ID   MLP1_YEAST              Reviewed;        1875 AA.
AC   Q02455; D6VXF5;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   27-MAR-2024, entry version 196.
DE   RecName: Full=Protein MLP1;
DE   AltName: Full=Myosin-like protein 1;
GN   Name=MLP1; OrderedLocusNames=YKR095W; ORFNames=YKR415;
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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8483450; DOI=10.1007/bf00279439;
RA   Koelling R., Nguyen T., Chen E.Y., Botstein D.;
RT   "A new yeast gene with a myosin-like heptad repeat structure.";
RL   Mol. Gen. Genet. 237:359-369(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8154186; DOI=10.1002/yea.320091209;
RA   Bou G., Esteban P.F., Baladron V., Gonzalez G.A., Cantalejo J.G.,
RA   Remacha M.A., Jimenez A., del Rey F., Ballesta J.P.G., Revuelta J.L.;
RT   "The complete sequence of a 15,820 bp segment of Saccharomyces cerevisiae
RT   chromosome XI contains the UBI2 and MPL1 genes and three new open reading
RT   frames.";
RL   Yeast 9:1349-1354(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
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   FUNCTION, AND FORMATION OF CHROMATIN EXCLUDING FILAMENTOUS STRUCTURES WITH
RP   MLP2.
RX   PubMed=10085285; DOI=10.1083/jcb.144.5.839;
RA   Strambio-de-Castillia C., Blobel G., Rout M.P.;
RT   "Proteins connecting the nuclear pore complex with the nuclear interior.";
RL   J. Cell Biol. 144:839-855(1999).
RN   [6]
RP   FUNCTION, AND PERINUCLEAR TELOMERE CLUSTERING.
RX   PubMed=10638763; DOI=10.1038/47528;
RA   Galy V., Olivo-Marin J.-C., Scherthan H., Doye V., Rascalou N.,
RA   Nehrbass U.;
RT   "Nuclear pore complexes in the organization of silent telomeric
RT   chromatin.";
RL   Nature 403:108-112(2000).
RN   [7]
RP   FUNCTION, AND PERINUCLEAR-DEPENDENT SILENCING.
RX   PubMed=11862215; DOI=10.1038/ncb756;
RA   Feuerbach F., Galy V., Trelles-Sticken E., Fromont-Racine M., Jacquier A.,
RA   Gilson E., Olivo-Marin J.-C., Scherthan H., Nehrbass U.;
RT   "Nuclear architecture and spatial positioning help establish
RT   transcriptional states of telomeres in yeast.";
RL   Nat. Cell Biol. 4:214-221(2002).
RN   [8]
RP   FUNCTION, AND TELOMERE LENGTH REGULATION.
RX   PubMed=12490156; DOI=10.1016/s1047-8477(02)00533-6;
RA   Hediger F., Dubrana K., Gasser S.M.;
RT   "Myosin-like proteins 1 and 2 are not required for silencing or telomere
RT   anchoring, but act in the Tel1 pathway of telomere length control.";
RL   J. Struct. Biol. 140:79-91(2002).
RN   [9]
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   [10]
RP   FUNCTION, AND INTERACTION WITH NAB2.
RX   PubMed=12531921; DOI=10.1073/pnas.0336594100;
RA   Green D.M., Johnson C.P., Hagan H., Corbett A.H.;
RT   "The C-terminal domain of myosin-like protein 1 (Mlp1p) is a docking site
RT   for heterogeneous nuclear ribonucleoproteins that are required for mRNA
RT   export.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1010-1015(2003).
RN   [11]
RP   FUNCTION, SUBCELLULAR LOCATION, AND NUCLEAR RETENTION OF UNSPLICED
RP   PRE-MRNA.
RX   PubMed=14718167; DOI=10.1016/s0092-8674(03)01026-2;
RA   Galy V., Gadal O., Fromont-Racine M., Romano A., Jacquier A., Nehrbass U.;
RT   "Nuclear retention of unspliced mRNAs in yeast is mediated by perinuclear
RT   Mlp1.";
RL   Cell 116:63-73(2004).
RN   [12]
RP   PHOSPHORYLATION BY CDC28.
RX   PubMed=14574415; DOI=10.1038/nature02062;
RA   Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K.,
RA   Shokat K.M., Morgan D.O.;
RT   "Targets of the cyclin-dependent kinase Cdk1.";
RL   Nature 425:859-864(2003).
