NEP_RABIT
ID NEP_RABIT Reviewed; 750 AA.
AC P08049;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Neprilysin;
DE EC=3.4.24.11 {ECO:0000269|PubMed:3162886};
DE AltName: Full=Atriopeptidase;
DE AltName: Full=Enkephalinase;
DE AltName: Full=Neutral endopeptidase 24.11 {ECO:0000303|PubMed:2440677};
DE Short=NEP;
DE Short=Neutral endopeptidase;
DE AltName: Full=Skin fibroblast elastase;
DE Short=SFE;
DE AltName: CD_antigen=CD10;
GN Name=MME;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Kidney;
RX PubMed=2440677; DOI=10.1002/j.1460-2075.1987.tb02370.x;
RA Devault A., Lazure C., Nault C., le Moual H., Seidah N.G., Chretien M.,
RA Kahn P., Powell J., Mallet J., Beaumont A., Roques B.P., Crine P.,
RA Boileau G.;
RT "Amino acid sequence of rabbit kidney neutral endopeptidase 24.11
RT (enkephalinase) deduced from a complementary DNA.";
RL EMBO J. 6:1317-1322(1987).
RN [2]
RP ERRATUM OF PUBMED:2440677.
RA Devault A., Lazure C., Nault C., le Moual H., Seidah N.G., Chretien M.,
RA Kahn P., Powell J., Mallet J., Beaumont A., Roques B.P., Crine P.,
RA Boileau G.;
RL EMBO J. 6:2506-2506(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 206-274.
RX PubMed=3297057; DOI=10.1016/0006-291x(87)91347-7;
RA Kahn P.H., Powell J.F., Beaumont A., Roques B.P., Mallet J.J.;
RT "An antibody purified with a lambda GT11 fusion protein precipitates
RT enkephalinase activity.";
RL Biochem. Biophys. Res. Commun. 145:488-493(1987).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF HIS-584; HIS-588
RP AND HIS-638.
RX PubMed=3162886; DOI=10.1016/0014-5793(88)80701-4;
RA Devault A., Sales V., Nault C., Beaumont A., Roques B., Crine P.,
RA Boileau G.;
RT "Exploration of the catalytic site of endopeptidase 24.11 by site-directed
RT mutagenesis. Histidine residues 583 and 587 are essential for catalysis.";
RL FEBS Lett. 231:54-58(1988).
RN [5]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=8171037; DOI=10.1073/pnas.91.9.4072;
RA Fournie-Zaluski M.C., Gonzalez W., Turcaud S., Pham I., Roques B.P.,
RA Michel J.B.;
RT "Dual inhibition of angiotensin-converting enzyme and neutral endopeptidase
RT by the orally active inhibitor mixanpril: a potential therapeutic approach
RT in hypertension.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:4072-4076(1994).
CC -!- FUNCTION: Thermolysin-like specificity, but is almost confined on
CC acting on polypeptides of up to 30 amino acids (PubMed:3162886).
CC Biologically important in the destruction of opioid peptides such as
CC Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Catalyzes
CC cleavage of bradykinin, substance P and neurotensin peptides (By
CC similarity). Able to cleave angiotensin-1, angiotensin-2 and
CC angiotensin 1-9. Involved in the degradation of atrial natriuretic
CC factor (ANF) and brain natriuretic factor (BNP(1-32)) (By similarity).
CC Displays UV-inducible elastase activity toward skin preelastic and
CC elastic fibers (By similarity). {ECO:0000250|UniProtKB:P08473,
CC ECO:0000269|PubMed:3162886}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage of polypeptides between hydrophobic
CC residues, particularly with Phe or Tyr at P1'.; EC=3.4.24.11;
CC Evidence={ECO:0000269|PubMed:3162886};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + substance P = L-Leu-L-Met-NH2 + substance P(1-9);
CC Xref=Rhea:RHEA:71459, ChEBI:CHEBI:15377, ChEBI:CHEBI:190692,
CC ChEBI:CHEBI:190693, ChEBI:CHEBI:190700;
CC Evidence={ECO:0000250|UniProtKB:P08473};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71460;
CC Evidence={ECO:0000250|UniProtKB:P08473};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + substance P = L-Phe-Gly-L-Leu-L-Met-NH2 + substance P(1-
CC 7); Xref=Rhea:RHEA:71467, ChEBI:CHEBI:15377, ChEBI:CHEBI:190692,
CC ChEBI:CHEBI:190695, ChEBI:CHEBI:190698;
CC Evidence={ECO:0000250|UniProtKB:P08473};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71468;
CC Evidence={ECO:0000250|UniProtKB:P08473};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + neurotensin = L-isoleucyl-L-leucine + neurotensin(1-11);
CC Xref=Rhea:RHEA:71475, ChEBI:CHEBI:15377, ChEBI:CHEBI:147362,
CC ChEBI:CHEBI:190704, ChEBI:CHEBI:190706;
CC Evidence={ECO:0000250|UniProtKB:P08473};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71476;
CC Evidence={ECO:0000250|UniProtKB:P08473};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + neurotensin = L-tyrosyl-L-isoleucyl-L-leucine +
CC neurotensin(1-10); Xref=Rhea:RHEA:71479, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:147362, ChEBI:CHEBI:190705, ChEBI:CHEBI:190707;
CC Evidence={ECO:0000250|UniProtKB:P08473};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71480;
CC Evidence={ECO:0000250|UniProtKB:P08473};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:3162886};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08473};
CC -!- ACTIVITY REGULATION: Inhibited by mixanpril, an orally-active drug used
CC for the treatment of hypertension. {ECO:0000269|PubMed:8171037}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08473};
CC Single-pass type II membrane protein {ECO:0000255}.
