ID   U520_MOUSE              Reviewed;        2136 AA.
AC   Q6P4T2; Q69ZZ3;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 168.
DE   RecName: Full=U5 small nuclear ribonucleoprotein 200 kDa helicase;
DE            EC=3.6.4.13 {ECO:0000250|UniProtKB:O75643};
DE   AltName: Full=BRR2 homolog;
DE   AltName: Full=U5 snRNP-specific 200 kDa protein;
DE            Short=U5-200KD;
GN   Name=Snrnp200; Synonyms=Kiaa0788;
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 [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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 228-2136.
RC   TISSUE=Embryonic tail;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1765, AND IDENTIFICATION BY
RP   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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT   chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225; THR-2131; SER-2133 AND
RP   SER-2135, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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: Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices,
CC       an essential step in the assembly of a catalytically active
CC       spliceosome. Plays a role in pre-mRNA splicing as core component of
CC       precatalytic, catalytic and postcatalytic spliceosomal complexes. As a
CC       component of the minor spliceosome, involved in the splicing of U12-
CC       type introns in pre-mRNAs (By similarity). Involved in spliceosome
CC       assembly, activation and disassembly. Mediates changes in the dynamic
CC       network of RNA-RNA interactions in the spliceosome.
CC       {ECO:0000250|UniProtKB:O75643}.
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:0000250|UniProtKB:O75643};
CC   -!- SUBUNIT: Component of a core complex containing at least PRPF8,
CC       SNRNP200, EFTUD2 and SNRNP40. Component of the U5 snRNP and U4/U6-U5
CC       tri-snRNP complexes, building blocks of the spliceosome. Component of
CC       the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and
CC       at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40,
CC       DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39. Component of
CC       precatalytic, catalytic and postcatalytic spliceosomal complexes.
CC       Component of the minor spliceosome, which splices U12-type introns (By
CC       similarity). Interacts with C9orf78; the interaction is direct and
CC       mutually exclusive with its interaction with WBP4. Interacts with WBP4;
CC       the interaction is mutually exclusive with its interaction with
CC       C9orf78. Interacts with PRPF8. Interacts with TSSC4; the interaction is
CC       direct, excludes recruitment of C9ORF78 and WBP4 to SNRNP200 and
CC       negatively regulates its RNA helicase activity (By similarity).
CC       {ECO:0000250|UniProtKB:O75643}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75643}.
CC   -!- DOMAIN: Contains two helicase domains. The N-terminal helicase domain
CC       has catalytic activity by itself, contrary to C-terminal helicase
CC       domain that may have a regulatory role and enhance the activity of the
CC       first helicase domain. {ECO:0000250|UniProtKB:O75643}.
CC   -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AL845368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC063261; AAH63261.1; -; mRNA.
DR   EMBL; AK173025; BAD32303.1; -; mRNA.
DR   CCDS; CCDS16695.1; -.
DR   RefSeq; NP_796188.2; NM_177214.4.
DR   AlphaFoldDB; Q6P4T2; -.
DR   SMR; Q6P4T2; -.
DR   BioGRID; 236173; 66.
DR   IntAct; Q6P4T2; 8.
DR   MINT; Q6P4T2; -.
DR   STRING; 10090.ENSMUSP00000099509; -.
DR   GlyGen; Q6P4T2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6P4T2; -.
DR   PhosphoSitePlus; Q6P4T2; -.
DR   SwissPalm; Q6P4T2; -.
DR   EPD; Q6P4T2; -.
DR   jPOST; Q6P4T2; -.
DR   MaxQB; Q6P4T2; -.
DR   PaxDb; 10090-ENSMUSP00000099509; -.
DR   PeptideAtlas; Q6P4T2; -.
DR   ProteomicsDB; 298056; -.
DR   Pumba; Q6P4T2; -.
DR   Antibodypedia; 32425; 105 antibodies from 20 providers.
DR   DNASU; 320632; -.
DR   Ensembl; ENSMUST00000103220.4; ENSMUSP00000099509.4; ENSMUSG00000003660.11.
DR   GeneID; 320632; -.
DR   KEGG; mmu:320632; -.
DR   UCSC; uc008mez.1; mouse.
DR   AGR; MGI:2444401; -.
DR   CTD; 23020; -.
DR   MGI; MGI:2444401; Snrnp200.
DR   VEuPathDB; HostDB:ENSMUSG00000003660; -.
DR   eggNOG; KOG0951; Eukaryota.
DR   GeneTree; ENSGT00940000154966; -.
DR   HOGENOM; CLU_000335_2_1_1; -.
DR   InParanoid; Q6P4T2; -.
DR   OMA; QTEIQYY; -.
