MDN1_YEAST
ID MDN1_YEAST Reviewed; 4910 AA.
AC Q12019; D6VYA6; Q7LGX0;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Midasin;
DE AltName: Full=Dynein-related AAA-ATPase REA1;
DE AltName: Full=MIDAS-containing protein;
DE AltName: Full=Ribosome export/assembly protein 1;
GN Name=MDN1; Synonyms=REA1; OrderedLocusNames=YLR106C;
GN ORFNames=L2901, L8004.13;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-115.
RC STRAIN=ATCC 90840 / EAY235 / FY23;
RX PubMed=9090053;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<241::aid-yea61>3.0.co;2-#;
RA Verhasselt P., Volckaert G.;
RT "Sequence analysis of a 37.6 kbp cosmid clone from the right arm of
RT Saccharomyces cerevisiae chromosome XII, carrying YAP3, HOG1, SNR6, tRNA-
RT Arg3 and 23 new open reading frames, among which several homologies to
RT proteins involved in cell division control and to mammalian growth factors
RT and other animal proteins are found.";
RL Yeast 13:241-250(1997).
RN [4]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=11583615; DOI=10.1016/s1097-2765(01)00342-2;
RA Bassler J., Grandi P., Gadal O., Lessmann T., Petfalski E., Tollervey D.,
RA Lechner J., Hurt E.;
RT "Identification of a 60S preribosomal particle that is closely linked to
RT nuclear export.";
RL Mol. Cell 8:517-529(2001).
RN [5]
RP CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=12102729; DOI=10.1186/1471-2164-3-18;
RA Garbarino J.E., Gibbons I.R.;
RT "Expression and genomic analysis of midasin, a novel and highly conserved
RT AAA protein distantly related to dynein.";
RL BMC Genomics 3:18-18(2002).
RN [6]
RP IDENTIFICATION IN PRE-60S RIBOSOMES, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12374754; DOI=10.1093/emboj/cdf547;
RA Nissan T.A., Bassler J., Petfalski E., Tollervey D., Hurt E.;
RT "60S pre-ribosome formation viewed from assembly in the nucleolus until
RT export to the cytoplasm.";
RL EMBO J. 21:5539-5547(2002).
RN [7]
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 [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15528184; DOI=10.1074/jbc.m406876200;
RA Galani K., Nissan T.A., Petfalski E., Tollervey D., Hurt E.;
RT "Rea1, a dynein-related nuclear AAA-ATPase, is involved in late rRNA
RT processing and nuclear export of 60 S subunits.";
RL J. Biol. Chem. 279:55411-55418(2004).
RN [9]
RP FUNCTION, AND SUBUNIT.
RX PubMed=15260980; DOI=10.1016/j.molcel.2004.06.033;
RA Nissan T.A., Galani K., Maco B., Tollervey D., Aebi U., Hurt E.;
RT "A pre-ribosome with a tadpole-like structure functions in ATP-dependent
RT maturation of 60S subunits.";
RL Mol. Cell 15:295-301(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1026; SER-2971; SER-4353 AND
RP THR-4388, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [11]
RP FUNCTION, ASSOCIATION WITH THE PRE-60S PARTICLE, AND INTERACTION WITH RSA4.
RX PubMed=19737519; DOI=10.1016/j.cell.2009.06.045;
RA Ulbrich C., Diepholz M., Bassler J., Kressler D., Pertschy B., Galani K.,
RA Bottcher B., Hurt E.;
RT "Mechanochemical removal of ribosome biogenesis factors from nascent 60S
RT ribosomal subunits.";
RL Cell 138:911-922(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2971 AND SER-4555, AND
RP 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 [13]
RP FUNCTION, INTERACTION WITH RSA4 AND YTM1, AND SUBCELLULAR LOCATION.
RX PubMed=20542003; DOI=10.1016/j.molcel.2010.05.024;
RA Bassler J., Kallas M., Pertschy B., Ulbrich C., Thoms M., Hurt E.;
RT "The AAA-ATPase Rea1 drives removal of biogenesis factors during multiple
RT stages of 60S ribosome assembly.";
RL Mol. Cell 38:712-721(2010).
RN [14]
RP FUNCTION.
