NU100_YEAST
ID NU100_YEAST Reviewed; 959 AA.
AC Q02629; D6VXL9;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Nucleoporin NUP100/NSP100;
DE AltName: Full=Nuclear pore protein NUP100/NSP100;
GN Name=NUP100; Synonyms=NSP100; OrderedLocusNames=YKL068W; ORFNames=YKL336;
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].
RX PubMed=1385442; DOI=10.1083/jcb.119.4.705;
RA Wente S.R., Rout M.P., Blobel G.;
RT "A new family of yeast nuclear pore complex proteins.";
RL J. Cell Biol. 119:705-723(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091863; DOI=10.1002/yea.320100009;
RA Rasmussen S.W.;
RT "Sequence of a 20.7 kb region of yeast chromosome XI includes the NUP100
RT gene, an open reading frame (ORF) possibly representing a nucleoside
RT diphosphate kinase gene, tRNAs for His, Val and Trp in addition to seven
RT ORFs with weak or no significant similarity to known proteins.";
RL Yeast 10:S69-S74(1994).
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 MRNA-BINDING MOTIF.
RX PubMed=8044840; DOI=10.1016/0092-8674(94)90297-6;
RA Fabre E., Boelens W.C., Wimmer C., Mattaj I.W., Hurt E.C.;
RT "Nup145p is required for nuclear export of mRNA and binds homopolymeric RNA
RT in vitro via a novel conserved motif.";
RL Cell 78:275-289(1994).
RN [6]
RP FUNCTION, AND INTERACTION WITH KAP95.
RX PubMed=8557738; DOI=10.1083/jcb.131.6.1699;
RA Iovine M.K., Watkins J.L., Wente S.R.;
RT "The GLFG repetitive region of the nucleoporin Nup116p interacts with
RT Kap95p, an essential yeast nuclear import factor.";
RL J. Cell Biol. 131:1699-1713(1995).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10684247; DOI=10.1083/jcb.148.4.635;
RA Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T.;
RT "The yeast nuclear pore complex: composition, architecture, and transport
RT mechanism.";
RL J. Cell Biol. 148:635-651(2000).
RN [8]
RP FUNCTION, AND INTERACTION WITH MEX67.
RX PubMed=11104765; DOI=10.1074/jbc.m008311200;
RA Strawn L.A., Shen T.X., Wente S.R.;
RT "The GLFG regions of Nup116p and Nup100p serve as binding sites for both
RT Kap95p and Mex67p at the nuclear pore complex.";
RL J. Biol. Chem. 276:6445-6452(2001).
RN [9]
RP FUNCTION, AND NUCLEOPORIN INTERACTING PROTEINS.
RX PubMed=11387327; DOI=10.1074/jbc.m102629200;
RA Allen N.P., Huang L., Burlingame A., Rexach M.;
RT "Proteomic analysis of nucleoporin interacting proteins.";
RL J. Biol. Chem. 276:29268-29274(2001).
RN [10]
RP FUNCTION, STRUCTURAL BASIS OF FG REPEAT INTERACTION, AND INTERACTION WITH
RP KAP95.
RX PubMed=12372823; DOI=10.1074/jbc.m209037200;
RA Bayliss R., Littlewood T., Strawn L.A., Wente S.R., Stewart M.;
RT "GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta.";
RL J. Biol. Chem. 277:50597-50606(2002).
RN [11]
RP FUNCTION, AND NUCLEOPORIN INTERACTING PROTEINS.
RX PubMed=12543930; DOI=10.1074/mcp.t200012-mcp200;
RA Allen N.P., Patel S.S., Huang L., Chalkley R.J., Burlingame A.,
RA Lutzmann M., Hurt E.C., Rexach M.;
RT "Deciphering networks of protein interactions at the nuclear pore
RT complex.";
RL Mol. Cell. Proteomics 1:930-946(2002).
RN [12]
RP FUNCTION, AND AFFINITY GRADIENT FOR KARYOPHERIN KAP95.
RX PubMed=12917401; DOI=10.1074/jbc.m307135200;
RA Pyhtila B., Rexach M.;
RT "A gradient of affinity for the karyopherin Kap95p along the yeast nuclear
RT pore complex.";
RL J. Biol. Chem. 278:42699-42709(2003).
RN [13]
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 [14]
RP FUNCTION, AND FG REPEAT STRUCTURE.