CC -!- PTM: Myristoylation is a determinant of membrane targeting.
CC {ECO:0000250|UniProtKB:P08473}.
CC -!- PTM: Glycosylation at Asn-628 is necessary both for surface expression
CC and neutral endopeptidase activity. {ECO:0000250|UniProtKB:P08473}.
CC -!- SIMILARITY: Belongs to the peptidase M13 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01233, ECO:0000305}.
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DR EMBL; X05338; CAA28950.1; -; mRNA.
DR EMBL; M16593; AAA53694.1; -; mRNA.
DR PIR; A29451; HYRBN.
DR RefSeq; NP_001095155.1; NM_001101685.1.
DR PDB; 4XBH; X-ray; 2.11 A; A/B=55-750.
DR PDB; 4ZR5; X-ray; 2.80 A; A/B=55-750.
DR PDB; 5V48; X-ray; 3.00 A; A/B=55-750.
DR PDBsum; 4XBH; -.
DR PDBsum; 4ZR5; -.
DR PDBsum; 5V48; -.
DR AlphaFoldDB; P08049; -.
DR SMR; P08049; -.
DR STRING; 9986.ENSOCUP00000024871; -.
DR BindingDB; P08049; -.
DR ChEMBL; CHEMBL3768; -.
DR DrugCentral; P08049; -.
DR MEROPS; M13.001; -.
DR GeneID; 100009251; -.
DR KEGG; ocu:100009251; -.
DR CTD; 4311; -.
DR eggNOG; KOG3624; Eukaryota.
DR InParanoid; P08049; -.
DR OrthoDB; 282463at2759; -.
DR PRO; PR:P08049; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005903; C:brush border; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044306; C:neuron projection terminus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
DR GO; GO:0042277; F:peptide binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0050435; P:amyloid-beta metabolic process; ISS:UniProtKB.
DR GO; GO:0010815; P:bradykinin catabolic process; ISS:UniProtKB.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISS:UniProtKB.
DR GO; GO:0071492; P:cellular response to UV-A; ISS:UniProtKB.
DR GO; GO:0071493; P:cellular response to UV-B; ISS:UniProtKB.
DR GO; GO:0046449; P:creatinine metabolic process; ISS:UniProtKB.
DR GO; GO:0042447; P:hormone catabolic process; ISS:UniProtKB.
DR GO; GO:0001822; P:kidney development; ISS:UniProtKB.
DR GO; GO:0006518; P:peptide metabolic process; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:0090399; P:replicative senescence; ISS:UniProtKB.
DR GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
DR GO; GO:0010814; P:substance P catabolic process; ISS:UniProtKB.
DR CDD; cd08662; M13; 1.
DR Gene3D; 1.10.1380.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR029727; MME/CD10/NEP.
DR InterPro; IPR000718; Peptidase_M13.
DR InterPro; IPR018497; Peptidase_M13_C.
DR InterPro; IPR042089; Peptidase_M13_dom_2.
DR InterPro; IPR008753; Peptidase_M13_N.
DR PANTHER; PTHR11733; PTHR11733; 1.
DR PANTHER; PTHR11733:SF114; PTHR11733:SF114; 1.
DR Pfam; PF01431; Peptidase_M13; 1.
DR Pfam; PF05649; Peptidase_M13_N; 1.
DR PRINTS; PR00786; NEPRILYSIN.
DR PROSITE; PS51885; NEPRILYSIN; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Lipoprotein; Membrane; Metal-binding;
KW Metalloprotease; Myristate; Phosphoprotein; Protease; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..750
FT /note="Neprilysin"
FT /id="PRO_0000078216"
FT TOPO_DOM 2..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..51
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..750
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 56..750
FT /note="Peptidase M13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 16..23
FT /note="Stop-transfer sequence"
FT /evidence="ECO:0000255"
FT ACT_SITE 585
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 651
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT BINDING 103
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /ligand_note="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07861"
FT BINDING 584
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000305|PubMed:3162886"
FT BINDING 588
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000305|PubMed:3162886"
FT BINDING 647
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08473"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08473"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P08473"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P08473"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P08473"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P08473"
FT CARBOHYD 628
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 57..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 80..735
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 88..695
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 143..411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 234..242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 621..747
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT MUTAGEN 584
FT /note="H->F: Abolished peptidase activity."
