ID NSF_CRIGR Reviewed; 744 AA. AC P18708; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 02-SEP-2026, entry version 178. DE RecName: Full=Vesicle-fusing ATPase; DE EC=3.6.4.6; DE AltName: Full=N-ethylmaleimide-sensitive fusion protein; DE Short=NEM-sensitive fusion protein; DE AltName: Full=Vesicular-fusion protein NSF; GN Name=NSF; OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; OC Cricetidae; Cricetinae; Cricetulus. OX NCBI_TaxID=10029; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Ovary; RX PubMed=2657434; DOI=10.1038/339355a0; RA Wilson D.W., Wilcox C.A., Flynn G.C., Chen E., Kuang W.-J., Henzel W.J., RA Block M.R., Ullrich A., Rothman J.E.; RT "A fusion protein required for vesicle-mediated transport in both mammalian RT cells and yeast."; RL Nature 339:355-359(1989). RN [2] RP FUNCTION. RX PubMed=2542798; DOI=10.1038/339397a0; RA Beckers C.J.M., Block M.R., Glick B.S., Rothman J.E., Balch W.E.; RT "Vesicular transport between the endoplasmic reticulum and the Golgi stack RT requires the NEM-sensitive fusion protein."; RL Nature 339:397-398(1989). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 487-740 IN COMPLEX WITH ATP RP ANALOG. RX PubMed=9727495; DOI=10.1016/s0092-8674(00)81593-7; RA Lenzen C.U., Steinmann D., Whiteheart S.W., Weis W.I.; RT "Crystal structure of the hexamerization domain of N-ethylmaleimide- RT sensitive fusion protein."; RL Cell 94:525-536(1998). RN [4] RP ERRATUM OF PUBMED:9727495. RA Lenzen C.U., Steinmann D., Whiteheart S.W., Weis W.I.; RL Cell 95:289-289(1998). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 478-744 IN COMPLEX WITH ATP AND RP MAGNESIUM. RX PubMed=9731775; DOI=10.1038/1843; RA Yu R.C., Hanson P.I., Jahn R., Bruenger A.T.; RT "Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide RT sensitive factor complexed with ATP."; RL Nat. Struct. Biol. 5:803-811(1998). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-205. RX PubMed=10445031; DOI=10.1016/s1097-2765(00)80191-4; RA Yu R.C., Jahn R., Brunger A.T.; RT "NSF N-terminal domain crystal structure: models of NSF function."; RL Mol. Cell 4:97-107(1999). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-203. RX PubMed=10559905; DOI=10.1038/11097; RA May A.P., Misura K.M., Whiteheart S.W., Weis W.I.; RT "Crystal structure of the amino-terminal domain of N-ethylmaleimide- RT sensitive fusion protein."; RL Nat. Cell Biol. 1:175-182(1999). CC -!- FUNCTION: Required for vesicle-mediated transport. Catalyzes the fusion CC of transport vesicles within the Golgi cisternae. Is also required for CC transport from the endoplasmic reticulum to the Golgi stack. Seems to CC function as a fusion protein required for the delivery of cargo CC proteins to all compartments of the Golgi stack independent of vesicle CC origin. Interaction with AMPAR subunit GRIA2 leads to influence GRIA2 CC membrane cycling. {ECO:0000269|PubMed:2542798}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000305|PubMed:9731775}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000305|PubMed:9731775}; CC -!