PRP8_MOUSE
ID PRP8_MOUSE Reviewed; 2335 AA.
AC Q99PV0; A5D6Q4; Q5ND30; Q5ND31; Q7TQK2; Q8BRZ5; Q8K001;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Pre-mRNA-processing-splicing factor 8;
DE AltName: Full=Splicing factor Prp8;
GN Name=Prpf8; Synonyms=Prp8;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Swiss Webster / NIH; TISSUE=Embryo;
RX PubMed=11275560; DOI=10.1093/oxfordjournals.jbchem.a002896;
RA Takahashi A., Muramatsu H., Takagi S., Fujisawa H., Miyake Y.,
RA Muramatsu T.;
RT "A splicing factor, Prp8: preferential localization in the testis and ovary
RT in adult mice.";
RL J. Biochem. 129:599-606(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, Mammary tumor, and Pancreas;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-772.
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=15169873; DOI=10.1091/mbc.e04-03-0253;
RA Saitoh N., Spahr C.S., Patterson S.D., Bubulya P., Neuwald A.F.,
RA Spector D.L.;
RT "Proteomic analysis of interchromatin granule clusters.";
RL Mol. Biol. Cell 15:3876-3890(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [7]
RP 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).
CC -!- FUNCTION: Plays role in pre-mRNA splicing as core component of
CC precatalytic, catalytic and postcatalytic spliceosomal complexes, both
CC of the predominant U2-type spliceosome and the minor U12-type
CC spliceosome. Functions as a scaffold that mediates the ordered assembly
CC of spliceosomal proteins and snRNAs. Required for the assembly of the
CC U4/U6-U5 tri-snRNP complex, a building block of the spliceosome.
CC Functions as scaffold that positions spliceosomal U2, U5 and U6 snRNAs
CC at splice sites on pre-mRNA substrates, so that splicing can occur.
CC Interacts with both the 5' and the 3' splice site.
CC {ECO:0000250|UniProtKB:Q6P2Q9}.
CC -!- SUBUNIT: Part of the U5 snRNP complex (By similarity). Component of the
CC U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at
CC least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40,
CC DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39 (By similarity).
CC Component of the U5.U4atac/U6atac snRNP complexes in U12-dependent
CC spliceosomes (By similarity). Core component of U2-type precatalytic,
CC catalytic and postcatalytic spliceosomal complexes (By similarity).
CC Found in a mRNA splicing-dependent exon junction complex (EJC) with
CC SRRM1 (By similarity). Interacts with U5 snRNP proteins SNRP116 and
CC SNRNP40 (By similarity). Interacts with EFTUD2 and SNRNP200 (By
CC similarity). Interacts (via the MPN (JAB/Mov34) domain) with PRPF3
CC ('Lys-63'-linked polyubiquitinated); may stabilize the U4/U6-U5 tri-
CC snRNP complex (By similarity). Interacts (via RNase H homology domain)
CC with AAR2 (By similarity). Interacts with RPAP3 and URI1 in a ZNHIT2-
CC dependent manner (By similarity). {ECO:0000250|UniProtKB:Q6P2Q9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6P2Q9}. Nucleus
CC speckle {ECO:0000269|PubMed:15169873}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in testis (preferentially in the
CC outer cell layer), and moderately in ovary (preferentially in granulosa
CC cells). {ECO:0000269|PubMed:11275560}.
CC -!- DEVELOPMENTAL STAGE: During embryogenesis, is highly expressed at day
CC 9.5 of gestation, and its expression decreases progressively during
CC embryogenesis. {ECO:0000269|PubMed:11275560}.
CC -!- DOMAIN: The MPN (JAB/Mov34) domain has structural similarity with
CC deubiquitinating enzymes, but lacks the residues that would bind the
CC catalytic metal ion. {ECO:0000250}.
CC -!- DOMAIN: Contains a region with structural similarity to reverse
CC transcripase, presenting the classical thumb, fingers and palm
CC architecture, but lacks enzyme activity, since the essential metal-
CC binding residues are not conserved. {ECO:0000250}.