FT /evidence="ECO:0000269|PubMed:3162886"
FT MUTAGEN 588
FT /note="H->F: Abolished peptidase activity."
FT /evidence="ECO:0000269|PubMed:3162886"
FT MUTAGEN 638
FT /note="H->F: Does not affect the peptidase activity."
FT /evidence="ECO:0000269|PubMed:3162886"
FT HELIX 60..72
FT /evidence="ECO:0007829|PDB:4XBH"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:4XBH"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 106..122
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 146..150
FT /evidence="ECO:0007829|PDB:4XBH"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 155..160
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:4XBH"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:4XBH"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 184..195
FT /evidence="ECO:0007829|PDB:4XBH"
FT STRAND 200..208
FT /evidence="ECO:0007829|PDB:4XBH"
FT STRAND 211..220
FT /evidence="ECO:0007829|PDB:4XBH"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 229..233
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 239..259
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 266..286
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:4XBH"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 305..311
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 323..331
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:4XBH"
FT STRAND 343..347
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 349..359
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 364..376
FT /evidence="ECO:0007829|PDB:4XBH"
FT TURN 377..379
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 385..389
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 392..399
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 407..418
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 420..431
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 436..454
FT /evidence="ECO:0007829|PDB:4XBH"
FT TURN 455..457
FT /evidence="ECO:0007829|PDB:4XBH"
FT STRAND 459..461
FT /evidence="ECO:0007829|PDB:5V48"
FT HELIX 463..475
FT /evidence="ECO:0007829|PDB:4XBH"
FT STRAND 477..481
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 485..488
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 490..496
FT /evidence="ECO:0007829|PDB:4XBH"
FT TURN 497..499
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 507..523
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 524..527
FT /evidence="ECO:0007829|PDB:4XBH"
FT STRAND 545..547
FT /evidence="ECO:0007829|PDB:4XBH"
FT TURN 548..551
FT /evidence="ECO:0007829|PDB:4XBH"
FT STRAND 552..556
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 557..559
FT /evidence="ECO:0007829|PDB:4XBH"
FT TURN 562..564
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 571..576
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 578..588
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 594..596
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 609..627
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 632..634
FT /evidence="ECO:0007829|PDB:4XBH"
FT TURN 641..644
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 645..669
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 682..693
FT /evidence="ECO:0007829|PDB:4XBH"
FT STRAND 696..698
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 700..709
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 715..724
FT /evidence="ECO:0007829|PDB:4XBH"
FT HELIX 727..732
FT /evidence="ECO:0007829|PDB:4XBH"
SQ SEQUENCE 750 AA; 85582 MW; 0F26AF7316BB9D12 CRC64;
MGRSESQMDI TDINTPKPKK KQRWTPLEIS LSVLVLLLTV IAVTMIALYA TYDDGICKSS
DCIKSAARLI QNMDATAEPC TDFFKYACGG WLKRNVIPET SSRYSNFDIL RDELEVILKD
VLQEPKTEDI VAVQKAKTLY RSCVNETAID SRGGQPLLKL LPDVYGWPVA TQNWEQTYGT
SWSAEKSIAQ LNSNYGKKVL INFFVGTDDK NSMNHIIHID QPRLGLPSRD YYECTGIYKE
ACTAYVDFMI AVAKLIRQEE GLPIDENQIS VEMNKVMELE KEIANATTKS EDRNDPMLLY
NKMTLAQIQN NFSLEINGKP FSWSNFTNEI MSTVNINIPN EEDVVVYAPE YLIKLKPILT
KYFPRDFQNL FSWRFIMDLV SSLSRTYKDS RNAFRKALYG TTSESATWRR CANYVNGNME
NAVGRLYVEA AFAGESKHVV EDLIAQIREV FIQTLDDLTW MDAETKKKAE EKALAIKERI
GYPDDIVSND NKLNNEYLEL NYKEDEYFEN IIQNLKFSQS KQLKKLREKV DKDEWITGAA
IVNAFYSSGR NQIVFPAGIL QPPFFSAQQS NSLNYGGIGM VIGHEITHGF DDNGRNFNKD
GDLVDWWTQQ SANNFKEQSQ CMVYQYGNFS WDLAGGQHLN GINTLGENIA DNGGIGQAYR
AYQNYVKKNG EEKLLPGIDL NHKQLFFLNF AQVWCGTYRP EYAVNSIKTD VHSPGNFRII
GSLQNSVEFS EAFQCPKNSY MNPEKKCRVW
