NIC96_YEAST
ID NIC96_YEAST Reviewed; 839 AA.
AC P34077; D6VTN2;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Nucleoporin NIC96;
DE AltName: Full=96 kDa nucleoporin-interacting component;
DE AltName: Full=Nuclear pore protein NIC96;
GN Name=NIC96; OrderedLocusNames=YFR002W;
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 PARTIAL PROTEIN SEQUENCE.
RX PubMed=7688296; DOI=10.1002/j.1460-2075.1993.tb05975.x;
RA Grandi P., Doye V., Hurt E.C.;
RT "Purification of NSP1 reveals complex formation with 'GLFG' nucleoporins
RT and a novel nuclear pore protein NIC96.";
RL EMBO J. 12:3061-3071(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-591.
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8789262;
RX DOI=10.1002/(sici)1097-0061(199601)12:1<77::aid-yea887>3.0.co;2-5;
RA Naitou M., Ozawa M., Sasanuma S., Kobayashi M., Hagiwara H., Shibata T.,
RA Hanaoka F., Watanabe K., Ono A., Yamazaki M., Tashiro H., Eki T.,
RA Murakami Y.;
RT "Sequencing of a 23 kb fragment from Saccharomyces cerevisiae chromosome
RT VI.";
RL Yeast 12:77-84(1996).
RN [5]
RP PROTEIN SEQUENCE OF 104-116 AND 277-291.
RX PubMed=8522578; DOI=10.1083/jcb.131.5.1133;
RA Aitchison J.D., Rout M.P., Marelli M., Blobel G., Wozniak R.W.;
RT "Two novel related yeast nucleoporins Nup170p and Nup157p: complementation
RT with the vertebrate homologue Nup155p and functional interactions with the
RT yeast nuclear pore-membrane protein Pom152p.";
RL J. Cell Biol. 131:1133-1148(1995).
RN [6]
RP FUNCTION, AND HEPTAD REPEAT DEPENDENT INTERACTION WITH NSP1.
RX PubMed=7828598; DOI=10.1002/j.1460-2075.1995.tb06977.x;
RA Grandi P., Schlaich N.L., Tekotte H., Hurt E.C.;
RT "Functional interaction of Nic96p with a core nucleoporin complex
RT consisting of Nsp1p, Nup49p and a novel protein Nup57p.";
RL EMBO J. 14:76-87(1995).
RN [7]
RP INTERACTION WITH NUP188.
RX PubMed=8682854; DOI=10.1083/jcb.133.6.1141;
RA Zabel U., Doye V., Tekotte H., Wepf R., Grandi P., Hurt E.C.;
RT "Nic96p is required for nuclear pore formation and functionally interacts
RT with a novel nucleoporin, Nup188p.";
RL J. Cell Biol. 133:1141-1152(1996).
RN [8]
RP FUNCTION, AND INTERACTION WITH NUP188.
RX PubMed=8682855; DOI=10.1083/jcb.133.6.1153;
RA Nehrbass U., Rout M.P., Maguire S., Blobel G., Wozniak R.W.;
RT "The yeast nucleoporin Nup188p interacts genetically and physically with
RT the core structures of the nuclear pore complex.";
RL J. Cell Biol. 133:1153-1162(1996).
RN [9]
RP FUNCTION, AND INTERACTION WITH NUP57 SUBCOMPLEX.
RX PubMed=9017593; DOI=10.1091/mbc.8.1.33;
RA Schlaich N.L., Haener M., Lustig A., Aebi U., Hurt E.C.;
RT "In vitro reconstitution of a heterotrimeric nucleoporin complex consisting
RT of recombinant Nsp1p, Nup49p, and Nup57p.";
RL Mol. Biol. Cell 8:33-46(1997).
RN [10]
RP FUNCTION, AND INTERACTION WITH NUP192.
RX PubMed=10428845; DOI=10.1074/jbc.274.32.22646;
RA Kosova B., Pante N., Rollenhagen C., Hurt E.C.;
RT "Nup192p is a conserved nucleoporin with a preferential location at the
RT inner site of the nuclear membrane.";
RL J. Biol. Chem. 274:22646-22651(1999).