DR   OrthoDB; 57056at2759; -.
DR   PhylomeDB; Q6P4T2; -.
DR   TreeFam; TF300056; -.
DR   Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-MMU-72165; mRNA Splicing - Minor Pathway.
DR   BioGRID-ORCS; 320632; 27 hits in 75 CRISPR screens.
DR   ChiTaRS; Snrnp200; mouse.
DR   PRO; PR:Q6P4T2; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q6P4T2; Protein.
DR   Bgee; ENSMUSG00000003660; Expressed in manus and 223 other cell types or tissues.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005681; C:spliceosomal complex; ISO:MGI.
DR   GO; GO:0071006; C:U2-type catalytic step 1 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0004386; F:helicase activity; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0000388; P:spliceosome conformational change to release U4 (or U4atac) and U1 (or U11); ISO:MGI.
DR   CDD; cd18019; DEXHc_Brr2_1; 1.
DR   CDD; cd18021; DEXHc_Brr2_2; 1.
DR   CDD; cd18795; SF2_C_Ski2; 2.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR   Gene3D; 2.60.40.150; C2 domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR   Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR   InterPro; IPR041094; Brr2_helicase_PWI.
DR   InterPro; IPR048863; BRR2_plug.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004179; Sec63-dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR   PANTHER; PTHR47961:SF4; U5 SMALL NUCLEAR RIBONUCLEOPROTEIN HELICASE; 1.
DR   Pfam; PF21188; BRR2_plug; 1.
DR   Pfam; PF00270; DEAD; 2.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF18149; Helicase_PWI; 1.
DR   Pfam; PF02889; Sec63; 2.
DR   PIRSF; PIRSF039073; BRR2; 1.
DR   SMART; SM00487; DEXDc; 2.
DR   SMART; SM00490; HELICc; 2.
DR   SMART; SM00973; Sec63; 2.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR   SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR   PROSITE; PS51194; HELICASE_CTER; 2.
DR   Genevisible; Q6P4T2; MM.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Coiled coil; Helicase; Hydrolase;
KW   Isopeptide bond; mRNA processing; mRNA splicing; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein;
KW   Spliceosome; Ubl conjugation.
FT   CHAIN           1..2136
FT                   /note="U5 small nuclear ribonucleoprotein 200 kDa helicase"
FT                   /id="PRO_0000422049"
FT   DOMAIN          490..673
FT                   /note="Helicase ATP-binding 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          684..921
FT                   /note="Helicase C-terminal 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          982..1286
FT                   /note="SEC63 1"
FT   DOMAIN          1337..1512
FT                   /note="Helicase ATP-binding 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1545..1753
FT                   /note="Helicase C-terminal 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          1812..2124
FT                   /note="SEC63 2"
FT   REGION          39..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          395..2129
FT                   /note="Interaction with C9orf78 and WBP4"
FT                   /evidence="ECO:0000250|UniProtKB:O75643"
FT   REGION          1282..2136
FT                   /note="Interaction with TSSC4"
FT                   /evidence="ECO:0000250|UniProtKB:O75643"
FT   COILED          54..84
FT                   /evidence="ECO:0000255"
FT   MOTIF           615..618
FT                   /note="DEAH box"
FT   MOTIF           1454..1457
FT                   /note="DEAH box"
FT   COMPBIAS        51..81
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         503..510
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   BINDING         1350..1357
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75643"
FT   MOD_RES         26
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75643"
FT   MOD_RES         225