CC -!- DOMAIN: Contains a region with structural similarity to type-2
CC restriction endonucleases, but the residues that would bind catalytic
CC metal ions in endonucleases are instead involved in hydrogen bonds that
CC stabilize the protein structure. {ECO:0000250}.
CC -!- DOMAIN: Contains a region with structural similarity to RNase H, but
CC lacks RNase H activity. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH54103.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB047391; BAB32671.1; -; mRNA.
DR EMBL; AL591496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034648; AAH34648.1; -; mRNA.
DR EMBL; BC054103; AAH54103.1; ALT_INIT; mRNA.
DR EMBL; BC093481; AAH93481.1; -; mRNA.
DR EMBL; AK041017; BAC30783.1; -; mRNA.
DR CCDS; CCDS25048.1; -.
DR RefSeq; NP_619600.2; NM_138659.2.
DR AlphaFoldDB; Q99PV0; -.
DR SMR; Q99PV0; -.
DR BioGRID; 228650; 119.
DR IntAct; Q99PV0; 60.
DR MINT; Q99PV0; -.
DR STRING; 10090.ENSMUSP00000018449; -.
DR iPTMnet; Q99PV0; -.
DR PhosphoSitePlus; Q99PV0; -.
DR SwissPalm; Q99PV0; -.
DR EPD; Q99PV0; -.
DR MaxQB; Q99PV0; -.
DR PaxDb; Q99PV0; -.
DR PeptideAtlas; Q99PV0; -.
DR PRIDE; Q99PV0; -.
DR ProteomicsDB; 291795; -.
DR Antibodypedia; 4094; 169 antibodies from 31 providers.
DR DNASU; 192159; -.
DR Ensembl; ENSMUST00000018449; ENSMUSP00000018449; ENSMUSG00000020850.
DR Ensembl; ENSMUST00000102510; ENSMUSP00000099568; ENSMUSG00000020850.
DR GeneID; 192159; -.
DR KEGG; mmu:192159; -.
DR UCSC; uc007kdx.1; mouse.
DR CTD; 10594; -.
DR MGI; MGI:2179381; Prpf8.
DR VEuPathDB; HostDB:ENSMUSG00000020850; -.
DR eggNOG; KOG1795; Eukaryota.
DR GeneTree; ENSGT00390000015210; -.
DR HOGENOM; CLU_000380_3_0_1; -.
DR InParanoid; Q99PV0; -.
DR OMA; VCMRREK; -.
DR OrthoDB; 156083at2759; -.
DR PhylomeDB; Q99PV0; -.
DR TreeFam; TF105613; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72165; mRNA Splicing - Minor Pathway.
DR BioGRID-ORCS; 192159; 30 hits in 75 CRISPR screens.
DR ChiTaRS; Prpf8; mouse.
DR PRO; PR:Q99PV0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q99PV0; protein.
DR Bgee; ENSMUSG00000020850; Expressed in embryonic post-anal tail and 261 other tissues.
DR ExpressionAtlas; Q99PV0; baseline and differential.
DR Genevisible; Q99PV0; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; ISS:UniProtKB.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; ISS:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISO:MGI.
DR GO; GO:0005682; C:U5 snRNP; ISO:MGI.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR GO; GO:0097157; F:pre-mRNA intronic binding; IBA:GO_Central.
DR GO; GO:0030619; F:U1 snRNA binding; IBA:GO_Central.
DR GO; GO:0030620; F:U2 snRNA binding; IBA:GO_Central.
DR GO; GO:0030623; F:U5 snRNA binding; IBA:GO_Central.
DR GO; GO:0017070; F:U6 snRNA binding; IBA:GO_Central.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; ISS:UniProtKB.
DR CDD; cd13838; RNase_H_like_Prp8_IV; 1.
DR Gene3D; 1.20.80.40; -; 1.
DR Gene3D; 3.30.420.230; -; 1.
DR Gene3D; 3.30.43.40; -; 1.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR012591; PRO8NT.
DR InterPro; IPR012592; PROCN.
DR InterPro; IPR012984; PROCT.
DR InterPro; IPR027652; PRP8.