RN   [13]
RP   INTERACTION WITH MLP2, AND SUBCELLULAR LOCATION.
RX   PubMed=16027220; DOI=10.1083/jcb.200504140;
RA   Niepel M., Strambio-de-Castillia C., Fasolo J., Chait B.T., Rout M.P.;
RT   "The nuclear pore complex-associated protein, Mlp2p, binds to the yeast
RT   spindle pole body and promotes its efficient assembly.";
RL   J. Cell Biol. 170:225-235(2005).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-337; SER-379; SER-1670;
RP   SER-1710 AND SER-1803, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-337; SER-1710 AND SER-1733,
RP   AND 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   [16]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN THE
RP   NUCLEAR PORE COMPLEX, AND SUBCELLULAR LOCATION.
RX   PubMed=24152732; DOI=10.1091/mbc.e13-07-0412;
RA   Niepel M., Molloy K.R., Williams R., Farr J.C., Meinema A.C.,
RA   Vecchietti N., Cristea I.M., Chait B.T., Rout M.P.,
RA   Strambio-De-Castillia C.;
RT   "The nuclear basket proteins Mlp1p and Mlp2p are part of a dynamic
RT   interactome including Esc1p and the proteasome.";
RL   Mol. Biol. Cell 24:3920-3938(2013).
CC   -!- FUNCTION: Together with the closely related MLP2, involved in the
CC       structural and functional organization of perinuclear chromatin
CC       (PubMed:10638763). Together with MLP2, associates with the nuclear pore
CC       complex and form filamentous structures along the nuclear periphery
CC       (PubMed:10085285, PubMed:24152732). Has a role in the localization of
CC       Esc1 to nucleolar regions (PubMed:24152732). Together with MLP2,
CC       mediates tethering of the some telomeres to the nuclear periphery,
CC       probably mediated by YKU70/YKU80 (HDF1/HDF2) heterodimer and show
CC       perinuclear location dependent silencing (PubMed:11862215). MLP1 and
CC       MLP2 are involved in telomere length regulation but not silencing or
CC       telomere anchoring (PubMed:12490156). Recognizes the 5'-splice site of
CC       pre-mRNAs and retains unspliced pre-mRNA in the nucleus without
CC       affecting splicing itself (PubMed:12490156, PubMed:12531921,
CC       PubMed:14718167). {ECO:0000269|PubMed:10085285,
CC       ECO:0000269|PubMed:10638763, ECO:0000269|PubMed:11862215,
CC       ECO:0000269|PubMed:12490156, ECO:0000269|PubMed:12531921,
CC       ECO:0000269|PubMed:14718167, ECO:0000269|PubMed:24152732}.
CC   -!- SUBUNIT: Component of the nuclear pore complex (NPC) (PubMed:24152732).
CC       NPC constitutes the exclusive means of nucleocytoplasmic transport
CC       (PubMed:24152732). NPCs allow the passive diffusion of ions and small
CC       molecules and the active, nuclear transport receptor-mediated
CC       bidirectional transport of macromolecules such as proteins, RNAs,
CC       ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear
CC       envelope (PubMed:24152732). Due to its 8-fold rotational symmetry, all
CC       subunits are present with 8 copies or multiples thereof
CC       (PubMed:24152732). Interacts with NAB2, a hnRNP required for mRNA
CC       export (PubMed:12531921). Interacts with MLP2 (PubMed:16027220).
CC       {ECO:0000269|PubMed:12531921, ECO:0000269|PubMed:16027220,
CC       ECO:0000269|PubMed:24152732}.
CC   -!- INTERACTION:
CC       Q02455; P40457: MLP2; NbExp=2; IntAct=EBI-11009, EBI-25261;
CC       Q02455; P32505: NAB2; NbExp=4; IntAct=EBI-11009, EBI-11770;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14718167,
CC       ECO:0000269|PubMed:16027220}. Nucleus, nuclear pore complex
CC       {ECO:0000269|PubMed:24152732}. Note=Distributed fairly evenly along a
CC       C-shaped portion of the nuclear periphery, where the spindle pole body
CC       localizes in 90% of the cases. {ECO:0000269|PubMed:16027220}.
CC   -!- PTM: May be phosphorylated by CDC28. {ECO:0000269|PubMed:14574415}.
CC   -!- MISCELLANEOUS: Present with 2710 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- CAUTION: PubMed:8154186 misquoted the gene name as 'MPL1'.