- SUBUNIT: Homohexamer. Interacts with GABARAP and GABARAPL2 (By CC similarity). Interacts with GRIA2 (By similarity). Interacts with PLK2, CC leading to disrupt the interaction with GRIA2 (By similarity). CC Interacts with MUSK; may regulate MUSK endocytosis and activity (By CC similarity). Interacts with CDK16 (By similarity). {ECO:0000250}. CC -!- INTERACTION: CC P18708; P18708: NSF; NbExp=5; IntAct=EBI-925742, EBI-925742; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- PTM: Phosphorylation at Ser-569 interferes with homohexamerization. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA33678.1; Type=Erroneous initiation; 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; X15652; CAA33678.1; ALT_INIT; mRNA. DR PIR; S04235; S04235. DR RefSeq; XP_007606206.1; XM_007608016.2. DR RefSeq; XP_027283716.1; XM_027427915.1. DR PDB; 1D2N; X-ray; 1.75 A; A=479-743. DR PDB; 1NSF; X-ray; 1.90 A; A=478-744. DR PDB; 1QCS; X-ray; 1.90 A; A=1-205. DR PDB; 1QDN; X-ray; 2.30 A; A/B/C=1-203. DR PDB; 3J94; EM; 4.20 A; A/B/C/D/E/F=1-744. DR PDB; 3J95; EM; 7.60 A; A/B/C/D/E/F=1-744. DR PDB; 3J96; EM; 7.60 A; A/B/C/D/E/F=1-744. DR PDB; 3J97; EM; 7.80 A; A/B/C/D/E/F=1-744. DR PDB; 3J98; EM; 8.40 A; A/B/C/D/E/F=1-744. DR PDB; 3J99; EM; 8.20 A; A/B/C/D/E/F=1-744. DR PDB; 6IP2; EM; 3.70 A; A/B/C/D/E/F=1-744. DR PDB; 6MDM; EM; 4.40 A; A/B/C/D/E/F=1-744. DR PDB; 6MDN; EM; 4.40 A; A/B/C/D/E/F=1-723. DR PDB; 6MDO; EM; 3.90 A; A/B/C/D/E/F=1-723. DR PDB; 6MDP; EM; 3.80 A; A/B/C/D/E/F=1-723. DR PDB; 9NV9; EM; 3.60 A; A/B/C/D/E/F/G=1-744. DR PDB; 9NVD; EM; 4.70 A; A/B/C/D/E/F=1-744. DR PDB; 9OJR; EM; 2.95 A; A/B/C/D/E/F=1-744. DR PDB; 9OJU; EM; 2.97 A; A/B/C/D/E/F=1-744. DR PDB; 9OJZ; EM; 3.39 A; A/B/C/D/E/F=1-744. DR PDB; 9OK5; EM; 3.29 A; A/B/C/D/E/F=1-744. DR PDB; 9OKC; EM; 3.67 A; A/B/C/D/E/F=1-744. DR PDB; 9OLJ; EM; 3.52 A; A/B/C/D/E/F=1-744. DR PDB; 9OLO; EM; 3.56 A; A/B/C/D/E/F=1-744. DR PDB; 9OMQ; EM; 3.86 A; A/B/C/D/E/F=1-744. DR PDB; 9PAF; EM; 3.82 A; A/B/C/D/E/F=1-744. DR PDB; 9PAG; EM; 3.62 A; A/B/C/D/E/F=1-744. DR PDB; 9PB9; EM; 3.45 A; A/B/C/D/E/F=1-744. DR PDB; 9PBA; EM; 3.47 A; A/B/C/D/E/F=1-744. DR PDB; 9PBF; EM; 4.01 A; A/B/C/D/E/F=1-744. DR PDB; 9PBV; EM; 3.91 A; A/B/C/D/E/F=1-744. DR PDB; 9PC3; EM; 3.69 A; A/B/C/D/E/F=1-744. DR PDB; 9PCX; EM; 4.03 A; A/B/C/D/E/F=1-744. DR PDB; 9PCZ; EM; 3.65 A; A/B/C/D/E/F=1-744. DR PDB; 9PD1; EM; 4.50 A; A/B/C/D/E/F=1-744. DR PDB; 9PD8; EM; 4.23 A; A/B/C/D/E/F=1-744. DR PDB; 9PDB; EM; 3.83 A; A/B/C/D/E/F=1-744. DR PDB; 9PDD; EM; 4.16 A; A/B/C/D/E/F=1-744. DR PDB; 9PF2; EM; 3.88 A; A/B/C/D/E/F=1-744. DR PDB; 9PFC; EM; 3.15 A; A/B/C/D/E/F=1-744. DR PDB; 9PFF; EM; 3.09 A; A/B/C/D/E/F=1-744. DR PDB; 9PFG; EM; 3.58 A; J/K=1-744. DR AlphaFoldDB; P18708; -. DR EMDB; EMD-49831; -. DR EMDB; EMD-49833; -. DR EMDB; EMD-6204; -. DR EMDB; EMD-6205; -. DR EMDB; EMD-6206; -. DR EMDB; EMD-6207; -. DR EMDB; EMD-6208; -. DR EMDB; EMD-6209; -. DR EMDB; EMD-6210; -. DR EMDB; EMD-70547; -. DR EMDB; EMD-70548; -. DR EMDB; EMD-70550; -. DR EMDB; EMD-70554; -. DR EMDB; EMD-70559; -. DR EMDB; EMD-70594; -. DR EMDB; EMD-70598; -. DR EMDB; EMD-70616; -. DR EMDB; EMD-71437; -. DR EMDB; EMD-71438; -. DR EMDB; EMD-71458; -. DR EMDB; EMD-71475; -. DR