RX PubMed=24240281; DOI=10.1038/nature12731;
RA Matsuo Y., Granneman S., Thoms M., Manikas R.G., Tollervey D., Hurt E.;
RT "Coupled GTPase and remodelling ATPase activities form a checkpoint for
RT ribosome export.";
RL Nature 505:112-116(2014).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (9.50 ANGSTROMS), AND INTERACTION WITH
RP RIX1.
RX PubMed=26619264; DOI=10.1038/nsmb.3132;
RA Barrio-Garcia C., Thoms M., Flemming D., Kater L., Berninghausen O.,
RA Bassler J., Beckmann R., Hurt E.;
RT "Architecture of the Rix1-Rea1 checkpoint machinery during pre-60S-ribosome
RT remodeling.";
RL Nat. Struct. Mol. Biol. 23:37-44(2016).
CC -!- FUNCTION: Nuclear chaperone required for maturation and nuclear export
CC of pre-60S ribosome subunits. Functions at successive maturation steps
CC to remove ribosomal factors at critical transition points, first
CC driving the exit of early pre-60S particles from the nucleolus and then
CC driving late pre-60S particles from the nucleus (PubMed:15260980,
CC PubMed:15528184, PubMed:19737519, PubMed:20542003). At an early stage
CC in 60S maturation, mediates the dissociation of the NOP7 complex (YTM1-
CC ERB1-NOP7) from early pre-60S particles, rendering them competent for
CC export from the nucleolus to the nucleoplasm (PubMed:20542003).
CC Subsequently recruited to the nucleoplasmic particles through
CC interaction with the RIX1 complex. This binding is only possible if the
CC 5S RNP at the central protuberance has undergone the rotation to
CC complete its maturation (PubMed:26619264). After remodeling, removes
CC the ribosome biogenesis factor RSA4 in an ATP hydrolysis-driven step
CC from pre-60S ribosomal subunits, rendering them competent for export
CC from the nucleoplasm to the cytoplasm (PubMed:19737519,
CC PubMed:20542003). Activates the GTPase activity of NOG2, which
CC disengages from the pre-60S particle upon GTP hydrolysis, thus freeing
CC its binding site for the nuclear export factor NMD3 (PubMed:24240281).
CC {ECO:0000269|PubMed:15260980, ECO:0000269|PubMed:15528184,
CC ECO:0000269|PubMed:19737519, ECO:0000269|PubMed:20542003,
CC ECO:0000269|PubMed:24240281, ECO:0000269|PubMed:26619264}.
CC -!- SUBUNIT: Associates with pre-60S ribosomes in the nucleoplasm
CC (PubMed:11583615, PubMed:12374754, PubMed:15260980, PubMed:19737519).
CC Interacts (via its hexameric AAA ATPase ring) with the RIX1 complex
CC (via RIX1); this interaction is crucial for recruitment of MDN1 to the
CC pre-ribosomal particle (PubMed:15260980, PubMed:26619264). Interacts
CC (via VWFA/MIDAS domain) with YTM1 (via UBL domain) (PubMed:20542003).
CC Interacts (via VWFA/MIDAS domain) with RSA4 (via UBL domain)
CC (PubMed:19737519, PubMed:20542003). {ECO:0000269|PubMed:11583615,
CC ECO:0000269|PubMed:12374754, ECO:0000269|PubMed:15260980,
CC ECO:0000269|PubMed:19737519, ECO:0000269|PubMed:20542003,
CC ECO:0000269|PubMed:26619264}.
CC -!- INTERACTION:
CC Q12019; P25382: RSA4; NbExp=5; IntAct=EBI-10633, EBI-21980;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11583615,
CC ECO:0000269|PubMed:12102729, ECO:0000269|PubMed:15528184}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:20542003}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:15528184}.
CC -!- DOMAIN: The protein has several distinct domains, an N-terminal
CC extension (35 kDa), followed by an ATPase domain containing a hexameric
CC ring of six tandem AAA protomers (between 28 and 40 kDa each), a linker
CC domain (260 kDa), an Asp/Glu-rich domain (approximately 70 kDa) and a
CC C-terminal VWFA domain (30 kDa) that possesses a MIDAS (metal ion-
CC dependent adhesion site). The ring-like ATPase head domain associates
CC with the RIX1 complex on the pre-ribosome, while the flexible tail
CC protrudes from the molecule. {ECO:0000305|PubMed:26619264}.