RN [11]
RP FUNCTION, AND INTERACTION WITH MLP2.
RX PubMed=10617624; DOI=10.1074/jbc.275.1.343;
RA Kosova B., Pante N., Rollenhagen C., Podtelejnikov A., Mann M., Aebi U.,
RA Hurt E.C.;
RT "Mlp2p, a component of nuclear pore attached intranuclear filaments,
RT associates with nic96p.";
RL J. Biol. Chem. 275:343-350(2000).
RN [12]
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 [13]
RP FUNCTION, AND NPC DE NOVO ASSEMBLY.
RX PubMed=11121302; DOI=10.1006/jsbi.2000.4305;
RA Gomez-Ospina N., Morgan G., Giddings T.H. Jr., Kosova B., Hurt E.C.,
RA Winey M.;
RT "Yeast nuclear pore complex assembly defects determined by nuclear envelope
RT reconstruction.";
RL J. Struct. Biol. 132:1-5(2000).
RN [14]
RP FUNCTION, AND LOCATION WITHIN THE NPC.
RX PubMed=10806080; DOI=10.1006/jsbi.2000.4223;
RA Fahrenkrog B., Aris J.P., Hurt E.C., Pante N., Aebi U.;
RT "Comparative spatial localization of protein-A-tagged and authentic yeast
RT nuclear pore complex proteins by immunogold electron microscopy.";
RL J. Struct. Biol. 129:295-305(2000).
RN [15]
RP FUNCTION, AND INTERACTION WITH NSP1 COILED-COIL DOMAIN.
RX PubMed=11689687; DOI=10.1128/mcb.21.23.7944-7955.2001;
RA Bailer S.M., Balduf C., Hurt E.C.;
RT "The Nsp1p carboxy-terminal domain is organized into functionally distinct
RT coiled-coil regions required for assembly of nucleoporin subcomplexes and
RT nucleocytoplasmic transport.";
RL Mol. Cell. Biol. 21:7944-7955(2001).
RN [16]
RP FUNCTION, AND INTERACTION WITH NUP53.
RX PubMed=12403813; DOI=10.1083/jcb.200203079;
RA Lusk C.P., Makhnevych T., Marelli M., Aitchison J.D., Wozniak R.W.;
RT "Karyopherins in nuclear pore biogenesis: a role for Kap121p in the
RT assembly of Nup53p into nuclear pore complexes.";
RL J. Cell Biol. 159:267-278(2002).
RN [17]
RP FUNCTION, AND INTERACTION WITH NUP53 AND NUP120.
RX PubMed=12496130; DOI=10.1016/s0006-3495(02)75363-0;
RA Damelin M., Silver P.A.;
RT "In situ analysis of spatial relationships between proteins of the nuclear
RT pore complex.";
RL Biophys. J. 83:3626-3636(2002).
RN [18]
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 [19]
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 [20]
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 [21]
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).
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. NIC96, which is localized to the core of the NPC and the
CC distal ring of the nuclear basket, is required for de novo assembly of
CC NPCs. It is involved in nuclear GSP1 import.
CC {ECO:0000269|PubMed:10428845, ECO:0000269|PubMed:10617624,
CC ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:10806080,
CC ECO:0000269|PubMed:11121302, ECO:0000269|PubMed:11689687,
CC ECO:0000269|PubMed:12403813, ECO:0000269|PubMed:12496130,
CC ECO:0000269|PubMed:12730220, ECO:0000269|PubMed:7828598,
CC ECO:0000269|PubMed:8682855, ECO:0000269|PubMed:9017593}.
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 NIC96 is part of three NPC subcomplexes, interacting with NSP1 of the
CC NUP57 subcomplex (NIC96, NSP1, NUP49, NUP57), with NUP120 of the NUP84
CC subcomplex (SEH1, NUP85, NUP120, NUP145C, SEC13, NUP84, NUP133), and
CC with NUP53 of the NUP53-NUP59-NUP170 subcomplex. The interaction with
CC NUP53 is cell cycle dependent. NIC96 is also associated with the distal
CC ring of the nuclear basket and interacts here with MLP2, which forms
CC together with MLP1 nuclear pore-attached intranuclear filaments.
