ID NUP1_YEAST Reviewed; 1076 AA. AC P20676; D6W2F9; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 27-MAR-2024, entry version 205. DE RecName: Full=Nucleoporin NUP1; DE AltName: Full=Nuclear pore protein NUP1; GN Name=NUP1; OrderedLocusNames=YOR098C; ORFNames=YOR3182C; 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=2190694; DOI=10.1016/0092-8674(90)90062-j; RA Davis L.I., Fink G.R.; RT "The NUP1 gene encodes an essential component of the yeast nuclear pore RT complex."; RL Cell 61:965-978(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9200815; RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i; RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C., RA Schwager C., Paces V., Sander C., Ansorge W.; RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV."; RL Yeast 13:655-672(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169874; RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."; RL Nature 387:98-102(1997). 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 INTERACTION WITH KAP122. RX PubMed=10525531; DOI=10.1083/jcb.147.2.235; RA Titov A.A., Blobel G.; RT "The karyopherin Kap122p/Pdr6p imports both subunits of the transcription RT factor IIA into the nucleus."; RL J. Cell Biol. 147:235-246(1999). RN [6] 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 [7] RP FUNCTION, AND SRP1 RECYCLING. RX PubMed=11046143; DOI=10.1128/mcb.20.22.8468-8479.2000; RA Solsbacher J., Maurer P., Vogel F., Schlenstedt G.; RT "Nup2p, a yeast nucleoporin, functions in bidirectional transport of RT importin alpha."; RL Mol. Cell. Biol. 20:8468-8479(2000). RN [8] RP FUNCTION, AND INTERACTION THROUGH FG REPEATS. 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 [9] RP FUNCTION, AND INTERACTION WITH NUP60. RX PubMed=11535617; DOI=10.1083/jcb.200101007; RA Denning D.P., Mykytka B., Allen N.P., Huang L., Burlingame A., Rexach M.; RT "The nucleoporin Nup60p functions as a Gsp1p-GTP-sensitive tether for Nup2p RT at the nuclear pore complex."; RL J. Cell Biol. 154:937-950(2001). RN [10] RP FUNCTION, AND STRUCTURAL BASIS OF FG REPEAT INTERACTION. 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 INTERACTION WITH KARYOPHERINS THROUGH FG REPEATS. 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 IMPORT COMPLEX DISASSEMBLY. RX PubMed=11867631; DOI=10.1074/jbc.m112306200; RA Gilchrist D., Mykytka B., Rexach M.; RT "Accelerating the rate of disassembly of karyopherin-cargo complexes."; RL J. Biol. Chem. 277:18161-18172(2002). RN [13] 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 [14] 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 [15] 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 [16] 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 [17] 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 [18] RP PHOSPHORYLATION BY CDC28. RX PubMed=14574415; DOI=10.1038/nature02062; RA Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K., RA Shokat K.M., Morgan D.O.; RT "Targets of the cyclin-dependent kinase Cdk1."; RL Nature 425:859-864(2003). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; THR-381; SER-383 AND RP SER-637, AND 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). RN [21] 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). RN [22] 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. 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). As one of the FG repeat CC nucleoporins NUP1 is involved in interactions with and guidance of CC nuclear transport receptors such as SRP1-KAP95 (importin alpha and CC beta) through the NPC. Like the closely related NUP2 it also plays an CC important role in disassembling and recycling SRP1-KAP95 to the CC cytoplasm after nuclear import. Upon entry of the heterotrimeric SRP1- CC KAP95-cargo complex in the nucleus, NUP1 binds through its C-terminus CC to KAP95, thus accelerating the release of KAP95 and, indirectly, of CC the nuclear localization signal (NLS)-containing cargo from the SRP1- CC KAP95-cargo complex. {ECO:0000269|PubMed:10684247, CC ECO:0000269|PubMed:11046143, ECO:0000269|PubMed:11387327, CC ECO:0000269|PubMed:11535617, ECO:0000269|PubMed:11867631, CC ECO:0000269|PubMed:12372823, ECO:0000269|PubMed:12543930, CC ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:12917401, CC ECO:0000269|PubMed:15039779}. 