CC -!- MISCELLANEOUS: Present with 538 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the midasin family. {ECO:0000305}.
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DR EMBL; U53876; AAB67548.1; -; Genomic_DNA.
DR EMBL; Z73278; CAA97671.1; -; Genomic_DNA.
DR EMBL; X89514; CAA61684.1; -; Genomic_DNA.
DR EMBL; Z73279; CAA97673.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09422.1; -; Genomic_DNA.
DR PIR; S64942; S64942.
DR RefSeq; NP_013207.1; NM_001181993.1.
DR PDB; 5FL8; EM; 9.50 A; s=1-4910.
DR PDB; 5JCS; EM; 9.50 A; s=1-4910.
DR PDB; 6HYD; EM; 3.90 A; A=2356-4041.
DR PDB; 6HYP; EM; 4.40 A; A=238-4910.
DR PDB; 6I26; EM; 4.30 A; A=238-4910.
DR PDB; 6I27; EM; 7.80 A; A=238-4910.
DR PDB; 6YLF; EM; 4.20 A; AP1=1-4910.
DR PDB; 6YLH; EM; 3.10 A; v=1-4910.
DR PDBsum; 5FL8; -.
DR PDBsum; 5JCS; -.
DR PDBsum; 6HYD; -.
DR PDBsum; 6HYP; -.
DR PDBsum; 6I26; -.
DR PDBsum; 6I27; -.
DR PDBsum; 6YLF; -.
DR PDBsum; 6YLH; -.
DR SMR; Q12019; -.
DR BioGRID; 31379; 159.
DR DIP; DIP-6285N; -.
DR IntAct; Q12019; 43.
DR MINT; Q12019; -.
DR STRING; 4932.YLR106C; -.
DR iPTMnet; Q12019; -.
DR MaxQB; Q12019; -.
DR PaxDb; Q12019; -.
DR PRIDE; Q12019; -.
DR EnsemblFungi; YLR106C_mRNA; YLR106C; YLR106C.
DR GeneID; 850796; -.
DR KEGG; sce:YLR106C; -.
DR SGD; S000004096; MDN1.
DR VEuPathDB; FungiDB:YLR106C; -.
DR eggNOG; KOG1808; Eukaryota.
DR GeneTree; ENSGT00550000074802; -.
DR HOGENOM; CLU_000050_0_2_1; -.
DR InParanoid; Q12019; -.
DR OMA; ELGPPNI; -.
DR BioCyc; YEAST:G3O-32254-MON; -.
DR PRO; PR:Q12019; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12019; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0110136; P:protein-RNA complex remodeling; IDA:SGD.
DR GO; GO:2000200; P:regulation of ribosomal subunit export from nucleus; IMP:SGD.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR Gene3D; 3.40.50.300; -; 6.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR040848; AAA_lid_7.
DR InterPro; IPR011704; ATPase_dyneun-rel_AAA.
DR InterPro; IPR012099; Midasin.
DR InterPro; IPR041190; Midasin_AAA_lid_5.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF07728; AAA_5; 8.
DR Pfam; PF17865; AAA_lid_5; 1.
DR Pfam; PF17867; AAA_lid_7; 3.
DR PIRSF; PIRSF010340; Midasin; 1.
DR SMART; SM00382; AAA; 6.