CC {ECO:0000269|PubMed:10428845, ECO:0000269|PubMed:10617624,
CC ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11689687,
CC ECO:0000269|PubMed:12403813, ECO:0000269|PubMed:12496130,
CC ECO:0000269|PubMed:8682854, ECO:0000269|PubMed:8682855,
CC ECO:0000269|PubMed:9017593}.
CC -!- INTERACTION:
CC P34077; P47054: NUP192; NbExp=3; IntAct=EBI-12056, EBI-25846;
CC P34077; Q02199: NUP49; NbExp=3; IntAct=EBI-12056, EBI-12315;
CC P34077; Q03790: NUP53; NbExp=3; IntAct=EBI-12056, EBI-27321;
CC P34077; P48837: NUP57; NbExp=5; IntAct=EBI-12056, EBI-12324;
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 -!- MISCELLANEOUS: Present with 15500 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the nucleoporin interacting component (NIC)
CC family. {ECO:0000305}.
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DR EMBL; X72923; CAA51427.1; -; Genomic_DNA.
DR EMBL; D50617; BAA09241.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12442.1; -; Genomic_DNA.
DR PIR; S35319; S35319.
DR RefSeq; NP_116657.1; NM_001179967.1.
DR PDB; 2QX5; X-ray; 2.50 A; A/B=186-839.
DR PDB; 2RFO; X-ray; 2.60 A; A/B=189-839.
DR PDB; 6X07; X-ray; 2.10 A; A=186-839.
DR PDB; 7N85; EM; 7.60 A; Q/R/S/T=1-839.
DR PDB; 7N9F; EM; 37.00 A; Q/R/S/T=1-839.
DR PDB; 7WOO; EM; 3.71 A; A/Z=1-839.
DR PDB; 7WOT; EM; 3.73 A; A/M/N/Z=1-839.
DR PDBsum; 2QX5; -.
DR PDBsum; 2RFO; -.
DR PDBsum; 6X07; -.
DR PDBsum; 7N85; -.
DR PDBsum; 7N9F; -.
DR PDBsum; 7WOO; -.
DR PDBsum; 7WOT; -.
DR AlphaFoldDB; P34077; -.
DR SMR; P34077; -.
DR BioGRID; 31150; 90.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-745N; -.
DR IntAct; P34077; 31.
DR MINT; P34077; -.
DR STRING; 4932.YFR002W; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR iPTMnet; P34077; -.
DR MaxQB; P34077; -.
DR PaxDb; P34077; -.
DR PRIDE; P34077; -.
DR EnsemblFungi; YFR002W_mRNA; YFR002W; YFR002W.
DR GeneID; 850552; -.
DR KEGG; sce:YFR002W; -.
DR SGD; S000001898; NIC96.
DR VEuPathDB; FungiDB:YFR002W; -.
DR eggNOG; KOG2168; Eukaryota.
DR GeneTree; ENSGT00390000016353; -.
DR HOGENOM; CLU_011846_0_0_1; -.
DR InParanoid; P34077; -.
DR OMA; LLMCGQF; -.
DR BioCyc; YEAST:G3O-30455-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; P34077; -.
DR PRO; PR:P34077; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P34077; 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:0044612; C:nuclear pore linkers; IDA:SGD.
DR GO; GO:0044615; C:nuclear pore nuclear basket; IDA:SGD.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IMP:SGD.
DR GO; GO:0006999; P:nuclear pore organization; IMP:SGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
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 InterPro; IPR007231; Nucleoporin_int_Nup93/Nic96.
DR PANTHER; PTHR11225; PTHR11225; 1.
DR Pfam; PF04097; Nic96; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Membrane; mRNA transport;
KW Nuclear pore complex; Nucleus; Protein transport; Reference proteome;
KW Translocation; Transport.
