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 27-MAR-2024, entry version 197. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 8TIE; EM; 8.10 A; a/l=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 PDBsum; 8TIE; -. DR AlphaFoldDB; P35729; -. DR EMDB; EMD-24231; -. DR EMDB; EMD-24258; -. DR EMDB; EMD-41285; -. DR SMR; P35729; -. DR BioGRID; 34076; 340. 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; 4932-YKL057C; -. DR PeptideAtlas; P35729; -. DR ABCD; P35729; 1 sequenced antibody. DR EnsemblFungi; YKL057C_mRNA; YKL057C; YKL057C. DR GeneID; 853808; -. DR KEGG; sce:YKL057C; -. DR AGR; SGD:S000001540; -. DR SGD; S000001540; NUP120. DR VEuPathDB; FungiDB:YKL057C; -. DR eggNOG; ENOG502QQWQ; Eukaryota. DR HOGENOM; CLU_294409_0_0_1; -. DR InParanoid; P35729; -. DR OMA; ILELYMI; -. DR OrthoDB; 2018920at2759; -. DR BioCyc; YEAST:G3O-31856-MONOMER; -. DR BioGRID-ORCS; 853808; 7 hits in 10 CRISPR screens. 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; NAS: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; NAS:ComplexPortal. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:SGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP: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 formation; 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; NUCLEAR PORE COMPLEX PROTEIN NUP160; 1. DR PANTHER; PTHR21286:SF0; NUCLEAR PORE COMPLEX PROTEIN NUP160; 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 //