DR SUPFAM; SSF52540; SSF52540; 6.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..4910
FT /note="Midasin"
FT /id="PRO_0000096337"
FT DOMAIN 4704..4899
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 305..528
FT /note="AAA-ATPase protomer 1"
FT /evidence="ECO:0000255"
FT REGION 636..975
FT /note="AAA-ATPase protomer 2"
FT /evidence="ECO:0000255"
FT REGION 695..803
FT /note="Interaction with RIX1"
FT /evidence="ECO:0000269|PubMed:26619264"
FT REGION 1054..1280
FT /note="AAA-ATPase protomer 3"
FT /evidence="ECO:0000255"
FT REGION 1345..1624
FT /note="AAA-ATPase protomer 4"
FT /evidence="ECO:0000255"
FT REGION 1732..1985
FT /note="AAA-ATPase protomer 5"
FT /evidence="ECO:0000255"
FT REGION 2036..2286
FT /note="AAA-ATPase protomer 6"
FT /evidence="ECO:0000255"
FT REGION 2372..4075
FT /note="Linker"
FT /evidence="ECO:0000305|PubMed:26619264"
FT REGION 4045..4600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4099..4152
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4153..4205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4206..4248
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4255..4276
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4277..4302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4303..4351
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4352..4382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4395..4430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4431..4449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4456..4497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4498..4517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4518..4556
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4557..4598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 315..322
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 653..660
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1083..1090
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1368..1375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1747..1754
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2054..2061
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 1026
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 2971
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 4353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 4388
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 4555
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 4910 AA; 559308 MW; E4E873BEDF6E1E5B CRC64;
MSQDRILLDL DVVNQRLILF NSAFPSDAIE APFHFSNKES TSENLDNLAG TILHSRSITG
HVFLYKHIFL EIVARWIKDS KKKDYVLVIE KLASIITIFP VAMPLIEDYL DKENDHFITI
