MLP1_YEAST
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 03-AUG-2022, entry version 189.
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; 321.
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 iPTMnet; Q02455; -.
DR MaxQB; Q02455; -.
DR PaxDb; Q02455; -.
DR PRIDE; Q02455; -.
DR EnsemblFungi; YKR095W_mRNA; YKR095W; YKR095W.
DR GeneID; 853970; -.
DR KEGG; sce:YKR095W; -.
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; KYDRVDP; -.
DR BioCyc; YEAST:G3O-32058-MON; -.
DR Reactome; R-SCE-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-SCE-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-SCE-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-SCE-4570464; SUMOylation of RNA binding proteins.
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; IC: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 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