DR InterPro; IPR021983; PRP8_domainIV.
DR InterPro; IPR043173; Prp8_domainIV_fingers.
DR InterPro; IPR043172; Prp8_domainIV_palm.
DR InterPro; IPR019581; Prp8_U5-snRNA-bd.
DR InterPro; IPR042516; Prp8_U5-snRNA-bd_sf.
DR InterPro; IPR019580; Prp8_U6-snRNA-bd.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR019582; RRM_spliceosomal_PrP8.
DR PANTHER; PTHR11140; PTHR11140; 1.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF08082; PRO8NT; 1.
DR Pfam; PF08083; PROCN; 1.
DR Pfam; PF08084; PROCT; 1.
DR Pfam; PF12134; PRP8_domainIV; 1.
DR Pfam; PF10598; RRM_4; 1.
DR Pfam; PF10597; U5_2-snRNA_bdg; 1.
DR Pfam; PF10596; U6-snRNA_bdg; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR SUPFAM; SSF53098; SSF53098; 2.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Methylation; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; RNA-binding;
KW Spliceosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q6P2Q9"
FT CHAIN 2..2335
FT /note="Pre-mRNA-processing-splicing factor 8"
FT /id="PRO_0000097041"
FT DOMAIN 2103..2234
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 812..1303
FT /note="Reverse transcriptase homology domain"
FT REGION 1304..1577
FT /note="Linker"
FT REGION 1513..1526
FT /note="Important for branch point selection"
FT /evidence="ECO:0000250"
FT REGION 1581..1752
FT /note="Restriction endonuclease homology domain"
FT REGION 1669..2034
FT /note="Involved in interaction with pre-mRNA 5' splice
FT site"
FT /evidence="ECO:0000250"
FT REGION 1767..2020
FT /note="RNase H homology domain"
FT REGION 2301..2335
FT /note="Required for interaction with EFTUD2 and SNRNP200"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2Q9"
FT MOD_RES 859
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2Q9"
FT MOD_RES 1358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2Q9"
FT MOD_RES 1425
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2Q9"
FT MOD_RES 1463
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2Q9"
FT CONFLICT 797
FT /note="D -> V (in Ref. 1; BAB32671)"
FT /evidence="ECO:0000305"
FT CONFLICT 2191..2195
FT /note="QDVTT -> THASA (in Ref. 3; AAH54103)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2335 AA; 273616 MW; C1A7A989B1AFB3B7 CRC64;
MAGVFPYRGP GNPVPGPLAP LPDYMSEEKL QEKARKWQQL QAKRYAEKRK FGFVDAQKED
MPPEHVRKII RDHGDMTNRK FRHDKRVYLG ALKYMPHAVL KLLENMPMPW EQIRDVPVLY
HITGAISFVN EIPWVIEPVY ISQWGSMWIM MRREKRDRRH FKRMRFPPFD DEEPPLDYAD
