NU120_YEAST
ID NU120_YEAST Reviewed; 1037 AA.
AC P35729; D6VXN0; P35730;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Nucleoporin NUP120;
DE AltName: Full=Nuclear pore protein NUP120;
GN Name=NUP120; Synonyms=RAT2; OrderedLocusNames=YKL057C;
GN ORFNames=YKL313, YKL314;
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=8091862; DOI=10.1002/yea.320100008;
RA Rasmussen S.W.;
RT "Sequence of a 28.6 kb region of yeast chromosome XI includes the FBA1 and
RT TOA2 genes, an open reading frame (ORF) similar to a translationally
RT controlled tumour protein, one ORF containing motifs also found in plant
RT storage proteins and 13 ORFs with weak or no homology to known proteins.";
RL Yeast 10:S63-S68(1994).
RN [2]
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 [3]
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 [4]
RP PROTEIN SEQUENCE OF 189-206 AND 800-807, CHARACTERIZATION, AND NUCLEAR MRNA
RP EXPORT.
RX PubMed=8557736; DOI=10.1083/jcb.131.6.1659;
RA Aitchison J.D., Blobel G., Rout M.P.;
RT "Nup120p: a yeast nucleoporin required for NPC distribution and mRNA
RT transport.";
RL J. Cell Biol. 131:1659-1676(1995).
RN [5]
RP FUNCTION, AND NPC ASSEMBLY AND DISTRIBUTION.
RX PubMed=8557737; DOI=10.1083/jcb.131.6.1677;
RA Heath C.V., Copeland C.S., Amberg D.C., Del Priore V., Snyder M.,
RA Cole C.N.;
RT "Nuclear pore complex clustering and nuclear accumulation of poly(A)+ RNA
RT associated with mutation of the Saccharomyces cerevisiae RAT2/NUP120
RT gene.";
RL J. Cell Biol. 131:1677-1697(1995).
RN [6]
RP FUNCTION, AND NUCLEAR ENVELOPE ORGANIZATION.
RX PubMed=8565072; DOI=10.1016/s0092-8674(00)80981-2;
RA Siniossoglou S., Wimmer C., Rieger M., Doye V., Tekotte H., Weise C.,
RA Emig S., Segref A., Hurt E.C.;
RT "A novel complex of nucleoporins, which includes Sec13p and a Sec13p
RT homolog, is essential for normal nuclear pores.";
RL Cell 84:265-275(1996).
RN [7]
RP FUNCTION, AND PRE-RIBOSOME EXPORT.
RX PubMed=11071906; DOI=10.1091/mbc.11.11.3777;
RA Stage-Zimmermann T., Schmidt U., Silver P.A.;
RT "Factors affecting nuclear export of the 60S ribosomal subunit in vivo.";
RL Mol. Biol. Cell 11:3777-3789(2000).
RN [8]
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 [9]
RP FUNCTION, AND NUP84 NPC SUBCOMPLEX ASSEMBLY/STRUCTURE.
RX PubMed=11823431; DOI=10.1093/emboj/21.3.387;
RA Lutzmann M., Kunze R., Buerer A., Aebi U., Hurt E.C.;
RT "Modular self-assembly of a Y-shaped multiprotein complex from seven
RT nucleoporins.";
RL EMBO J. 21:387-397(2002).
RN [10]
RP FUNCTION, AND NUCLEAR GSP1 IMPORT.
RX PubMed=12730220; DOI=10.1074/jbc.m301607200;
RA Gao H., Sumanaweera N., Bailer S.M., Stochaj U.;
RT "Nuclear accumulation of the small GTPase Gsp1p depends on nucleoporins
RT Nup133p, Rat2p/Nup120p, Nup85p, Nic96p, and the acetyl-CoA carboxylase
RT Acc1p.";
RL J. Biol. Chem. 278:25331-25340(2003).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-417, 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).
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. NUP120 is involved in nuclear poly(A)+ RNA and pre-ribosome
CC export, in GSP1 nuclear import, in NPC assembly and distribution, as
CC well as in nuclear envelope organization. {ECO:0000269|PubMed:10684247,
CC ECO:0000269|PubMed:11071906, ECO:0000269|PubMed:11823431,
CC ECO:0000269|PubMed:12730220, ECO:0000269|PubMed:8557737,
CC ECO:0000269|PubMed:8565072}.
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 NUP120 is part of the heptameric 0.5 MDa autoassembling NUP84 NPC
CC subcomplex (NUP84, NUP85, NUP120, NUP133, NUP145C, SEC13 and SEH1).
CC {ECO:0000269|PubMed:10684247}.