EMDB; EMD-71478; -. DR EMDB; EMD-71491; -. DR EMDB; EMD-71496; -. DR EMDB; EMD-71521; -. DR EMDB; EMD-71522; -. DR EMDB; EMD-71523; -. DR EMDB; EMD-71529; -. DR EMDB; EMD-71530; -. DR EMDB; EMD-71533; -. DR EMDB; EMD-71591; -. DR EMDB; EMD-71598; -. DR EMDB; EMD-71600; -. DR EMDB; EMD-71601; -. DR EMDB; EMD-9100; -. DR EMDB; EMD-9101; -. DR EMDB; EMD-9102; -. DR EMDB; EMD-9103; -. DR EMDB; EMD-9698; -. DR SMR; P18708; -. DR DIP; DIP-35598N; -. DR IntAct; P18708; 9. DR BindingDB; P18708; -. DR ChEMBL; CHEMBL4739845; -. DR iPTMnet; P18708; -. DR Ensembl; ENSCGRT00001028633; ENSCGRP00001024387; ENSCGRG00001022331. DR GeneID; 100770898; -. DR KEGG; cge:100770898; -. DR CTD; 4905; -. DR eggNOG; KOG0741; Eukaryota. DR OrthoDB; 9982946at2759; -. DR EvolutionaryTrace; P18708; -. DR Proteomes; UP001108280; Chromosome 7. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005795; C:Golgi stack; IEA:TreeGrafter. DR GO; GO:0030496; C:midbody; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl. DR GO; GO:0140545; F:ATP-dependent protein disaggregase activity; IDA:ParkinsonsUK-UCL. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IEA:Ensembl. DR GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl. DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl. DR GO; GO:0044877; F:protein-containing complex binding; IDA:ParkinsonsUK-UCL. DR GO; GO:0000149; F:SNARE binding; IDA:ParkinsonsUK-UCL. DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IEA:TreeGrafter. DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IEA:TreeGrafter. DR GO; GO:0006886; P:intracellular protein transport; IEA:Ensembl. DR GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl. DR GO; GO:0001921; P:positive regulation of receptor recycling; IEA:Ensembl. DR GO; GO:0035494; P:SNARE complex disassembly; IDA:ParkinsonsUK-UCL. DR CDD; cd19504; RecA-like_NSF-SEC18_r1-like; 1. DR FunFam; 1.10.8.60:FF:000026; vesicle-fusing ATPase isoform X1; 1. DR FunFam; 1.10.8.60:FF:000031; vesicle-fusing ATPase isoform X1; 1. DR FunFam; 2.40.40.20:FF:000006; vesicle-fusing ATPase isoform X1; 1. DR FunFam; 3.10.330.10:FF:000003; vesicle-fusing ATPase isoform X1; 1. DR FunFam; 3.40.50.300:FF:000166; vesicle-fusing ATPase isoform X1; 1. DR FunFam; 3.40.50.300:FF:000187; Vesicular-fusion ATPase SEC18; 1. DR Gene3D; 1.10.8.60; -; 2. DR Gene3D; 2.40.40.20; -; 1. DR Gene3D; 3.10.330.10; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR041569; AAA_lid_3. DR InterPro; IPR009010; Asp_de-COase-like_dom_sf. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR003960; ATPase_AAA_CS. DR InterPro; IPR004201; Cdc48_dom2. DR InterPro; IPR029067; CDC48_domain_2-like_sf. DR InterPro; IPR003338; CDC4_N-term_subdom. DR InterPro; IPR054419; NSF_ATPase_lid. