NLE1_YEAST
ID NLE1_YEAST Reviewed; 515 AA.
AC P25382; D6VR74; Q8NKJ4;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Ribosome assembly protein 4 {ECO:0000303|PubMed:16221974};
DE AltName: Full=Notchless protein homolog 1 {ECO:0000250|UniProtKB:Q9VPR4};
DE AltName: Full=Ribosome biogenesis factor RSA4 {ECO:0000303|PubMed:19737519};
GN Name=RSA4 {ECO:0000303|PubMed:16221974};
GN OrderedLocusNames=YCR072C {ECO:0000312|SGD:S000000668}; ORFNames=YCR72C;
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=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [2]
RP SEQUENCE REVISION.
RA Jimenez A.;
RL Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE REVISION TO 444.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16221974; DOI=10.1093/nar/gki887;
RA de la Cruz J., Sanz-Martinez E., Remacha M.;
RT "The essential WD-repeat protein Rsa4p is required for rRNA processing and
RT intra-nuclear transport of 60S ribosomal subunits.";
RL Nucleic Acids Res. 33:5728-5739(2005).
RN [7]
RP COPURIFICATION WITH RIBOSOMAL COMPLEXES, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16702403; DOI=10.1101/gad.1422006;
RA Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.;
RT "Systematic identification and functional screens of uncharacterized
RT proteins associated with eukaryotic ribosomal complexes.";
RL Genes Dev. 20:1294-1307(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP 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 [10]
RP ASSOCIATION WITH THE PRE-60S PARTICLE.
RX PubMed=18658244; DOI=10.1093/nar/gkn469;
RA Lebreton A., Rousselle J.C., Lenormand P., Namane A., Jacquier A.,
RA Fromont-Racine M., Saveanu C.;
RT "60S ribosomal subunit assembly dynamics defined by semi-quantitative mass
RT spectrometry of purified complexes.";
RL Nucleic Acids Res. 36:4988-4999(2008).
RN [11]
RP FUNCTION, ASSOCIATION WITH THE PRE-60S PARTICLE, INTERACTION WITH MDN1, AND
RP MUTAGENESIS OF GLU-114.
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 FUNCTION, AND INTERACTION WITH MDN1.
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 [13]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), AND INTERACTION WITH NSA2.
RX PubMed=25404745; DOI=10.1083/jcb.201408111;
RA Bassler J., Paternoga H., Holdermann I., Thoms M., Granneman S.,
RA Barrio-Garcia C., Nyarko A., Lee W., Stier G., Clark S.A., Schraivogel D.,
RA Kallas M., Beckmann R., Tollervey D., Barbar E., Sinning I., Hurt E.;
RT "A network of assembly factors is involved in remodeling rRNA elements
RT during preribosome maturation.";
RL J. Cell Biol. 207:481-498(2014).
RN [14]
RP ERRATUM OF PUBMED:25404745.
RX PubMed=26150393; DOI=10.1083/jcb.20140811106112015c;
RA Bassler J., Paternoga H., Holdermann I., Thoms M., Granneman S.,
RA Barrio-Garcia C., Nyarko A., Lee W., Stier G., Clark S.A., Schraivogel D.,
RA Kallas M., Beckmann R., Tollervey D., Barbar E., Sinning I., Hurt E.;
RL J. Cell Biol. 210:169-170(2015).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (8.70 ANGSTROMS).
RX PubMed=24662372; DOI=10.1038/ncomms4491;
RA Leidig C., Thoms M., Holdermann I., Bradatsch B., Berninghausen O.,
RA Bange G., Sinning I., Hurt E., Beckmann R.;
RT "60S ribosome biogenesis requires rotation of the 5S ribonucleoprotein
RT particle.";
RL Nat. Commun. 5:3491-3491(2014).
RN [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (9.50 ANGSTROMS).
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).
RN [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.08 ANGSTROMS).
RX PubMed=27251291; DOI=10.1038/nature17942;
RA Wu S., Tutuncuoglu B., Yan K., Brown H., Zhang Y., Tan D., Gamalinda M.,
RA Yuan Y., Li Z., Jakovljevic J., Ma C., Lei J., Dong M.Q.,
RA Woolford J.L. Jr., Gao N.;
RT "Diverse roles of assembly factors revealed by structures of late nuclear
RT pre-60S ribosomes.";
RL Nature 534:133-137(2016).
