NU133_YEAST
ID NU133_YEAST Reviewed; 1157 AA.
AC P36161; D6VXE2;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Nucleoporin NUP133;
DE AltName: Full=Nuclear pore protein NUP133;
GN Name=NUP133; Synonyms=RAT3; OrderedLocusNames=YKR082W; ORFNames=YKR402;
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], AND FUNCTION IN NUCLEAR MRNA EXPORT.
RC STRAIN=JUXJR;
RX PubMed=7813444; DOI=10.1002/j.1460-2075.1994.tb06953.x;
RA Doye V., Wepf R., Hurt E.C.;
RT "A novel nuclear pore protein Nup133p with distinct roles in poly(A)+ RNA
RT transport and nuclear pore distribution.";
RL EMBO J. 13:6062-6075(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8203164; DOI=10.1002/yea.320100210;
RA Garcia-Cantalejo J.M., Baladron V., Esteban P.F., Santos M.A., Bou G.,
RA Remacha M.A., Revuelta J.L., Ballesta J.P.G., Jimenez A., del Rey F.;
RT "The complete sequence of an 18,002 bp segment of Saccharomyces cerevisiae
RT chromosome XI contains the HBS1, MRP-L20 and PRP16 genes, and six new open
RT reading frames.";
RL Yeast 10:231-245(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 NPC ASSEMBLY AND DISTRIBUTION.
RX PubMed=7862658; DOI=10.1073/pnas.92.4.1187;
RA Pemberton L.F., Rout M.P., Blobel G.;
RT "Disruption of the nucleoporin gene NUP133 results in clustering of nuclear
RT pore complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:1187-1191(1995).
RN [6]
RP FUNCTION, AND NUCLEAR TRNA EXPORT.
RX PubMed=8524308; DOI=10.1128/mcb.16.1.294;
RA Sharma K., Fabre E., Tekotte H., Hurt E.C., Tollervey D.;
RT "Yeast nucleoporin mutants are defective in pre-tRNA splicing.";
RL Mol. Cell. Biol. 16:294-301(1996).
RN [7]
RP FUNCTION, AND NUP133 N-TERMINUS IN NPC DISTRIBUTION.
RX PubMed=9049242; DOI=10.1083/jcb.136.4.747;
RA Belgareh N., Doye V.;
RT "Dynamics of nuclear pore distribution in nucleoporin mutant yeast cells.";
RL J. Cell Biol. 136:747-759(1997).
RN [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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. NUP133 is involved in nuclear poly(A)+ RNA, tRNA and pre-
CC ribosome export, in GSP1 nuclear import, in NPC assembly and
CC distribution, as well as in nuclear envelope organization.
CC {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11071906,
CC ECO:0000269|PubMed:11823431, ECO:0000269|PubMed:12730220,
CC ECO:0000269|PubMed:7813444, ECO:0000269|PubMed:7862658,
CC ECO:0000269|PubMed:8524308, ECO:0000269|PubMed:9049242}.
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 NUP133 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 P36161; P35729: NUP120; NbExp=6; IntAct=EBI-11722, EBI-11713;
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 -!- DOMAIN: Usually mRNA binding pumilio repeats come in 8 copies. In the
CC 8-fold symmetry of the NPC the 8 repeats may be provided by eight
CC copies of NUP133.
CC -!- MISCELLANEOUS: Present with 3060 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the nucleoporin Nup133 family. {ECO:0000305}.
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DR EMBL; X80066; CAA56372.1; -; Genomic_DNA.
DR EMBL; Z27116; CAA81633.1; -; Genomic_DNA.
DR EMBL; Z28307; CAA82161.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09232.1; -; Genomic_DNA.
DR PIR; S38160; S38160.
DR RefSeq; NP_013008.3; NM_001179872.3.
DR PDB; 3KFO; X-ray; 1.90 A; A=881-1157.
DR PDB; 6X02; X-ray; 6.38 A; B=521-1157.
DR PDB; 6X03; X-ray; 7.30 A; B=521-1157.
DR PDB; 6X04; X-ray; 2.68 A; A/C/E/G/I/K=55-481.
DR PDB; 6X05; X-ray; 2.10 A; A=55-481.