CC       {ECO:0000305}.
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DR   EMBL; L01992; AAA34783.1; -; Genomic_DNA.
DR   EMBL; X73541; CAA51948.1; -; Genomic_DNA.
DR   EMBL; Z28320; CAA82174.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09245.1; -; Genomic_DNA.
DR   PIR; S38173; S38173.
DR   RefSeq; NP_013021.1; NM_001179885.1.
DR   AlphaFoldDB; Q02455; -.
DR   SMR; Q02455; -.
DR   BioGRID; 34226; 332.
DR   ComplexPortal; CPX-824; Nuclear pore complex.
DR   DIP; DIP-6675N; -.
DR   IntAct; Q02455; 9.
DR   MINT; Q02455; -.
DR   STRING; 4932.YKR095W; -.
DR   TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR   CarbonylDB; Q02455; -.
DR   GlyGen; Q02455; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q02455; -.
DR   MaxQB; Q02455; -.
DR   PaxDb; 4932-YKR095W; -.
DR   PeptideAtlas; Q02455; -.
DR   EnsemblFungi; YKR095W_mRNA; YKR095W; YKR095W.
DR   GeneID; 853970; -.
DR   KEGG; sce:YKR095W; -.
DR   AGR; SGD:S000001803; -.
DR   SGD; S000001803; MLP1.
DR   VEuPathDB; FungiDB:YKR095W; -.
DR   eggNOG; KOG4674; Eukaryota.
DR   GeneTree; ENSGT00940000176562; -.
DR   HOGENOM; CLU_002365_0_0_1; -.
DR   InParanoid; Q02455; -.
DR   OMA; HAQQNYE; -.
DR   OrthoDB; 2730913at2759; -.
DR   BioCyc; YEAST:G3O-32058-MONOMER; -.
DR   BioGRID-ORCS; 853970; 1 hit in 10 CRISPR screens.
DR   PRO; PR:Q02455; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; Q02455; Protein.
DR   GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR   GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR   GO; GO:0044615; C:nuclear pore nuclear basket; IDA:SGD.
DR   GO; GO:0005654; C:nucleoplasm; IDA:SGD.
DR   GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR   GO; GO:0140586; F:promoter-terminator loop anchoring activity; IMP:SGD.
DR   GO; GO:0043021; F:ribonucleoprotein complex binding; IGI:SGD.
DR   GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR   GO; GO:1901925; P:negative regulation of protein import into nucleus during spindle assembly checkpoint; IGI:SGD.
DR   GO; GO:0071028; P:nuclear mRNA surveillance; IMP:SGD.
DR   GO; GO:0006913; P:nucleocytoplasmic transport; NAS:ComplexPortal.
DR   GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
DR   GO; GO:0006606; P:protein import into nucleus; IGI:SGD.
DR   GO; GO:0090204; P:protein localization to nuclear pore; IMP:SGD.
DR   GO; GO:0034398; P:telomere tethering at nuclear periphery; IGI:SGD.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR012929; TPR/MLP1.
DR   PANTHER; PTHR18898:SF2; NUCLEOPROTEIN TPR; 1.
DR   PANTHER; PTHR18898; NUCLEOPROTEIN TPR-RELATED; 1.
DR   Pfam; PF07926; TPR_MLP1_2; 1.