CC -!- FUNCTION: Involved in ribosome biogenesis. Required for processing and
CC efficient intra-nuclear transport of pre-60S ribosomal subunits.
CC Interacts with the AAA-ATPase Midasin (MDN1/REA1), which is essential
CC for the ATP-dependent dissociation of a group of nonribosomal factors
CC from the pre-60S particle. {ECO:0000269|PubMed:16221974,
CC ECO:0000269|PubMed:19737519, ECO:0000269|PubMed:20542003}.
CC -!- SUBUNIT: Associates with the pre-60S ribosomal particle
CC (PubMed:16702403, PubMed:18658244, PubMed:19737519). Interacts (via WD
CC repeats) with uL18 (RPL5) (PubMed:25404745). Interacts (via UBL domain)
CC with MDN1 (via VWFA/MIDAS domain) (PubMed:19737519, PubMed:20542003).
CC Interacts (via WD repeats) with NSA2 (PubMed:25404745).
CC {ECO:0000269|PubMed:16702403, ECO:0000269|PubMed:18658244,
CC ECO:0000269|PubMed:19737519, ECO:0000269|PubMed:20542003,
CC ECO:0000269|PubMed:25404745}.
CC -!- INTERACTION:
CC P25382; Q12019: MDN1; NbExp=5; IntAct=EBI-21980, EBI-10633;
CC P25382; P40078: NSA2; NbExp=4; IntAct=EBI-21980, EBI-22681;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16221974}.
CC -!- SIMILARITY: Belongs to the NLE1/RSA4 family. {ECO:0000305}.
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DR EMBL; X59720; CAC42989.1; -; Genomic_DNA.
DR EMBL; AY692666; AAT92685.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07543.1; -; Genomic_DNA.
DR PIR; S19487; S19487.
DR RefSeq; NP_009997.2; NM_001178782.1.
DR PDB; 3JCT; EM; 3.08 A; x=1-515.
DR PDB; 4V7F; EM; 8.70 A; q=1-515.
DR PDB; 4WJU; X-ray; 2.80 A; A/B=1-515.
DR PDB; 4WJV; X-ray; 3.20 A; A/B/C/D=137-515.
DR PDB; 5FL8; EM; 9.50 A; q=1-515.
DR PDB; 5JCS; EM; 9.50 A; q=1-515.
DR PDB; 6FT6; EM; 3.90 A; x=1-515.
DR PDB; 6M62; EM; 3.20 A; x=1-515.
DR PDB; 6YLF; EM; 4.20 A; xP1=1-515.
DR PDB; 6YLG; EM; 3.00 A; x=1-515.
DR PDB; 6YLH; EM; 3.10 A; x=1-515.
DR PDB; 7BT6; EM; 3.12 A; x=1-515.
DR PDB; 7BTB; EM; 3.22 A; x=1-515.
DR PDB; 7OH3; EM; 3.40 A; x=1-515.
DR PDB; 7OHQ; EM; 3.10 A; x=1-515.
DR PDB; 7OHT; EM; 4.70 A; x=1-515.
DR PDBsum; 3JCT; -.
DR PDBsum; 4V7F; -.
DR PDBsum; 4WJU; -.
DR PDBsum; 4WJV; -.
DR PDBsum; 5FL8; -.
DR PDBsum; 5JCS; -.
DR PDBsum; 6FT6; -.
DR PDBsum; 6M62; -.
DR PDBsum; 6YLF; -.
DR PDBsum; 6YLG; -.
DR PDBsum; 6YLH; -.
DR PDBsum; 7BT6; -.
DR PDBsum; 7BTB; -.
DR PDBsum; 7OH3; -.
DR PDBsum; 7OHQ; -.
DR PDBsum; 7OHT; -.
DR AlphaFoldDB; P25382; -.
DR SMR; P25382; -.
DR BioGRID; 31047; 105.
DR DIP; DIP-5365N; -.
DR IntAct; P25382; 19.
DR MINT; P25382; -.
DR STRING; 4932.YCR072C; -.
DR iPTMnet; P25382; -.
DR MaxQB; P25382; -.