DR PDB; 7N84; EM; 11.60 A; g/r=1-1157.
DR PDB; 7N9F; EM; 37.00 A; g/n=1-1157.
DR PDBsum; 3KFO; -.
DR PDBsum; 6X02; -.
DR PDBsum; 6X03; -.
DR PDBsum; 6X04; -.
DR PDBsum; 6X05; -.
DR PDBsum; 7N84; -.
DR PDBsum; 7N9F; -.
DR AlphaFoldDB; P36161; -.
DR SMR; P36161; -.
DR BioGRID; 34213; 558.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-2428N; -.
DR IntAct; P36161; 14.
DR MINT; P36161; -.
DR STRING; 4932.YKR082W; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR iPTMnet; P36161; -.
DR MaxQB; P36161; -.
DR PaxDb; P36161; -.
DR PRIDE; P36161; -.
DR DNASU; 853957; -.
DR EnsemblFungi; YKR082W_mRNA; YKR082W; YKR082W.
DR GeneID; 853957; -.
DR KEGG; sce:YKR082W; -.
DR SGD; S000001790; NUP133.
DR VEuPathDB; FungiDB:YKR082W; -.
DR eggNOG; KOG4121; Eukaryota.
DR GeneTree; ENSGT00390000011529; -.
DR HOGENOM; CLU_274661_0_0_1; -.
DR InParanoid; P36161; -.
DR OMA; EHIIPWI; -.
DR BioCyc; YEAST:G3O-32045-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; P36161; -.
DR PRO; PR:P36161; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36161; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
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:0005634; C:nucleus; IDA:SGD.
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: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:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
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:0006606; P:protein import into nucleus; IMP:SGD.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IDA:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR GO; GO:0034398; P:telomere tethering at nuclear periphery; IMP:SGD.
DR GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IBA:GO_Central.
DR GO; GO:0006409; P:tRNA export from nucleus; IMP:SGD.
DR DisProt; DP02158; -.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR014908; Nucleoporin_Nup133/Nup155_N.
DR InterPro; IPR037624; Nup133-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR13405; PTHR13405; 1.
DR Pfam; PF08801; Nucleoporin_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Membrane; mRNA transport; Nuclear pore complex;
KW Nucleus; Protein transport; Reference proteome; Translocation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1157
FT /note="Nucleoporin NUP133"
FT /id="PRO_0000204841"
FT REGION 44..236
FT /note="Required for normal NPC distribution"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:6X05"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:6X05"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:6X05"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:6X05"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:6X05"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:6X05"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:6X05"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:6X04"
FT STRAND 240..247
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 267..277
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 280..287
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 291..301
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 305..311
FT /evidence="ECO:0007829|PDB:6X05"
FT HELIX 313..320
FT /evidence="ECO:0007829|PDB:6X05"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:6X05"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:6X05"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 342..353