RX PubMed=12604785; DOI=10.1073/pnas.0437902100;
RA Denning D.P., Patel S.S., Uversky V., Fink A.L., Rexach M.;
RT "Disorder in the nuclear pore complex: the FG repeat regions of
RT nucleoporins are natively unfolded.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2450-2455(2003).
RN [15]
RP FUNCTION, AND FG REPEATS IN NPC TRANSPORT.
RX PubMed=15039779; DOI=10.1038/ncb1097;
RA Strawn L.A., Shen T.X., Shulga N., Goldfarb D.S., Wente S.R.;
RT "Minimal nuclear pore complexes define FG repeat domains essential for
RT transport.";
RL Nat. Cell Biol. 6:197-206(2004).
RN [16]
RP REVIEW.
RX PubMed=12791264; DOI=10.1016/s1534-5807(03)00162-x;
RA Suntharalingam M., Wente S.R.;
RT "Peering through the pore: nuclear pore complex structure, assembly, and
RT function.";
RL Dev. Cell 4:775-789(2003).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763, AND IDENTIFICATION BY
RP 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, AND IDENTIFICATION BY
RP 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763 AND SER-783, 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).
CC -!- FUNCTION: Functions as a component of the nuclear pore complex (NPC).
CC NPC components, collectively referred to as nucleoporins (NUPs), can
CC play the role of both NPC structural components and of docking or
CC interaction partners for transiently associated nuclear transport
CC factors. Active directional transport is assured by both, a Phe-Gly
CC (FG) repeat affinity gradient for these transport factors across the
CC NPC and a transport cofactor concentration gradient across the nuclear
CC envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in
CC the nucleus, with GDP in the cytoplasm). NUP100 plays an important role
CC in several nuclear export and import pathways including poly(A)+ RNA
CC and protein transport. {ECO:0000269|PubMed:10684247,
CC ECO:0000269|PubMed:11104765, ECO:0000269|PubMed:11387327,
CC ECO:0000269|PubMed:12372823, ECO:0000269|PubMed:12543930,
CC ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:12917401,
CC ECO:0000269|PubMed:15039779, ECO:0000269|PubMed:8044840,
CC ECO:0000269|PubMed:8557738}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC). NPC constitutes
CC the exclusive means of nucleocytoplasmic transport. NPCs allow the
CC passive diffusion of ions and small molecules and the active, nuclear
CC transport receptor-mediated bidirectional transport of macromolecules
CC such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal
CC subunits across the nuclear envelope. Due to its 8-fold rotational
CC symmetry, all subunits are present with 8 copies or multiples thereof.
CC Through its FG repeats NUP100 interacts with numerous karyopherins
CC including KAP95, and MEX67. {ECO:0000269|PubMed:10684247,
CC ECO:0000269|PubMed:11104765, ECO:0000269|PubMed:12372823,
CC ECO:0000269|PubMed:8557738}.
CC -!- INTERACTION:
CC Q02629; Q06142: KAP95; NbExp=6; IntAct=EBI-11698, EBI-9145;
CC Q02629; Q02630: NUP116; NbExp=4; IntAct=EBI-11698, EBI-11703;
CC Q02629; P49686: NUP42; NbExp=2; IntAct=EBI-11698, EBI-12310;
CC Q02629; P48837: NUP57; NbExp=3; IntAct=EBI-11698, EBI-12324;
CC Q02629; P52891: NUP84; NbExp=2; IntAct=EBI-11698, EBI-12337;
CC Q02629; P46673: NUP85; NbExp=4; IntAct=EBI-11698, EBI-12345;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane
CC protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane
CC protein; Nucleoplasmic side. Note=Biased towards cytoplasmic side.
CC -!- DOMAIN: Contains FG repeats. FG repeats are interaction sites for
CC karyopherins (importins, exportins) and form probably an affinity
CC gradient, guiding the transport proteins unidirectionally with their
CC cargo through the NPC. FG repeat regions are highly flexible and lack
CC ordered secondary structure. The overall conservation of FG repeats
CC regarding exact sequence, spacing, and repeat unit length is limited.
CC FG repeat types and their physico-chemical environment change across
CC the NPC from the nucleoplasmic to the cytoplasmic side: GLFG repeats
CC are especially abundant in NUPs in the central region (lacking a
CC charged environment but are enriched in Ser, Thr, Gln, and Asn).
CC -!- MISCELLANEOUS: Present with 358 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the nucleoporin GLFG family. {ECO:0000305}.