CC -!- INTERACTION:
CC P35729; P35729: NUP120; NbExp=4; IntAct=EBI-11713, EBI-11713;
CC P35729; P36161: NUP133; NbExp=6; IntAct=EBI-11713, EBI-11722;
CC P35729; P49687: NUP145; NbExp=23; IntAct=EBI-11713, EBI-11730;
CC P35729; P52891: NUP84; NbExp=12; IntAct=EBI-11713, EBI-12337;
CC P35729; P46673: NUP85; NbExp=21; IntAct=EBI-11713, 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=Symmetric distribution.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA53415.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X75781; CAA53414.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X75781; CAA53415.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z28057; CAA81894.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09100.1; -; Genomic_DNA.
DR PIR; S37879; S37879.
DR RefSeq; NP_012866.1; NM_001179623.1.
DR PDB; 3F7F; X-ray; 2.60 A; A/B/C/D=1-729.
DR PDB; 3H7N; X-ray; 3.00 A; A/B/C/D=1-729.
DR PDB; 3HXR; X-ray; 3.00 A; A=1-757.
DR PDB; 4XMM; X-ray; 7.38 A; E=2-1037.
DR PDB; 4XMN; X-ray; 7.60 A; E=1-1037.
DR PDB; 6X06; X-ray; 4.27 A; A=1-757.
DR PDB; 7N84; EM; 11.60 A; a/l=1-1037.
DR PDB; 7N9F; EM; 37.00 A; a/h=1-1037.
DR PDBsum; 3F7F; -.
DR PDBsum; 3H7N; -.
DR PDBsum; 3HXR; -.
DR PDBsum; 4XMM; -.
DR PDBsum; 4XMN; -.
DR PDBsum; 6X06; -.
DR PDBsum; 7N84; -.
DR PDBsum; 7N9F; -.
DR AlphaFoldDB; P35729; -.
DR SMR; P35729; -.
DR BioGRID; 34076; 336.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-2721N; -.
DR IntAct; P35729; 20.
DR MINT; P35729; -.
DR STRING; 4932.YKL057C; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR iPTMnet; P35729; -.
DR MaxQB; P35729; -.
DR PaxDb; P35729; -.
DR PRIDE; P35729; -.
DR ABCD; P35729; 1 sequenced antibody.
DR EnsemblFungi; YKL057C_mRNA; YKL057C; YKL057C.
DR GeneID; 853808; -.
DR KEGG; sce:YKL057C; -.
DR SGD; S000001540; NUP120.
DR VEuPathDB; FungiDB:YKL057C; -.
DR eggNOG; ENOG502QQWQ; Eukaryota.
DR HOGENOM; CLU_294409_0_0_1; -.
DR InParanoid; P35729; -.
DR OMA; NEWERFA; -.
DR BioCyc; YEAST:G3O-31856-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 EvolutionaryTrace; P35729; -.
DR PRO; PR:P35729; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P35729; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
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:0031080; C:nuclear pore outer ring; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IMP:SGD.
DR GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:SGD.
DR GO; GO:0031990; P:mRNA export from nucleus in response to heat stress; IMP:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0051664; P:nuclear pore localization; IMP:SGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:SGD.
DR GO; GO:0000973; P:post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD.
DR GO; GO:0006611; P:protein export from nucleus; IMP:SGD.
DR GO; GO:0006606; P:protein import into nucleus; IMP:SGD.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR GO; GO:0034398; P:telomere tethering at nuclear periphery; IMP:SGD.
DR DisProt; DP02157; -.
DR InterPro; IPR021717; Nucleoporin_Nup160.