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR039812; Vesicle-fus_ATPase. DR PANTHER; PTHR23078:SF3; VESICLE-FUSING ATPASE; 1. DR PANTHER; PTHR23078; VESICULAR-FUSION PROTEIN NSF; 1. DR Pfam; PF00004; AAA; 2. DR Pfam; PF17862; AAA_lid_3; 1. DR Pfam; PF02933; CDC48_2; 1. DR Pfam; PF02359; CDC48_N; 1. DR Pfam; PF21964; NSF_ATPase_lid; 1. DR PRINTS; PR00830; ENDOLAPTASE. DR SMART; SM00382; AAA; 2. DR SMART; SM01072; CDC48_2; 1. DR SMART; SM01073; CDC48_N; 1. DR SUPFAM; SSF50692; ADC-like; 1. DR SUPFAM; SSF54585; Cdc48 domain 2-like; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS00674; AAA; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Cytoplasm; KW Direct protein sequencing; Hydrolase; Magnesium; Metal-binding; KW Nucleotide-binding; Phosphoprotein; Protein transport; Reference proteome; KW Repeat; Transport. FT CHAIN 1..744 FT /note="Vesicle-fusing ATPase" FT /id="PRO_0000084562" FT BINDING 505..510 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:9731775, FT ECO:0000305|PubMed:9727495" FT BINDING 545..552 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:9731775, FT ECO:0000305|PubMed:9727495" FT BINDING 550 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:9731775" FT MOD_RES 105 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P46460" FT MOD_RES 207 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46459" FT MOD_RES 259 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P46460" FT MOD_RES 569 FT /note="Phosphoserine; by CDK16" FT /evidence="ECO:0000250|UniProtKB:P46460" FT STRAND 4..10 FT /evidence="ECO:0007829|PDB:1QCS" FT HELIX 14..19 FT /evidence="ECO:0007829|PDB:1QCS" FT STRAND 22..24 FT /evidence="ECO:0007829|PDB:1QCS" FT TURN 26..28 FT /evidence="ECO:0007829|PDB:1QCS" FT STRAND 34..40 FT /evidence="ECO:0007829|PDB:1QCS" FT STRAND 43..51 FT /evidence="ECO:0007829|PDB:1QCS" FT STRAND 59..62 FT /evidence="ECO:0007829|PDB:1QCS" FT HELIX 64..70 FT /evidence="ECO:0007829|PDB:1QCS" FT STRAND 77..83 FT /evidence="ECO:0007829|PDB:1QCS" FT HELIX 87..90 FT /evidence="ECO:0007829|PDB:1QCS" FT STRAND 91..102 FT /evidence="ECO:0007829|PDB:1QCS" FT HELIX 104..106 FT /evidence="ECO:0007829|PDB:1QCS" FT STRAND 111..113 FT /evidence="ECO:0007829|PDB:1QCS" FT HELIX 114..125 FT /evidence="ECO:0007829|PDB:1QCS" FT STRAND 129..131 FT /evidence="ECO:0007829|PDB:1QCS" FT STRAND 135..140 FT /evidence="ECO:0007829|PDB:1QCS" FT STRAND 143..154 FT /evidence="ECO:0007829|PDB:1QCS" FT HELIX 155..158 FT /evidence="ECO:0007829|PDB:1QCS" FT STRAND 173..176 FT /evidence="ECO:0007829|PDB:1QCS" FT STRAND 182..187 FT /evidence="ECO:0007829|PDB:1QCS" FT STRAND 194..200 FT /evidence="ECO:0007829|PDB:1QCS" FT HELIX 205..207 FT /evidence="ECO:0007829|PDB:9PB9" FT TURN 216..219 FT /evidence="ECO:0007829|PDB:9OJR" FT HELIX 224..234 FT /evidence="ECO:0007829|PDB:9OJR" FT HELIX 236..239 FT /evidence="ECO:0007829|PDB:9OJR" FT HELIX 242..248 FT /evidence="ECO:0007829|PDB:9OJR" FT HELIX 251..253 FT /evidence="ECO:0007829|PDB:9OJR" FT STRAND 255..259 FT /evidence="ECO:0007829|PDB:9OJR" FT HELIX 266..276 FT /evidence="ECO:0007829|PDB:9OJR" FT HELIX 279..282 FT /evidence="ECO:0007829|PDB:9OJU" FT STRAND 283..286 FT /evidence="ECO:0007829|PDB:9OJR" FT HELIX 287..289 FT /evidence="ECO:0007829|PDB:9OJR" FT HELIX 297..303 FT /evidence="ECO:0007829|PDB:9OJR" FT HELIX 304..306 FT /evidence="ECO:0007829|PDB:9OJR" FT HELIX 307..316 FT /evidence="ECO:0007829|PDB:9OJR" FT HELIX 320..322 FT /evidence="ECO:0007829|PDB:9PBA" FT STRAND 323..329 FT /evidence="ECO:0007829|PDB:9OJR" FT HELIX 330..332 