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DR EMBL; Z15035; CAA78753.1; -; Genomic_DNA.
DR EMBL; X75780; CAA53406.1; -; Genomic_DNA.
DR EMBL; Z28068; CAA81905.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09089.1; -; Genomic_DNA.
DR PIR; B44402; B44402.
DR RefSeq; NP_012855.1; NM_001179634.1.
DR AlphaFoldDB; Q02629; -.
DR BioGRID; 34065; 146.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-2351N; -.
DR IntAct; Q02629; 31.
DR MINT; Q02629; -.
DR STRING; 4932.YKL068W; -.
DR MEROPS; S59.952; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR iPTMnet; Q02629; -.
DR MaxQB; Q02629; -.
DR PaxDb; Q02629; -.
DR PRIDE; Q02629; -.
DR DNASU; 853796; -.
DR EnsemblFungi; YKL068W_mRNA; YKL068W; YKL068W.
DR GeneID; 853796; -.
DR KEGG; sce:YKL068W; -.
DR SGD; S000001551; NUP100.
DR VEuPathDB; FungiDB:YKL068W; -.
DR eggNOG; KOG0845; Eukaryota.
DR GeneTree; ENSGT00550000074799; -.
DR HOGENOM; CLU_011051_0_0_1; -.
DR InParanoid; Q02629; -.
DR OMA; PMIENEK; -.
DR BioCyc; YEAST:G3O-31864-MON; -.
DR PRO; PR:Q02629; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; Q02629; protein.
DR GO; GO:0005635; C:nuclear envelope; IC:ComplexPortal.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IDA:SGD.
DR GO; GO:0044613; C:nuclear pore central transport channel; IDA:SGD.
DR GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IBA:GO_Central.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IDA:SGD.
DR GO; GO:0006406; P:mRNA export from nucleus; IPI:SGD.
DR GO; GO:0031990; P:mRNA export from nucleus in response to heat stress; IMP:SGD.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IGI:SGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IGI:SGD.
DR GO; GO:0000973; P:post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD.
DR GO; GO:0006606; P:protein import into nucleus; IGI:SGD.
DR GO; GO:0036228; P:protein localization to nuclear inner membrane; IGI:SGD.
DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR DisProt; DP01076; -.
DR Gene3D; 3.30.1610.10; -; 1.
DR InterPro; IPR025574; Nucleoporin_FG_rpt.
DR InterPro; IPR037665; Nucleoporin_S59-like.
DR InterPro; IPR037637; NUP98-NUP96.
DR InterPro; IPR007230; Nup98_auto-Pept-S59_dom.
DR InterPro; IPR036903; Nup98_auto-Pept-S59_dom_sf.
DR PANTHER; PTHR23198; PTHR23198; 1.
DR PANTHER; PTHR23198:SF6; PTHR23198:SF6; 1.
DR Pfam; PF04096; Nucleoporin2; 1.
DR Pfam; PF13634; Nucleoporin_FG; 4.
DR SUPFAM; SSF82215; SSF82215; 1.
DR PROSITE; PS51434; NUP_C; 1.
PE 1: Evidence at protein level;
KW Membrane; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Translocation; Transport.