FT CHAIN 1..839
FT /note="Nucleoporin NIC96"
FT /id="PRO_0000124787"
FT REGION 25..60
FT /note="Leucine zipper-like heptad repeat, required for
FT interaction with NSP1"
FT CONFLICT 59
FT /note="Missing (in Ref. 1; CAA51427)"
FT /evidence="ECO:0000305"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 206..228
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 234..244
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 248..263
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 270..289
FT /evidence="ECO:0007829|PDB:6X07"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:2RFO"
FT HELIX 301..312
FT /evidence="ECO:0007829|PDB:6X07"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:2QX5"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 333..342
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 346..355
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:6X07"
FT TURN 361..364
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 365..375
FT /evidence="ECO:0007829|PDB:6X07"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 384..397
FT /evidence="ECO:0007829|PDB:6X07"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:6X07"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:2RFO"
FT HELIX 406..416
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:2QX5"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 432..442
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:6X07"
FT TURN 452..454
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 459..469
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 478..484
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 488..496
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 500..512
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 534..541
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 542..545
FT /evidence="ECO:0007829|PDB:6X07"
FT TURN 546..548
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 550..557
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 558..562
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 568..583
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 586..590
FT /evidence="ECO:0007829|PDB:6X07"
FT STRAND 591..593
FT /evidence="ECO:0007829|PDB:6X07"
FT STRAND 595..597
FT /evidence="ECO:0007829|PDB:2RFO"
FT STRAND 599..601
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 603..606
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 608..611
FT /evidence="ECO:0007829|PDB:6X07"
FT STRAND 615..617
FT /evidence="ECO:0007829|PDB:2RFO"
FT HELIX 618..634
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 637..646
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 650..667
FT /evidence="ECO:0007829|PDB:6X07"
FT STRAND 675..679
FT /evidence="ECO:0007829|PDB:2RFO"
FT TURN 681..683
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 685..696
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 700..703
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 708..728
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 732..741
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 750..760
FT /evidence="ECO:0007829|PDB:6X07"
FT STRAND 761..763
FT /evidence="ECO:0007829|PDB:2RFO"
FT HELIX 765..768
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 771..789
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 799..820
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 821..823
FT /evidence="ECO:0007829|PDB:6X07"
FT HELIX 828..836
FT /evidence="ECO:0007829|PDB:6X07"
SQ SEQUENCE 839 AA; 96174 MW; 48EC3BC71281CB44 CRC64;
MLETLRGNKL HSGTSKGANK KLNELLESSD NLPSASSELG SIQVSINELR RRVFQLRSKN
KASKDYTKAH YLLANSGLSF EDVDAFIKDL QTNQFLEPNP PKIIESEELE FYIRTKKEEN
ILMSIEQLLN GATKDFDNFI NHNLNLDWAQ HKNEVMKNFG ILIQDKKTVD HKKSISSLDP
KLPSWGNKGN NILNSNESRL NVNENNILRE KFENYARIVF QFNNSRQANG NFDIANEFIS
ILSSANGTRN AQLLESWKIL ESMKSKDINI VEVGKQYLEQ QFLQYTDNLY KKNMNEGLAT
NVNKIKSFID TKLKKADKSW KISNLTVING VPIWALIFYL LRAGLIKEAL QVLVENKANI
KKVEQSFLTY FKAYASSKDH GLPVEYSTKL HTEYNQHIKS SLDGDPYRLA VYKLIGRCDL
SRKNIPAVTL SIEDWLWMHL MLIKEKDAEN DPVYERYSLE DFQNIIISYG PSRFSNYYLQ
TLLLSGLYGL AIDYTYTFSE MDAVHLAIGL ASLKLFKIDS STRLTKKPKR DIRFANILAN
YTKSFRYSDP RVAVEYLVLI TLNEGPTDVE LCHEALRELV LETKEFTVLL GKIGRDGARI
PGVIEERQPL LHVRDEKEFL HTITEQAARR ADEDGRIYDS ILLYQLAEEY DIVITLVNSL
LSDTLSASDL DQPLVGPDDN SETNPVLLAR RMASIYFDNA GISRQIHVKN KEICMLLLNI
SSIRELYFNK QWQETLSQME LLDLLPFSDE LSARKKAQDF SNLDDNIVKN IPNLLIITLS
CISNMIHILN ESKYQSSTKG QQIDSLKNVA RQCMIYAGMI QYRMPRETYS TLINIDVSL