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 Interacts through its FG repeats with nuclear transport receptors. CC Binds to the nuclear basket of the NPC through NUP60. Interacts with CC KAP122. {ECO:0000269|PubMed:10525531, ECO:0000269|PubMed:10684247, CC ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:11535617, CC ECO:0000269|PubMed:12543930}. CC -!- INTERACTION: CC P20676; Q06142: KAP95; NbExp=6; IntAct=EBI-12392, EBI-9145; CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex CC {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane CC protein; Nucleoplasmic 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: FXFG repeats CC are especially abundant in NUPs on the nucleoplasmic side (in a highly CC charged environment and enriched in Ser and Thr). CC -!- PTM: Phosphorylated by CDC28. {ECO:0000305|PubMed:14574415}. CC -!- MISCELLANEOUS: Present with 468 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. 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; M33632; AAA34822.1; -; Genomic_DNA. DR EMBL; X94335; CAA64020.1; -; Genomic_DNA. DR EMBL; Z75006; CAA99295.1; -; Genomic_DNA. DR EMBL; BK006948; DAA10875.1; -; Genomic_DNA. DR PIR; A35622; A35622. DR RefSeq; NP_014741.1; NM_001183517.1. DR PDB; 4C31; X-ray; 3.00 A; C/F/X/Y=322-355. DR PDB; 4MBE; X-ray; 2.61 A; G/H/X/Y=316-340. DR PDB; 5OWU; X-ray; 2.00 A; B=1-1076. DR PDBsum; 4C31; -. DR PDBsum; 4MBE; -. DR PDBsum; 5OWU; -. DR AlphaFoldDB; P20676; -. DR SMR; P20676; -. DR BioGRID; 34496; 106. DR ComplexPortal; CPX-824; Nuclear pore complex. DR DIP; DIP-81N; -. DR IntAct; P20676; 47. DR MINT; P20676; -. DR STRING; 4932.YOR098C; -. DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family. DR GlyGen; P20676; 7 sites, 1 O-linked glycan (7 sites). DR iPTMnet; P20676; -. DR MaxQB; P20676; -. DR PaxDb; 4932-YOR098C; -. DR PeptideAtlas; P20676; -. DR EnsemblFungi; YOR098C_mRNA; YOR098C; YOR098C. DR GeneID; 854265; -. DR KEGG; sce:YOR098C; -. DR AGR; SGD:S000005624; -. DR SGD; S000005624; NUP1. DR VEuPathDB; FungiDB:YOR098C; -. DR eggNOG; KOG4719; Eukaryota. DR HOGENOM; CLU_316464_0_0_1; -. DR InParanoid; P20676; -. DR OMA; YGTENTE; -. DR OrthoDB; 2032019at2759; -. DR BioCyc; YEAST:G3O-33631-MONOMER; -. DR BioGRID-ORCS; 854265; 9 hits in 10 CRISPR screens. DR EvolutionaryTrace; P20676; -. DR PRO; PR:P20676; -. DR Proteomes; UP000002311; Chromosome XV. DR RNAct; P20676; Protein. 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:0044613; C:nuclear pore central transport channel; IDA:SGD. DR GO; GO:0044615; C:nuclear pore nuclear basket; IDA:SGD. DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central. DR GO; GO:0017056; F:structural constituent of nuclear pore; IMP:SGD. DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IMP:SGD. DR GO; GO:0006913; P:nucleocytoplasmic transport; NAS:ComplexPortal. DR GO; GO:0016973; P:poly(A)+ mRNA 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:0006405; P:RNA export from nucleus; IBA:GO_Central. DR GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD. DR DisProt; DP01075; -. DR IDEAL; IID50271; -. DR InterPro; IPR026054; Nucleoporin. DR PANTHER; PTHR23193; NUCLEAR PORE COMPLEX PROTEIN NUP; 1. DR PANTHER; PTHR23193:SF40; NUCLEAR PORE COMPLEX PROTEIN NUP214; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Membrane; mRNA transport; Nuclear pore complex; KW Nucleus; Phosphoprotein; Protein