DR   PROSITE; PS51450; LRR; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; DNA damage; DNA repair; mRNA transport;
KW   Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW   Reference proteome; Translocation; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..1875
FT                   /note="Protein MLP1"
FT                   /id="PRO_0000096501"
FT   REGION          1641..1690
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1716..1875
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          69..487
FT                   /evidence="ECO:0000255"
FT   COILED          531..1678
FT                   /evidence="ECO:0000255"
FT   COILED          1834..1866
FT                   /evidence="ECO:0000255"
FT   MOTIF           1496..1565
FT                   /note="Required for nuclear localization"
FT   COMPBIAS        1668..1689
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1716..1737
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1738..1752
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1766..1798
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1799..1875
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         337
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         379
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         1670
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         1710
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         1733
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1803
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   CONFLICT        301
FT                   /note="R -> A (in Ref. 1; AAA34783)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1875 AA;  218456 MW;  683A0D34C9066867 CRC64;
     MSDHDTPMES IQNGENSDER LNAIASFFGC SLEQVKSFDG DVVKHLNDKL LQFNELKSEN
     LKVTVSFDEL KASSLKKIDG LKTEMENVIR ENDKIRKERN DTFVKFESVE NEKMKLSSEL
     EFVKRKLDDL TEEKKETQSN QQRTLKILDE RLKEIELVRV ENNRSNSECK KLRSTIMDLE
     TKQQGYITND LNSRTELERK TQELTLLQSN NDWLEKELRS KNEQYLSYRQ KTDKVILDIR
     NELNRLRNDF QMERTNNDVL KQKNNELSKS LQEKLLEIKG LSDSLNSEKQ EFSAEMSLKQ
     RLVDLLESQL NAVKEELNSI RELNTAKVIA DDSKKQTPEN EDLLKELQLT KEKLAQCEKE
     CLRLSSITDE ADEDNENLSA KSSSDFIFLK KQLIKERRTK EHLQNQIETF IVELEHKVPI
     INSFKERTDM LENELNNAAL LLEHTSNEKN AKVKELNAKN QKLVECENDL QTLTKQRLDL
     CRQIQYLLIT NSVSNDSKGP LRKEEIQFIQ NIMQEDDSTI TESDSQKVVT ERLVEFKNII
     QLQEKNAELL KVVRNLADKL ESKEKKSKQS LQKIESETVN EAKEAIITLK SEKMDLESRI
     EELQKELEEL KTSVPNEDAS YSNVTIKQLT ETKRDLESQV QDLQTRISQI TRESTENMSL
     LNKEIQDLYD SKSDISIKLG KEKSSRILAE ERFKLLSNTL DLTKAENDQL RKRFDYLQNT
     ILKQDSKTHE TLNEYVSCKS KLSIVETELL NLKEEQKLRV HLEKNLKQEL NKLSPEKDSL
     RIMVTQLQTL QKEREDLLEE TRKSCQKKID ELEDALSELK KETSQKDHHI KQLEEDNNSN
     IEWYQNKIEA LKKDYESVIT SVDSKQTDIE KLQYKVKSLE KEIEEDKIRL HTYNVMDETI
     NDDSLRKELE KSKINLTDAY SQIKEYKDLY ETTSQSLQQT NSKLDESFKD FTNQIKNLTD
     EKTSLEDKIS LLKEQMFNLN NELDLQKKGM EKEKADFKKR ISILQNNNKE VEAVKSEYES
     KLSKIQNDLD QQTIYANTAQ NNYEQELQKH ADVSKTISEL REQLHTYKGQ VKTLNLSRDQ
     LENALKENEK SWSSQKESLL EQLDLSNSRI EDLSSQNKLL YDQIQIYTAA DKEVNNSTNG
     PGLNNILITL RRERDILDTK VTVAERDAKM LRQKISLMDV ELQDARTKLD NSRVEKENHS
     SIIQQHDDIM EKLNQLNLLR ESNITLRNEL ENNNNKKKEL QSELDKLKQN VAPIESELTA
     LKYSMQEKEQ ELKLAKEEVH RWKKRSQDIL EKHEQLSSSD YEKLESEIEN LKEELENKER
     QGAEAEEKFN RLRRQAQERL KTSKLSQDSL TEQVNSLRDA KNVLENSLSE ANARIEELQN
     AKVAQGNNQL EAIRKLQEDA EKASRELQAK LEESTTSYES TINGLNEEIT TLKEEIEKQR
     QIQQQLQATS ANEQNDLSNI VESMKKSFEE DKIKFIKEKT QEVNEKILEA QERLNQPSNI
     NMEEIKKKWE SEHEQEVSQK IREAEEALKK RIRLPTEEKI NKIIERKKEE LEKEFEEKVE
     ERIKSMEQSG EIDVVLRKQL EAKVQEKQKE LENEYNKKLQ EELKDVPHSS HISDDERDKL
     RAEIESRLRE EFNNELQAIK KKSFDEGKQQ AMMKTTLLER KLAKMESQLS ETKQSAESPP
     KSVNNVQNPL LGLPRKIEEN SNSPFNPLLS GEKLLKLNSK SSSGGFNPFT SPSPNKHLQN
     DNDKRESLAN KTDPPTHLEP SFNIPASRGL ISSSSTLSTD TNDEELTSNN PAQKDSSNRN
     VQSEEDTEKK KEGEPVKRGE AIEEQTKSNK RPIDEVGELK NDEDDTTENI NESKKIKTED
     EEEKETDKVN DENSI
//