DR PANTHER; PTHR21286; PTHR21286; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Direct protein sequencing; Membrane;
KW mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..1037
FT /note="Nucleoporin NUP120"
FT /id="PRO_0000204836"
FT REGION 131..152
FT /note="Leucine-zipper 1"
FT /evidence="ECO:0000255"
FT REGION 290..311
FT /note="Leucine-zipper 2"
FT /evidence="ECO:0000255"
FT MOD_RES 417
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:3F7F"
FT TURN 11..14
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3HXR"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:3F7F"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:3F7F"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:3H7N"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 114..126
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:3F7F"
FT HELIX 135..139
FT /evidence="ECO:0007829|PDB:3F7F"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 170..178
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:3HXR"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:3HXR"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:3F7F"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:3H7N"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:3F7F"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:3F7F"
FT TURN 248..251
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 252..258
FT /evidence="ECO:0007829|PDB:3F7F"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 280..291
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 297..304
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:3H7N"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:3F7F"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 330..338
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:3HXR"
FT STRAND 348..357
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 360..368
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 375..381
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:3HXR"
FT HELIX 386..392
FT /evidence="ECO:0007829|PDB:3F7F"
FT HELIX 406..415
FT /evidence="ECO:0007829|PDB:3F7F"
FT HELIX 417..428
FT /evidence="ECO:0007829|PDB:3F7F"
FT TURN 429..431
FT /evidence="ECO:0007829|PDB:3F7F"
FT HELIX 440..457
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 460..466
FT /evidence="ECO:0007829|PDB:3F7F"
FT TURN 467..469
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 470..477
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 480..486
FT /evidence="ECO:0007829|PDB:3F7F"
FT HELIX 489..494
FT /evidence="ECO:0007829|PDB:3F7F"
FT TURN 495..499
FT /evidence="ECO:0007829|PDB:3F7F"
FT HELIX 505..517
FT /evidence="ECO:0007829|PDB:3F7F"
FT HELIX 522..537
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 538..540
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:3H7N"
FT HELIX 546..557
FT /evidence="ECO:0007829|PDB:3F7F"
FT TURN 558..560
FT /evidence="ECO:0007829|PDB:3F7F"
FT HELIX 564..574
FT /evidence="ECO:0007829|PDB:3F7F"
FT HELIX 579..588
FT /evidence="ECO:0007829|PDB:3F7F"
FT TURN 589..591
FT /evidence="ECO:0007829|PDB:3F7F"
FT HELIX 609..639
FT /evidence="ECO:0007829|PDB:3F7F"
FT TURN 644..647
FT /evidence="ECO:0007829|PDB:3F7F"
FT HELIX 648..670
FT /evidence="ECO:0007829|PDB:3F7F"
FT HELIX 672..680
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 681..684
FT /evidence="ECO:0007829|PDB:3F7F"
FT STRAND 685..688
FT /evidence="ECO:0007829|PDB:3HXR"
FT HELIX 695..711
FT /evidence="ECO:0007829|PDB:3F7F"
FT HELIX 719..728
FT /evidence="ECO:0007829|PDB:3F7F"
SQ SEQUENCE 1037 AA; 120448 MW; D4655E6116C54503 CRC64;
MACLSRIDAN LLQYYEKPEP NNTVDLYVSN NSNNNGLKEG DKSISTPVPQ PYGSEYSNCL
LLSNSEYICY HFSSRSTLLT FYPLSDAYHG KTINIHLPNA SMNQRYTLTI QEVEQQLLVN
VILKDGSFLT LQLPLSFLFS SANTLNGEWF HLQNPYDFTV RVPHFLFYVS PQFSVVFLED
GGLLGLKKVD GVHYEPLLFN DNSYLKSLTR FFSRSSKSDY DSVISCKLFH ERYLIVLTQN
CHLKIWDLTS FTLIQDYDMV SQSDSDPSHF RKVEAVGEYL SLYNNTLVTL LPLENGLFQM
GTLLVDSSGI LTYTFQNNIP TNLSASAIWS IVDLVLTRPL ELNVEASYLN LIVLWKSGTA
SKLQILNVND ESFKNYEWIE SVNKSLVDLQ SEHDLDIVTK TGDVERGFCN LKSRYGTQIF
ERAQQILSEN KIIMAHNEDE EYLANLETIL RDVKTAFNEA SSITLYGDEI ILVNCFQPYN
HSLYKLNTTV ENWFYNMHSE TDGSELFKYL RTLNGFASTL SNDVLRSISK KFLDIITGEL
PDSMTTVEKF TDIFKNCLEN QFEITNLKIL FDELNSFDIP VVLNDLINNQ MKPGIFWKKD
FISAIKFDGF TSIISLESLH QLLSIHYRIT LQVLLTFVLF DLDTEIFGQH ISTLLDLHYK
QFLLLNLYRQ DKCLLAEVLL KDSSEFSFGV KFFNYGQLIA YIDSLNSNVY NASITENSFF
MTFFRSYIIE NTSHKNIRFF LENVECPFYL RHNEVQEFMF AMTLFSCGNF DQSYEIFQLH
DYPEAINDKL PTFLEDLKSE NYHGDSIWKD LLCTFTVPYR HSAFYYQLSL LFDRNNSQEF
ALKCISKSAE YSLKEIQIEE LQDFKEKQHI HYLNLLIHFR MFEEVLDVLR LGHECLSDTV
RTNFLQLLLQ EDIYSRDFFS TLLRLCNAHS DNGELYLRTV DIKIVDSILS QNLRSGDWEC
FKKLYCFRML NKSERAAAEV LYQYILMQAD LDVIRKRKCY LMVINVLSSF DSAYDQWILN
GSKVVTLTDL RDELRGL