DR PaxDb; P25382; -.
DR PRIDE; P25382; -.
DR EnsemblFungi; YCR072C_mRNA; YCR072C; YCR072C.
DR GeneID; 850435; -.
DR KEGG; sce:YCR072C; -.
DR SGD; S000000668; RSA4.
DR VEuPathDB; FungiDB:YCR072C; -.
DR eggNOG; KOG0271; Eukaryota.
DR GeneTree; ENSGT00940000157881; -.
DR HOGENOM; CLU_000288_57_16_1; -.
DR InParanoid; P25382; -.
DR OMA; HINCLAW; -.
DR BioCyc; YEAST:G3O-29372-MON; -.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:P25382; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25382; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0110136; P:protein-RNA complex remodeling; IMP:SGD.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR012972; NLE.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF08154; NLE; 1.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 8.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 5.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; Repeat; Ribosome biogenesis;
KW WD repeat.
FT CHAIN 1..515
FT /note="Ribosome assembly protein 4"
FT /id="PRO_0000051471"
FT REPEAT 141..181
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 184..223
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 227..273
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 276..314
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 352..396
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 400..439
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 442..481
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REPEAT 484..515
FT /note="WD 8"
FT /evidence="ECO:0000255"
FT REGION 20..128
FT /note="Interaction with MDN1"
FT /evidence="ECO:0000269|PubMed:19737519"
FT REGION 29..125
FT /note="Ubiquitin-like (UBL) domain"
FT /evidence="ECO:0000305|PubMed:25404745"
FT MUTAGEN 114
FT /note="E->A: Impairs interaction with MDN1."
FT /evidence="ECO:0000269|PubMed:19737519"
FT MUTAGEN 114
FT /note="E->D: Impairs interaction with MDN1. Blocks
FT progression of the nascent pre-60S subunit and subsequent
FT export to the cytoplasm."
FT /evidence="ECO:0000269|PubMed:19737519"
FT MUTAGEN 448
FT /note="Y->E: Impairs interaction with NSA2."
FT /evidence="ECO:0000269|PubMed:25404745"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:4WJU"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:4WJU"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 117..126
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:4WJU"
FT TURN 173..176
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:4WJU"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:4WJU"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:4WJU"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:4WJU"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 323..330
FT /evidence="ECO:0007829|PDB:4WJU"
FT HELIX 331..336
FT /evidence="ECO:0007829|PDB:4WJU"
FT HELIX 349..364
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:4WJU"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 395..398
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 405..410
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 414..421
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:4WJU"
FT TURN 431..433
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 436..440
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 447..452
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 456..463
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 466..472
FT /evidence="ECO:0007829|PDB:4WJU"
FT TURN 473..476
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 477..483
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 489..494
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 500..505
FT /evidence="ECO:0007829|PDB:4WJU"
FT STRAND 510..514
FT /evidence="ECO:0007829|PDB:4WJU"
SQ SEQUENCE 515 AA; 57026 MW; 04451B0C38FB5318 CRC64;
MSTLIPPPSK KQKKEAQLPR EVAIIPKDLP NVSIKFQALD TGDNVGGALR VPGAISEKQL
EELLNQLNGT SDDPVPYTFS CTIQGKKASD PVKTIDITDN LYSSLIKPGY NSTEDQITLL
YTPRAVFKVK PVTRSSSAIA GHGSTILCSA FAPHTSSRMV TGAGDNTARI WDCDTQTPMH
TLKGHYNWVL CVSWSPDGEV IATGSMDNTI RLWDPKSGQC LGDALRGHSK WITSLSWEPI
HLVKPGSKPR LASSSKDGTI KIWDTVSRVC QYTMSGHTNS VSCVKWGGQG LLYSGSHDRT
VRVWDINSQG RCINILKSHA HWVNHLSLST DYALRIGAFD HTGKKPSTPE EAQKKALENY
EKICKKNGNS EEMMVTASDD YTMFLWNPLK STKPIARMTG HQKLVNHVAF SPDGRYIVSA
SFDNSIKLWD GRDGKFISTF RGHVASVYQV AWSSDCRLLV SCSKDTTLKV WDVRTRKLSV
DLPGHKDEVY TVDWSVDGKR VCSGGKDKMV RLWTH