LQNPSTQKDS DMFKILLAYY RLLYHNKEVF ARFIQPDILY QLVDLLTKEQ ENQVVIFLAL
KVLSLYLDMG EKTLNDMLDT YIKSRDSLLG HFEGDSGIDY SFLELNEAKR CANFSKLPSV
PECFTIEKKS SYFIIEPQDL STKVASICGV IVPKVHTIHD KVFYPLTFVP THKTVSSLRQ
LGRKIQNSTP IMLIGKAGSG KTFLINELSK YMGCHDSIVK IHLGEQTDAK LLIGTYTSGD
KPGTFEWRAG VLATAVKEGR WVLIEDIDKA PTDVLSILLS LLEKRELTIP SRGETVKAAN
GFQLISTVRI NEDHQKDSSN KIYNLNMIGM RIWNVIELEE PSEEDLTHIL AQKFPILTNL
IPKLIDSYKN VKSIYMNTKF ISLNKGAHTR VVSVRDLIKL CERLDILFKN NGINKPDQLI
QSSVYDSIFS EAADCFAGAI GEFKALEPII QAIGESLDIA SSRISLFLTQ HVPTLENLDD
SIKIGRAVLL KEKLNIQKKS MNSTLFAFTN HSLRLMEQIS VCIQMTEPVL LVGETGTGKT
TVVQQLAKML AKKLTVINVS QQTETGDLLG GYKPVNSKTV AVPIQENFET LFNATFSLKK
NEKFHKMLHR CFNKNQWKNV VKLWNEAYKM AQSILKITNT ENENENAKKK KRRLNTHEKK
LLLDKWADFN DSVKKFEAQS SSIENSFVFN FVEGSLVKTI RAGEWLLLDE VNLATADTLE
SISDLLTEPD SRSILLSEKG DAEPIKAHPD FRIFACMNPA TDVGKRDLPM GIRSRFTEIY
VHSPERDITD LLSIIDKYIG KYSVSDEWVG NDIAELYLEA KKLSDNNTIV DGSNQKPHFS
IRTLTRTLLY VTDIIHIYGL RRSLYDGFCM SFLTLLDQKS EAILKPVIEK FTLGRLKNVK
SIMSQTPPSP GPDYVQFKHY WMKKGPNTIQ EQAHYIITPF VEKNMMNLVR ATSGKRFPVL
IQGPTSSGKT SMIKYLADIT GHKFVRINNH EHTDLQEYLG TYVTDDTGKL SFKEGVLVEA
LRKGYWIVLD ELNLAPTDVL EALNRLLDDN RELFIPETQE VVHPHPDFLL FATQNPPGIY
GGRKILSRAF RNRFLELHFD DIPQDELEII LRERCQIAPS YAKKIVEVYR QLSIERSASR
LFEQKNSFAT LRDLFRWALR DAVGYEQLAA SGYMLLAERC RTPQEKVTVK KTLEKVMKVK
LDMDQYYASL EDKSLEAIGS VTWTKGMRRL SVLVSSCLKN KEPVLLVGET GCGKTTICQL
LAQFMGRELI TLNAHQNTET GDILGAQRPV RNRSEIQYKL IKSLKTALNI ANDQDVDLKE
LLQLYSKSDN KNIAEDVQLE IQKLRDSLNV LFEWSDGPLI QAMRTGNFFL LDEISLADDS
VLERLNSVLE PERSLLLAEQ GSSDSLVTAS ENFQFFATMN PGGDYGKKEL SPALRNRFTE
IWVPSMEDFN DVNMIVSSRL LEDLKDLANP IVKFSEWFGK KLGGGNATSG VISLRDILAW
VEFINKVFPK IQNKSTALIQ GASMVFIDAL GTNNTAYLAE NENDLKSLRT ECIIQLLKLC
GDDLELQQIE TNEIIVTQDE LQVGMFKIPR FPDAQSSSFN LTAPTTASNL VRVVRAMQVH
KPILLEGSPG VGKTSLITAL ANITGNKLTR INLSEQTDLV DLFGADAPGE RSGEFLWHDA
PFLRAMKKGE WVLLDEMNLA SQSVLEGLNA CLDHRGEAYI PELDISFSCH PNFLVFAAQN
PQYQGGGRKG LPKSFVNRFS VVFIDMLTSD DLLLIAKHLY PSIEPDIIAK MIKLMSTLED
QVCKRKLWGN SGSPWEFNLR DTLRWLKLLN QYSICEDVDV FDFVDIIVKQ RFRTISDKNK
AQLLIEDIFG KFSTKENFFK LTEDYVQINN EVALRNPHYR YPITQNLFPL ECNVAVYESV
LKAINNNWPL VLVGPSNSGK TETIRFLASI LGPRVDVFSM NSDIDSMDIL GGYEQVDLTR
QISYITEELT NIVREIISMN MKLSPNATAI MEGLNLLKYL LNNIVTPEKF QDFRNRFNRF
FSHLEGHPLL KTMSMNIEKM TEIITKEASV KFEWFDGMLV KAVEKGHWLI LDNANLCSPS
VLDRLNSLLE IDGSLLINEC SQEDGQPRVL KPHPNFRLFL TMDPKYGELS RAMRNRGVEI
YIDELHSRST AFDRLTLGFE LGENIDFVSI DDGIKKIKLN EPDMSIPLKH YVPSYLSRPC
IFAQVHDILL LSDEEPIEES LAAVIPISHL GEVGKWANNV LNCTEYSEKK IAERLYVFIT
FLTDMGVLEK INNLYKPANL KFQKALGLHD KQLTEETVSL TLNEYVLPTV SKYSDKIKSP
ESLYLLSSLR LLLNSLNALK LINEKSTHGK IDELTYIELS AAAFNGRHLK NIPRIPIFCI