NILDVEPLEA IQLELDPEED APVLDWFYDH QPLRDSRKYV NGSTYQRWQF TLPMMSTLYR
LANQLLTDLV DDNYFYLFDL KAFFTSKALN MAIPGGPKFE PLVRDINLQD EDWNEFNDIN
KIIIRQPIRT EYKIAFPYLY NNLPHHVHLT WYHTPNVVFI KTEDPDLPAF YFDPLINPIS
HRHSVKSQEP LPDDDEEFEL PEFVEPFLKD TPLYTDNTAN GIALLWAPRP FNLRSGRTRR
ALDIPLVKNW YREHCPAGQP VKVRVSYQKL LKYYVLNALK HRPPKAQKKR YLFRSFKATK
FFQSTKLDWV EVGLQVCRQG YNMLNLLIHR KNLNYLHLDY NFNLKPVKTL TTKERKKSRF
GNAFHLCREV LRLTKLVVDS HVQYRLGNVD AFQLADGLQY IFAHVGQLTG MYRYKYKLMR
QIRMCKDLKH LIYYRFNTGP VGKGPGCGFW AAGWRVWLFF MRGITPLLER WLGNLLARQF
EGRHSKGVAK TVTKQRVESH FDLELRAAVM HDILDMMPEG IKQNKARTIL QHLSEAWRCW
KANIPWKVPG LPTPIENMIL RYVKAKADWW TNTAHYNRER IRRGATVDKT VCKKNLGRLT
RLYLKAEQER QHNYLKDGPY ITAEEAVAVY TTTVHWLESR RFSPIPFPPL SYKHDTKLLI
LALERLKEAY SVKSRLNQSQ REELGLIEQA YDNPHEALSR IKRHLLTQRA FKEVGIEFMD
LYSHLVPVYD VEPLEKITDA YLDQYLWYEA DKRRLFPPWI KPADTEPPPL LVYKWCQGIN
NLQDVWETSE GECNVMLESR FEKMYEKIDL TLLNRLLRLI VDHNIADYMT AKNNVVINYK
DMNHTNSYGI IRGLQFASFI VQYYGLVMDL LVLGLHRASE MAGPPQMPND FLSFQDIATE
AAHPIRLFCR YIDRIHIFFR FTADEARDLI QRYLTEHPDP NNENIVGYNN KKCWPRDARM
RLMKHDVNLG RAVFWDIKNR LPRSVTTVQW ENSFVSVYSK DNPNLLFNMC GFECRILPKC
RTSYEEFTHK DGVWNLQNEV TKERTAQCFL RVDDESMQRF HNRVRQILMA SGSTTFTKIV
NKWNTALIGL MTYFREAVVN TQELLDLLVK CENKIQTRIK IGLNSKMPSR FPPVVFYTPK
ELGGLGMLSM GHVLIPQSDL RWSKQTDVGI THFRSGMSHE EDQLIPNLYR YIQPWESEFI
DSQRVWAEYA LKRQEAIAQN RRLTLEDLED SWDRGIPRIN TLFQKDRHTL AYDKGWRVRT
DFKQYQVLKQ NPFWWTHQRH DGKLWNLNNY RTDMIQALGG VEGILEHTLF KGTYFPTWEG
LFWEKASGFE ESMKWKKLTN AQRSGLNQIP NRRFTLWWSP TINRANVYVG FQVQLDLTGI
FMHGKIPTLK ISLIQIFRAH LWQKIHESIV MDLCQVFDQE LDALEIETVQ KETIHPRKSY
KMNSSCADIL LFASYKWNVS RPSLLADSKD VMDSTTTQKY WIDIQLRWGD YDSHDIERYA
RAKFLDYTTD NMSIYPSPTG VLIAIDLAYN LHSAYGNWFP GSKPLIQQAM AKIMKANPAL
YVLRERIRKG LQLYSSEPTE PYLSSQNYGE LFSNQIIWFV DDTNVYRVTI HKTFEGNLTT
KPINGAIFIF NPRTGQLFLK IIHTSVWAGQ KRLGQLAKWK TAEEVAALIR SLPVEEQPKQ
IIVTRKGMLD PLEVHLLDFP NIVIKGSELQ LPFQACLKVE KFGDLILKAT EPQMVLFNLY
DDWLKTISSY TAFSRLILIL RALHVNNDRA KVILKPDKTT VTEPHHIWPT LTDEEWIKVE
VQLKDLILAD YGKKNNVNVA SLTQSEIRDI ILGMEISAPS QQRQQIAEIE KQTKEQSQLT
ATQTRTVNKH GDEIITSTTS NYETQTFSSK TEWRVRAISA ANLHLRTNHI YVSSDDIKET
GYTYILPKNV LKKFICISDL RAQIAGYLYG VSPPDNPQVK EIRCIVMVPQ WGTHQTVHLP
SQLPQHEYLK EMEPLGWIHT QPNESPQLSP QDVTTHAKIM ADNPSWDGEK TIIITCSFTP
GSCTLTAYKL TPSGYEWGRQ NTDKGNNPKG YLPSHYERVQ MLLSDRFLGF FMVPAQSSWN
YNFMGVRHDP NMKYELQLAN PKEFYHEVHR PSHFLNFALL QEGEVYSADR EDLYA