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT   MOD_RES         389
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O75643"
FT   MOD_RES         709
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:F1LNJ2"
FT   MOD_RES         971
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O75643"
FT   MOD_RES         1428
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O75643"
FT   MOD_RES         1765
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17525332"
FT   MOD_RES         2002
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75643"
FT   MOD_RES         2131
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         2133
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         2135
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CROSSLNK        46
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O75643"
FT   CROSSLNK        944
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        971
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        1071
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        1199
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        2091
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   2136 AA;  244547 MW;  BBDD6058CA635519 CRC64;
     MADVTARSLQ YEYKANSNLV LQADRSLIDR TRRDEPTGEV LSLVGKLEGT RMGDKAQRTK
     PQMQEERRAK RRKRDEDRHD MNKMKGYTLL SEGIDEMVGI IYKPKTKETR ETYEVLLSFI
     QAALGDQPRD ILCGAADEVL AVLKNEKLRD KERRREIDLL LGQTDDTRYH VLVNLGKKIT
     DYGGDKEIQN MDDNIDETYG VNVQFESDEE EGDEDVYGEV REEASDDDME GDEAVVRCTL
     SANLVASGEL MSSKKKDLHP RDIDAFWLQR QLSRFYDDAI VSQKKADEVL EILKTASDDR
     ECENQLVLLL GFNTFDFIKV LRQHRMMILY CTLLASAQSE PEKERIVGKM EADPELSKFL
     YQLHETEKED LIREERSRRE RVRQSRMDTD LETMDLDQGG EALAPRQVLD LEDLVFTQGS
     HFMANKRCQL PDGSFRRQRK GYEEVHVPAL KPKPFGSEEQ LLPVEKLPKY AQAGFEGFKT
     LNRIQSKLYR AALETDENLL LCAPTGAGKT NVALMCMLRE IGKHINMDGT INVDDFKIIY
     IAPMRSLVQE MVGSFGKRLA TYGITVAELT GDHQLCKEEI SATQIIVCTP EKWDIITRKG
     GERTYTQLVR LIVLDEIHLL HDDRGPVLEA LVARAIRNIE MTQEDVRLIG LSATLPNYED
     VATFLRVDPA KGLFYFDNSF RPVPLEQTYV GITEKKAIKR FQIMNEIVYE KIMEHAGKNQ
     VLVFVHSRKE TGKTARAIRD MCLEKDTLGL FLREGSASTE VLRTEAEQCK NLELKDLLPY
     GFAIHHAGMT RVDRTLVEDL FADKHIQVLV STATLAWGVN LPAHTVIIKG TQVYSPEKGR
     WTELGALDIL QMLGRAGRPQ YDTKGEGILI TSHGELQYYL SLLNQQLPIE SQMVSKLPDM
     LNAEIVLGNV QNAKDAVNWL GYAYLYIRML RSPTLYGISH DDLKGDPLLD QRRLDLVHTA
     ALMLDKNNLV KYDKKTGNFQ VTELGRIASH YYITNDTVQT YNQLLKPTLS EIELFRVFSL
     SSEFKNITVR EEEKLELQKL LERVPIPVKE SIEEPSAKIN VLLQAFISQL KLEGFALMAD
     MVYVTQSAGR LMRAIFEIVL NRGWAQLTDK TLNLCKMIDK RMWQSMCPLR QFRKLPEEVV
     KKIEKKNFPF ERLYDLNHNE IGELIRMPKM GKTIHKYVHL FPKLELSVHL QPITRSTLKV
     ELTITPDFQW DEKVHGSSEA FWILVEDVDS EVILHHEYFL LKAKYAQDEH LITFFVPVFE
     PLPPQYFIRV VSDRWLSCET QLPVSFRHLI LPEKYPPPTE LLDLQPLPVS ALRNSAFESL
     YQDKFPFFNP IQTQVFNTVY NSDDNVFVGA PTGSGKTICA EFAILRMLLQ NSEGRCVYIT
     PMEALAEQVY MDWYEKFQDR LNKKVVLLTG ETSTDLKLLG KGNIIISTPE KWDILSRRWK
     QRKNVQNINL FVVDEVHLIG GENGPVLEVI CSRMRYISSQ IERPIRIVAL SSSLSNAKDV
     AHWLGCSATS TFNFHPNVRP VPLELHIQGF NISHTQTRLL SMAKPVYHAI TKHSPKKPVI
     VFVPSRKQTR LTAIDILTTC AADIQRQRFL HCTEKDLIPY LEKLSDSTLK ETLLNGVGYL
     HEGLSPMERR LVEQLFSSGA IQVVVASRSL CWGMNVAAHL VIIMDTQYYN GKIHAYVDYP
     IYDVLQMVGH ANRPLQDDEG RCVIMCQGSK KDFFKKFLYE PLPVESHLDH CMHDHFNAEI
     VTKTIENKQD AVDYLTWTFL YRRMTQNPNY YNLQGISHRH LSDHLSELVE QTLSDLEQSK
     CISIEDEMDV APLNLGMIAA YYYINYTTIE LFSMSLNAKT KVRGLIEIIS NAAEYENIPI
     RHHEDNLLRQ LAQKVPHKLN NPKFNDPHVK TNLLLQAHLS RMQLSAELQS DTEEILSKAI
     RLIQACVDVL SSNGWLSPAL AAMELAQMVT QAMWSKDSYL KQLPHFTSEH IKRCTDKGVE
     SVFDIMEMED EERNALLQLT DSQIADVARF CNRYPNIELS YEVVDKDSIR SGGPVVVLVQ
     LEREEEVTGP VIAPLFPQKR EEGWWVVIGD AKSNSLISIK RLTLQQKAKV KLDFVAPATG
     GHNYTLYFMS DAYMGCDQEY KFSVDVKEAE TDSDSD
//