMBL; L06011; AAA16950.1; -; Unassigned_DNA.
DR EMBL; BK006948; DAA10830.1; -; Genomic_DNA.
DR PIR; S20126; S20126.
DR RefSeq; NP_014691.1; NM_001183467.1.
DR AlphaFoldDB; Q02792; -.
DR SMR; Q02792; -.
DR BioGRID; 34449; 526.
DR ComplexPortal; CPX-1332; RAT1-RAI1 RNA polymerase II termination complex.
DR DIP; DIP-6692N; -.
DR IntAct; Q02792; 4.
DR MINT; Q02792; -.
DR STRING; 4932.YOR048C; -.
DR iPTMnet; Q02792; -.
DR MaxQB; Q02792; -.
DR PaxDb; Q02792; -.
DR PRIDE; Q02792; -.
DR EnsemblFungi; YOR048C_mRNA; YOR048C; YOR048C.
DR GeneID; 854213; -.
DR KEGG; sce:YOR048C; -.
DR SGD; S000005574; RAT1.
DR VEuPathDB; FungiDB:YOR048C; -.
DR eggNOG; KOG2044; Eukaryota.
DR GeneTree; ENSGT00670000098098; -.
DR HOGENOM; CLU_006038_1_1_1; -.
DR OMA; CLHYYVH; -.
DR BioCyc; YEAST:G3O-33592-MON; -.
DR BRENDA; 3.1.13.B1; 984.
DR PRO; PR:Q02792; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q02792; protein.
DR GO; GO:0090730; C:Las1 complex; IPI:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0110103; C:RNA polymerase II termination complex; IPI:ComplexPortal.
DR GO; GO:0004534; F:5'-3' exoribonuclease activity; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IDA:GO_Central.
DR GO; GO:0000448; P:cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IDA:SGD.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:1901408; P:negative regulation of phosphorylation of RNA polymerase II C-terminal domain; IMP:SGD.
DR GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0071028; P:nuclear mRNA surveillance; IMP:SGD.
DR GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IMP:SGD.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IBA:GO_Central.
DR GO; GO:1904595; P:positive regulation of termination of RNA polymerase II transcription; IDA:ComplexPortal.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR GO; GO:0043144; P:sno(s)RNA processing; IMP:SGD.
DR GO; GO:0030847; P:termination of RNA polymerase II transcription, exosome-dependent; IMP:SGD.
DR GO; GO:0030846; P:termination of RNA polymerase II transcription, poly(A)-coupled; IMP:SGD.
DR InterPro; IPR027073; 5_3_exoribonuclease.
DR InterPro; IPR004859; Put_53exo.
DR InterPro; IPR041412; Xrn1_helical.
DR InterPro; IPR017151; Xrn2/3/4.
DR PANTHER; PTHR12341; PTHR12341; 1.
DR Pfam; PF17846; XRN_M; 2.
DR Pfam; PF03159; XRN_N; 1.
DR PIRSF; PIRSF037239; Exonuclease_Xrn2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Direct protein sequencing; Exonuclease; Hydrolase;
KW mRNA processing; Nuclease; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; rRNA processing; Transcription; Transcription regulation;
KW Transcription termination.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7608167"
FT CHAIN 2..1006
FT /note="5'-3' exoribonuclease 2"
FT /id="PRO_0000071399"
FT REPEAT 955..958
FT /note="1-1"
FT REPEAT 961..964
FT /note="2-1"
FT REPEAT 972..974
FT /note="2-2"
FT REPEAT 975..978
FT /note="3-1"
FT REPEAT 984..986
FT /note="3-2"
FT REPEAT 996..999
FT /note="1-2"
FT REGION 492..529
FT /note="Required for retention in the nucleus"
FT REGION 561..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..999
FT /note="2 X 4 AA repeats of S-R-Y-D, N-N-N-Y, Y-S-G-N"
FT COILED 256..287
FT /evidence="ECO:0000255"
FT COILED 453..544
FT /evidence="ECO:0000255"
FT COMPBIAS 939..997
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 235
FT /note="D->A: Abrogates exonuclease activity and impairs
FT termination of transcription by RNA polymerase II."