FT /evidence="ECO:0007829|PDB:6X05"
FT TURN 354..357
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 358..369
FT /evidence="ECO:0007829|PDB:6X05"
FT TURN 370..373
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 374..382
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:6X05"
FT HELIX 402..405
FT /evidence="ECO:0007829|PDB:6X04"
FT STRAND 413..420
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 423..430
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 437..440
FT /evidence="ECO:0007829|PDB:6X04"
FT STRAND 442..448
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 455..460
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 462..469
FT /evidence="ECO:0007829|PDB:6X05"
FT TURN 470..472
FT /evidence="ECO:0007829|PDB:6X05"
FT STRAND 473..479
FT /evidence="ECO:0007829|PDB:6X05"
FT HELIX 951..965
FT /evidence="ECO:0007829|PDB:3KFO"
FT HELIX 973..975
FT /evidence="ECO:0007829|PDB:3KFO"
FT HELIX 978..992
FT /evidence="ECO:0007829|PDB:3KFO"
FT STRAND 993..995
FT /evidence="ECO:0007829|PDB:3KFO"
FT HELIX 999..1006
FT /evidence="ECO:0007829|PDB:3KFO"
FT HELIX 1012..1025
FT /evidence="ECO:0007829|PDB:3KFO"
FT HELIX 1026..1028
FT /evidence="ECO:0007829|PDB:3KFO"
FT HELIX 1031..1049
FT /evidence="ECO:0007829|PDB:3KFO"
FT HELIX 1056..1067
FT /evidence="ECO:0007829|PDB:3KFO"
FT HELIX 1070..1073
FT /evidence="ECO:0007829|PDB:3KFO"
FT HELIX 1081..1084
FT /evidence="ECO:0007829|PDB:3KFO"
FT HELIX 1087..1089
FT /evidence="ECO:0007829|PDB:3KFO"
FT HELIX 1092..1099
FT /evidence="ECO:0007829|PDB:3KFO"
FT STRAND 1102..1104
FT /evidence="ECO:0007829|PDB:3KFO"
FT HELIX 1106..1123
FT /evidence="ECO:0007829|PDB:3KFO"
FT HELIX 1124..1127
FT /evidence="ECO:0007829|PDB:3KFO"
FT HELIX 1128..1141
FT /evidence="ECO:0007829|PDB:3KFO"
FT STRAND 1144..1149
FT /evidence="ECO:0007829|PDB:3KFO"
FT TURN 1150..1153
FT /evidence="ECO:0007829|PDB:3KFO"
FT STRAND 1154..1157
FT /evidence="ECO:0007829|PDB:3KFO"
SQ SEQUENCE 1157 AA; 133321 MW; C8BDBB7D709C5C08 CRC64;
MSEKKVHLRL RKELSVPIAV VENESLAQLS YEEESQASLM DISMEQQQLR LHSHFDNSKV
FTENNRYIVK TLQTDYSSGF SNDDELNGYI DMQIGYGLVN DHKKVYIWNI HSTQKDTPYI
TVPFRSDDND EIAVAPRCIL TFPATMDESP LALNPNDQDE TGGLIIIKGS KAIYYEDINS
INNLNFKLSE KFSHELELPI NSSGGEKCDL MLNCEPAGIV LSTNMGRIFF ITIRNSMGKP
QLKLGKLLNK PFKLGIWSKI FNTNSSVVSL RNGPILGKGT RLVYITTNKG IFQTWQLSAT
NSHPTKLIDV NIYEAILESL QDLYPFAHGT LKIWDSHPLQ DESSQLFLSS IYDSSCNETY
YILSTIIFDS SSNSFTIFST YRLNTFMESI TDTKFKPKIF IPQMENANDT NEVTSILVMF
PNAVVITQVN SKLDSSYSMR RKWEDIVSLR NDIDIIGSGY DSKSLYVLTK QMGVLQFFVK
ENEETNSKPE VGFVKSHVDQ AVYFSKINAN PIDFNLPPEI SLDQESIEHD LKLTSEEIFH
SNGKYIPPML NTLGQHLSVR KEFFQNFLTF VAKNFNYKIS PELKLDLIEK FEILNCCIKF
NSIIRQSDVL NDIWEKTLSN YNLTQNEHLT TKTVVINSPD VFPVIFKQFL NHVVFVLFPS
QNQNFKLNVT NLINLCFYDG ILEEGEKTIR YELLELDPME VDTSKLPWFI NFDYLNCINQ
CFFDFTFACE EEGSLDSYKE GLLKIVKILY YQFNQFKIWI NTQPVKSVNA NDNFININNL
YDDNHLDWNH VLCKVNLKEQ CIQIAEFYKD LSGLVQTLQT LDQNDSTTVS LYETFFNEFP
KEFSFTLFEY LIKHKKLNDL IFRFPQQHDV LIQFFQESAP KYGHVAWIQQ ILDGSYADAM
NTLKNITVDD SKKGESLSEC ELHLNVAKLS SLLVEKDNLD INTLRKIQYN LDTIDAEKNI
SNKLKKGEVQ ICKRFKNGSI REVFNILVEE LKSTTVVNLS DLVELYSMLD DEESLFIPLR
LLSVDGNLLN FEVKKFLNAL VWRRIVLLNA SNEGDKLLQH IVKRVFDEEL PKNNDFPLPS
VDLLCDKSLL TPEYISETYG RFPIDQNAIR EEIYEEISQV ETLNSDNSLE IKLHSTIGSV
AKEKNYTINY ETNTVEY