FT CHAIN 1..959
FT /note="Nucleoporin NUP100/NSP100"
FT /id="PRO_0000204830"
FT REPEAT 2..3
FT /note="FG 1"
FT REPEAT 9..10
FT /note="FG 2"
FT REPEAT 17
FT /note="FG 3"
FT REPEAT 21..24
FT /note="SLFG 1; approximate"
FT REPEAT 33..36
FT /note="SLFG 2"
FT REPEAT 51..54
FT /note="SLFG 3; approximate"
FT REPEAT 66..69
FT /note="SLFG 4"
FT REPEAT 77..80
FT /note="GLFG 1; approximate"
FT REPEAT 89..92
FT /note="SLFG 5; approximate"
FT REPEAT 105..106
FT /note="FG 4"
FT REPEAT 112..115
FT /note="GLFG 2; approximate"
FT REPEAT 131..134
FT /note="SLFG 6; approximate"
FT REPEAT 145..146
FT /note="FG 5"
FT REPEAT 157..160
FT /note="SLFG 7"
FT REPEAT 168..171
FT /note="GLFG 3; approximate"
FT REPEAT 175..178
FT /note="SLFG 8; approximate"
FT REPEAT 189..190
FT /note="FG 6"
FT REPEAT 202..205
FT /note="SLFG 9"
FT REPEAT 210..213
FT /note="SLFG 10; approximate"
FT REPEAT 220..223
FT /note="SLFG 11"
FT REPEAT 233..234
FT /note="FG 7"
FT REPEAT 242..245
FT /note="SLFG 12; approximate"
FT REPEAT 253..256
FT /note="SLFG 13"
FT REPEAT 271..274
FT /note="GLFG 4"
FT REPEAT 287..290
FT /note="GLFG 5"
FT REPEAT 300..303
FT /note="GLFG 6; approximate"
FT REPEAT 318..321
FT /note="SLFG 14"
FT REPEAT 333..336
FT /note="GLFG 7"
FT REPEAT 345..348
FT /note="GLFG 8"
FT REPEAT 358..361
FT /note="GLFG 9"
FT REPEAT 379..382
FT /note="GLFG 10"
FT REPEAT 393..396
FT /note="GLFG 11"
FT REPEAT 405..408
FT /note="SLFG 15"
FT REPEAT 417..420
FT /note="SLFG 16"
FT REPEAT 436..439
FT /note="SLFG 17"
FT REPEAT 448..449
FT /note="FG 8"
FT REPEAT 462..465
FT /note="SLFG 18"
FT REPEAT 474..477
FT /note="SLFG 19; approximate"
FT REPEAT 490..493
FT /note="GLFG 12"
FT REPEAT 506..509
FT /note="GLFG 13"
FT REPEAT 523..526
FT /note="GLFG 14"
FT REPEAT 542..543
FT /note="FG 9"
FT REPEAT 550..553
FT /note="GLFG 15"
FT REPEAT 569..570
FT /note="FG 10"
FT DOMAIN 814..956
FT /note="Peptidase S59"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00765"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..955
FT /note="Nucleoporin RNA-binding motif (NRM)"
FT COMPBIAS 8..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..778
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 763
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 959 AA; 99988 MW; D3985F9901BBAA51 CRC64;
MFGNNRPMFG GSNLSFGSNT SSFGGQQSQQ PNSLFGNSNN NNNSTSNNAQ SGFGGFTSAA
GSNSNSLFGN NNTQNNGAFG QSMGATQNSP FGSLNSSNAS NGNTFGGSSS MGSFGGNTNN
AFNNNSNSTN SPFGFNKPNT GGTLFGSQNN NSAGTSSLFG GQSTSTTGTF GNTGSSFGTG
LNGNGSNIFG AGNNSQSNTT GSLFGNQQSS AFGTNNQQGS LFGQQSQNTN NAFGNQNQLG
GSSFGSKPVG SGSLFGQSNN TLGNTTNNRN GLFGQMNSSN QGSSNSGLFG QNSMNSSTQG
VFGQNNNQMQ INGNNNNSLF GKANTFSNSA SGGLFGQNNQ QQGSGLFGQN SQTSGSSGLF
GQNNQKQPNT FTQSNTGIGL FGQNNNQQQQ STGLFGAKPA GTTGSLFGGN SSTQPNSLFG
TTNVPTSNTQ SQQGNSLFGA TKLTNMPFGG NPTANQSGSG NSLFGTKPAS TTGSLFGNNT
ASTTVPSTNG LFGNNANNST STTNTGLFGA KPDSQSKPAL GGGLFGNSNS NSSTIGQNKP
VFGGTTQNTG LFGATGTNSS AVGSTGKLFG QNNNTLNVGT QNVPPVNNTT QNALLGTTAV
PSLQQAPVTN EQLFSKISIP NSITNPVKAT TSKVNADMKR NSSLTSAYRL APKPLFAPSS
NGDAKFQKWG KTLERSDRGS STSNSITDPE SSYLNSNDLL FDPDRRYLKH LVIKNNKNLN
VINHNDDEAS KVKLVTFTTE SASKDDQASS SIAASKLTEK AHSPQTDLKD DHDESTPDPQ
SKSPNGSTSI PMIENEKISS KVPGLLSNDV TFFKNNYYIS PSIETLGNKS LIELRKINNL
VIGHRNYGKV EFLEPVDLLN TPLDTLCGDL VTFGPKSCSI YENCSIKPEK GEGINVRCRV
TLYSCFPIDK ETRKPIKNIT HPLLKRSIAK LKENPVYKFE SYDPVTGTYS YTIDHPVLT