LYNILTVMSE NLKTESLFCG SNQYQYYWDL LVIVIAALET AVTKDEARLR VYKELIDSWI
ASVKSKSDIE ITPFLNINLE FTDVLQLSRG HSITLLWDIF RKNYPTTSNS WLAFEKLINL
SEKFDKVRLL QFSESYNSIK DLMDVFRLLN DDVLNNKLSE FNLLLSKLED GINELELISN
KFLNKRKHYF ADEFDNLIRY TFSVDTAELI KELAPASSLA TQKLTKLITN KYNYPPIFDV
LWTEKNAKLT SFTSTIFSSQ FLEDVVRKSN NLKSFSGNQI KQSISDAELL LSSTIKCSPN
LLKSQMEYYK NMLLSWLRKV IDIHVGGDCL KLTLKELCSL IEEKTASETR VTFAEYIFPA
LDLAESSKSL EELGEAWITF GTGLLLLFVP DSPYDPAIHD YVLYDLFLKT KTFSQNLMKS
WRNVRKVISG DEEIFTEKLI NTISDDDAPQ SPRVYRTGMS IDSLFDEWMA FLSSTMSSRQ
IKELVSSYKC NSDQSDRRLE MLQQNSAHFL NRLESGYSKF ADLNDILAGY IYSINFGFDL
LKLQKSKDRA SFQISPLWSM DPINISCAEN VLSAYHELSR FFKKGDMEDT SIEKVLMYFL
TLFKFHKRDT NLLEIFEAAL YTLYSRWSVR RFRQEQEENE KSNMFKFNDN SDDYEADFRK
LFPDYEDTAL VTNEKDISSP ENLDDIYFKL ADTYISVFDK DHDANFSSEL KSGAIITTIL
SEDLKNTRIE ELKSGSLSAV INTLDAETQS FKNTEVFGNI DFYHDFSIPE FQKAGDIIET
VLKSVLKLLK QWPEHATLKE LYRVSQEFLN YPIKTPLARQ LQKIEQIYTY LAEWEKYASS
EVSLNNTVKL ITDLIVSWRK LELRTWKGLF NSEDAKTRKS IGKWWFYLYE SIVISNFVSE
KKETAPNATL LVSSLNLFFS KSTLGEFNAR LDLVKAFYKH IQLIGLRSSK IAGLLHNTIK
FYYQFKPLID ERITNGKKSL EKEIDDIILL ASWKDVNVDA LKQSSRKSHN NLYKIVRKYR
DLLNGDAKTI IEAGLLYSNE NKLKLPTLKQ HFYEDPNLEA SKNLVKEIST WSMRAAPLRN
IDTVASNMDS YLEKISSQEF PNFADLASDF YAEAERLRKE TPNVYTKENK KRLAYLKTQK
SKLLGDALKE LRRIGLKVNF REDIQKVQSS TTTILANIAP FNNEYLNSSD AFFFKILDLL
PKLRSAASNP SDDIPVAAIE RGMALAQSLM FSLITVRHPL SEFTNDYCKI NGMMLDLEHF
TCLKGDIVHS SLKANVDNVR LFEKWLPSLL DYAAQTLSVI SKYSATSEQQ KILLDAKSTL
SSFFVHFNSS RIFDSSFIES YSRFELFINE LLKKLENAKE TGNAFVFDII IEWIKANKGG
PIKKEQKRGP SVEDVEQAFR RTFTSIILSF QKVIGDGIES ISETDDNWLS ASFKKVMVNV
KLLRSSVVSK NIETALSLLK DFDFTTTESI YVKSVISFTL PVITRYYNAM TVVLERSRIY
YTNTSRGMYI LSTILHSLAK NGFCSPQPPS EEVDDKNLQE GTGLGDGEGA QNNNKDVEQD
EDLTEDAQNE NKEQQDKDER DDENEDDAVE MEGDMAGELE DLSNGEENDD EDTDSEEEEL
DEEIDDLNED DPNAIDDKMW DDKASDNSKE KDTDQNLDGK NQEEDVQAAE NDEQQRDNKE
GGDEDPNAPE DGDEEIENDE NAEEENDVGE QEDEVKDEEG EDLEANVPEI ETLDLPEDMN
LDSEHEESDE DVDMSDGMPD DLNKEEVGNE DEEVKQESGI ESDNENDEPG PEEDAGETET
ALDEEEGAEE DVDMTNDEGK EDEENGPEEQ AMSDEEELKQ DAAMEENKEK GGEQNTEGLD
GVEEKADTED IDQEAAVQQD SGSKGAGADA TDTQEQDDVG GSGTTQNTYE EDQEDVTKNN
EESREEATAA LKQLGDSMKE YHRRRQDIKE AQTNGEEDEN LEKNNERPDE FEHVEGANTE
TDTQALGSAT QDQLQTIDED MAIDDDREEQ EVDQKELVED ADDEKMDIDE EEMLSDIDAH
DANNDVDSKK SGFIGKRKSE EDFENELSNE HFSADQEDDS EIQSLIENIE DNPPDASASL
TPERSLEESR ELWHKSEIST ADLVSRLGEQ LRLILEPTLA TKLKGDYKTG KRLNMKRIIP
YIASQFRKDK IWLRRTKPSK RQYQIMIALD DSKSMSESKC VKLAFDSLCL VSKTLTQLEA
GGLSIVKFGE NIKEVHSFDQ QFSNESGARA FQWFGFQETK TDVKKLVAES TKIFERARAM
VHNDQWQLEI VISDGICEDH ETIQKLVRRA RENKIMLVFV IIDGITSNES ILDMSQVNYI
PDQYGNPQLK ITKYLDTFPF EFYVVVHDIS ELPEMLSLIL RQYFTDLASS