FT /evidence="ECO:0007829|PDB:9OJR" FT HELIX 336..338 FT /evidence="ECO:0007829|PDB:9OJR" FT TURN 341..343 FT /evidence="ECO:0007829|PDB:9PFF" FT HELIX 348..358 FT /evidence="ECO:0007829|PDB:9OJR" FT STRAND 359..362 FT /evidence="ECO:0007829|PDB:9OK5" FT STRAND 366..374 FT /evidence="ECO:0007829|PDB:9OJR" FT HELIX 376..378 FT /evidence="ECO:0007829|PDB:9OJR" FT TURN 381..384 FT /evidence="ECO:0007829|PDB:9OJR" FT STRAND 391..394 FT /evidence="ECO:0007829|PDB:9OJR" FT HELIX 400..410 FT /evidence="ECO:0007829|PDB:9OJR" FT HELIX 412..416 FT /evidence="ECO:0007829|PDB:9OJR" FT HELIX 426..432 FT /evidence="ECO:0007829|PDB:9OJR" FT HELIX 438..462 FT /evidence="ECO:0007829|PDB:9OJR" FT HELIX 467..472 FT /evidence="ECO:0007829|PDB:9OJR" FT HELIX 478..486 FT /evidence="ECO:0007829|PDB:9OJR" FT STRAND 491..493 FT /evidence="ECO:0007829|PDB:9OJR" FT HELIX 496..499 FT /evidence="ECO:0007829|PDB:9OK5" FT TURN 500..502 FT /evidence="ECO:0007829|PDB:1D2N" FT STRAND 503..505 FT /evidence="ECO:0007829|PDB:9PFF" FT HELIX 512..530 FT /evidence="ECO:0007829|PDB:1D2N" FT STRAND 535..542 FT /evidence="ECO:0007829|PDB:1D2N" FT HELIX 549..560 FT /evidence="ECO:0007829|PDB:1D2N" FT STRAND 563..568 FT /evidence="ECO:0007829|PDB:1D2N" FT HELIX 570..572 FT /evidence="ECO:0007829|PDB:1D2N" FT HELIX 578..593 FT /evidence="ECO:0007829|PDB:1D2N" FT STRAND 595..602 FT /evidence="ECO:0007829|PDB:1D2N" FT HELIX 605..608 FT /evidence="ECO:0007829|PDB:1D2N" FT TURN 613..616 FT /evidence="ECO:0007829|PDB:1D2N" FT HELIX 620..629 FT /evidence="ECO:0007829|PDB:1D2N" FT HELIX 632..634 FT /evidence="ECO:0007829|PDB:9PFF" FT STRAND 635..637 FT /evidence="ECO:0007829|PDB:9PFF" FT STRAND 639..647 FT /evidence="ECO:0007829|PDB:1D2N" FT HELIX 649..654 FT /evidence="ECO:0007829|PDB:1D2N" FT TURN 658..660 FT /evidence="ECO:0007829|PDB:1D2N" FT STRAND 661..666 FT /evidence="ECO:0007829|PDB:1D2N" FT STRAND 670..672 FT /evidence="ECO:0007829|PDB:1D2N" FT HELIX 673..683 FT /evidence="ECO:0007829|PDB:1D2N" FT HELIX 688..698 FT /evidence="ECO:0007829|PDB:1D2N" FT STRAND 701..705 FT /evidence="ECO:0007829|PDB:1D2N" FT HELIX 707..717 FT /evidence="ECO:0007829|PDB:1D2N" FT HELIX 722..724 FT /evidence="ECO:0007829|PDB:1D2N" FT HELIX 725..735 FT /evidence="ECO:0007829|PDB:1D2N" SQ SEQUENCE 744 AA; 82536 MW; F3E0CEB2CF1BD582 CRC64; MAGRSMQAAR CPTDELSLSN CAVVSEKDYQ SGQHVIVRTS PNHKYIFTLR THPSVVPGSV AFSLPQRKWA GLSIGQEIEV ALYSFDKAKQ CIGTMTIEID FLQKKNIDSN PYDTDKMAAE FIQQFNNQAF SVGQQLVFSF NDKLFGLLVK DIEAMDPSIL KGEPASGKRQ KIEVGLVVGN SQVAFEKAEN SSLNLIGKAK TKENRQSIIN PDWNFEKMGI GGLDKEFSDI FRRAFASRVF PPEIVEQMGC KHVKGILLYG PPGCGKTLLA RQIGKMLNAR EPKVVNGPEI LNKYVGESEA NIRKLFADAE EEQRRLGANS GLHIIIFDEI DAICKQRGSM AGSTGVHDTV VNQLLSKIDG VEQLNNILVI GMTNRPDLID EALLRPGRLE VKMEIGLPDE KGRLQILHIH TARMRGHQLL SADVDIKELA VETKNFSGAE LEGLVRAAQS TAMNRHIKAS TKVEVDMEKA ESLQVTRGDF LASLENDIKP AFGTNQEDYA SYIMNGIIKW GDPVTRVLDD GELLVQQTKN SDRTPLVSVL LEGPPHSGKT ALAAKIAEES NFPFIKICSP DKMIGFSETA KCQAMKKIFD DAYKSQLSCV VVDDIERLLD YVPIGPRFSN LVLQALLVLL KKAPPQGRKL LIIGTTSRKD VLQEMEMLNA FSTTIHVPNI ATGEQLLEAL ELLGNFKDKE RTTIAQQVKG KKVWIGIKKL LMLIEMSLQM DPEYRVRKFL ALLREEGASP LDFD //