transport; Reference proteome; Repeat; KW Translocation; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..1076 FT /note="Nucleoporin NUP1" FT /id="PRO_0000204902" FT REPEAT 336..338 FT /note="FXF 1" FT REPEAT 384..386 FT /note="FXF 2" FT REPEAT 406..409 FT /note="FXFG 1" FT REPEAT 422..425 FT /note="FXFG 2" FT REPEAT 448..451 FT /note="FXFG 3" FT REPEAT 484..487 FT /note="FXFG 4" FT REPEAT 510..513 FT /note="FXFG 5" FT REPEAT 525..528 FT /note="FXFG 6" FT REPEAT 543..546 FT /note="FXFG 7" FT REPEAT 571..574 FT /note="FXFG 8" FT REPEAT 591..593 FT /note="FXF 3" FT REPEAT 614..616 FT /note="FXF 4" FT REPEAT 636..638 FT /note="FXF 5" FT REPEAT 657..659 FT /note="FXF 6" FT REPEAT 671..674 FT /note="FXFG 9" FT REPEAT 689..691 FT /note="FXF 7" FT REPEAT 708..711 FT /note="FXFG 10" FT REPEAT 727..730 FT /note="FXFG 11" FT REPEAT 753..755 FT /note="FXF 8" FT REPEAT 800..803 FT /note="FXFG 12" FT REPEAT 819..821 FT /note="FXF 9" FT REPEAT 866..868 FT /note="FXF 10" FT REPEAT 885..888 FT /note="FXFG 13" FT REPEAT 929..931 FT /note="FXF 11" FT REPEAT 1008..1009 FT /note="FG 1" FT REPEAT 1027..1028 FT /note="FG 2" FT REPEAT 1038..1039 FT /note="FG 3" FT REGION 1..39 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 143..183 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 224..260 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 403..518 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 548..743 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 940..979 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1025..1054 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1040..1076 FT /note="Interaction with KAP95" FT COMPBIAS 143..176 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 238..260 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 403..426 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 462..476 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 487..504 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 548..592 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 630..671 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 681..743 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 54 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 161 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950" FT MOD_RES 381 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 383 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 637 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT HELIX 1004..1007 FT /evidence="ECO:0007829|PDB:5OWU" FT TURN 1008..1010 FT /evidence="ECO:0007829|PDB:5OWU" SQ SEQUENCE 1076 AA; 113581 MW; 4AC23567D2FB53CC CRC64; MSSNTSSVMS SPRVEKRSFS STLKSFFTNP NKKRPSSKKV FSSNLSYANH LEESDVEDTL HVNKRKRVSG TSQHSDSLTQ NNNNAPIIIY GTENTERPPL LPILPIQRLR LLREKQRVRN MRELGLIQST EFPSITSSVI LGSQSKSDEG GSYLCTSSTP SPIKNGSCTR QLAGKSGEDT NVGLPILKSL KNRSNRKRFH SQSKGTVWSA NFEYDLSEYD AIQKKDNKDK EGNAGGDQKT SENRNNIKSS ISNGNLATGP NLTSEIEDLR ADINSNRLSN PQKNLLLKGP ASTVAKTAPI QESFVPNSER SGTPTLKKNI EPKKDKESIV LPTVGFDFIK DNETPSKKTS PKATSSAGAV FKSSVEMGKT DKSTKTAEAP TLSFNFSQKA NKTKAVDNTV PSTTLFNFGG KSDTVTSASQ PFKFGKTSEK SENHTESDAP PKSTAPIFSF GKQEENGDEG DDENEPKRKR RLPVSEDTNT KPLFDFGKTG DQKETKKGES EKDASGKPSF VFGASDKQAE GTPLFTFGKK ADVTSNIDSS AQFTFGKAAT AKETHTKPSE TPATIVKKPT FTFGQSTSEN KISEGSAKPT FSFSKSEEER KSSPISNEAA KPSFSFPGKP VDVQAPTDDK TLKPTFSFTE PAQKDSSVVS EPKKPSFTFA SSKTSQPKPL FSFGKSDAAK EPPGSNTSFS FTKPPANETD KRPTPPSFTF GGSTTNNTTT TSTKPSFSFG APESMKSTAS TAAANTEKLS NGFSFTKFNH NKEKSNSPTS FFDGSASSTP IPVLGKPTDA TGNTTSKSAF SFGTANTNGT NASANSTSFS FNAPATGNGT TTTSNTSGTN IAGTFNVGKP DQSIASGNTN GAGSAFGFSS SGTAATGAAS NQSSFNFGNN GAGGLNPFTS ATSSTNANAG LFNKPPSTNA QNVNVPSAFN FTGNNSTPGG GSVFNMNGNT NANTVFAGSN NQPHQSQTPS FNTNSSFTPS TVPNINFSGL NGGITNTATN ALRPSDIFGA NAASGSNSNV TNPSSIFGGA GGVPTTSFGQ PQSAPNQMGM GTNNGMSMGG GVMANRKIAR MRHSKR //