FT /evidence="ECO:0000269|PubMed:15565157"
FT MUTAGEN 518
FT /note="H->Y: Causes mislocalization to the cytoplasm and
FT suppresses the requirement for XRN1 function."
FT /evidence="ECO:0000269|PubMed:9315672"
FT MUTAGEN 520
FT /note="L->P: Suppresses the requirement for XRN1 function."
FT /evidence="ECO:0000269|PubMed:9315672"
FT MUTAGEN 534
FT /note="K->A: Causes mislocalization to the cytoplasm; when
FT associated with A-535 and A-537."
FT /evidence="ECO:0000269|PubMed:9315672"
FT MUTAGEN 535
FT /note="K->A: Causes mislocalization to the cytoplasm; when
FT associated with A-534 and A-537."
FT /evidence="ECO:0000269|PubMed:9315672"
FT MUTAGEN 535
FT /note="K->N: Causes mislocalization to the cytoplasm and
FT suppresses the requirement for XRN1 function."
FT /evidence="ECO:0000269|PubMed:9315672"
FT MUTAGEN 537
FT /note="K->A: Causes mislocalization to the cytoplasm; when
FT associated with A-534 and A-535."
FT /evidence="ECO:0000269|PubMed:9315672"
FT MUTAGEN 537
FT /note="K->E: Causes mislocalization to the cytoplasm and
FT suppresses the requirement for XRN1 function."
FT /evidence="ECO:0000269|PubMed:9315672"
FT MUTAGEN 683
FT /note="Y->H: In allele TAP1-1; activates transcription of
FT the promoter-defective yeast SUP4 tRNA(Tyr) allele
FT SUP4A53T61."
SQ SEQUENCE 1006 AA; 115934 MW; 5DDD5B0245F3E12A CRC64;
MGVPSFFRWL SRKYPKIISP VLEEQPQIVD GVILPLDYSA SNPNGELDNL YLDMNGIVHP
CSHPENKPPP ETEDEMLLAV FEYTNRVLNM ARPRKVLVMA VDGVAPRAKM NQQRARRFRS
ARDAQIENEA REEIMRQREE VGEIIDDAVR NKKTWDSNAI TPGTPFMDKL AAALRYWTAF
KLATDPGWKN LQVIISDATV PGEGEHKIMN FIRSQRADPE YNPNTTHCIY GLDADLIFLG
LATHEPHFKI LREDVFAQDN RKRNNLKDTI NMTEEEKQFL QKQNSEQPFL WLHINVLREY
LSAELWVPGL PFTFDLERAI DDWVFMCFFC GNDFLPHLPC LDVRENSIDI LLDIWKVVLP
KLKTYMTCDG VLNLPSVETL LQHLGSREGD IFKTRHIQEA RKKEAFERRK AQKNMSKGQD
RHPTVATEQL QMYDTQGNLA KGSWNLTTSD MVRLKKELML ANEGNEEAIA KVKQQSDKNN
ELMKDISKEE IDDAVSKANK TNFNLAEVMK QKIINKKHRL EKDNEEEEIA KDSKKVKTEK
AESECDLDAE IKDEIVADVN DRENSETTEV SRDSPVHSTV NVSEGPKNGV FDTDEFVKLF
EPGYHERYYT AKFHVTPQDI EQLRKDMVKC YIEGVAWVLM YYYQGCASWN WFYPYHYAPL
ATDFHGFSHL EIKFEEGTPF LPYEQLMSVL PAASGHALPK IFRSLMSEPD SEIIDFYPEE
FPIDMNGKKM SWQGIALLPF IDQDRLLTAV RAQYPLLSDA ERARNIRGEP VLLISNKNAN
YERFSKKLYS KENNNNNVVV KFQHFKSGLS GIVSKDVEGF ELNGKIVCPI QGGSLPNLST
TLILKMSYRL IPLPSRNKSI ILNGFIPSEP VLTAYDLDSI MYKYNNQNYS RRWNFGNDLK
QNIVPVGPKG ITQYKPRTGG YRAFFYFAEL SRNNVQPAHN YGRNSYNSQP GFNNSRYDGG
NNNYRQNSNY RNNNYSGNRN SGQYSGNSYS RNNKQSRYDN SRANRR
