true1990-11-012024-03-27244VINC_HUMANComplete sequence of human vinculin and assignment of the gene to chromosome 10.Weller P.A.Ogryzko E.P.Corben E.B.Zhidkova N.I.Patel B.Price G.J.Spurr N.K.Koteliansky V.E.Critchley D.R.doi:10.1073/pnas.87.15.56671990Proc. Natl. Acad. Sci. U.S.A.875667-5671NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)Endothelial cellThe full-ORF clone resource of the German cDNA consortium.Bechtel S.Rosenfelder H.Duda A.Schmidt C.P.Ernst U.Wellenreuther R.Mehrle A.Schuster C.Bahr A.Bloecker H.Heubner D.Hoerlein A.Michel G.Wedler H.Koehrer K.Ottenwaelder B.Poustka A.Wiemann S.Schupp I.doi:10.1186/1471-2164-8-3992007BMC Genomics8399NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3)RetinaThe DNA sequence and comparative analysis of human chromosome 10.Deloukas P.Earthrowl M.E.Grafham D.V.Rubenfield M.French L.Steward C.A.Sims S.K.Jones M.C.Searle S.Scott C.Howe K.Hunt S.E.Andrews T.D.Gilbert J.G.R.Swarbreck D.Ashurst J.L.Taylor A.Battles J.Bird C.P.Ainscough R.Almeida J.P.Ashwell R.I.S.Ambrose K.D.Babbage A.K.Bagguley C.L.Bailey J.Banerjee R.Bates K.Beasley H.Bray-Allen S.Brown A.J.Brown J.Y.Burford D.C.Burrill W.Burton J.Cahill P.Camire D.Carter N.P.Chapman J.C.Clark S.Y.Clarke G.Clee C.M.Clegg S.Corby N.Coulson A.Dhami P.Dutta I.Dunn M.Faulkner L.Frankish A.Frankland J.A.Garner P.Garnett J.Gribble S.Griffiths C.Grocock R.Gustafson E.Hammond S.Harley J.L.Hart E.Heath P.D.Ho T.P.Hopkins B.Horne J.Howden P.J.Huckle E.Hynds C.Johnson C.Johnson D.Kana A.Kay M.Kimberley A.M.Kershaw J.K.Kokkinaki M.Laird G.K.Lawlor S.Lee H.M.Leongamornlert D.A.Laird G.Lloyd C.Lloyd D.M.Loveland J.Lovell J.McLaren S.McLay K.E.McMurray A.Mashreghi-Mohammadi M.Matthews L.Milne S.Nickerson T.Nguyen M.Overton-Larty E.Palmer S.A.Pearce A.V.Peck A.I.Pelan S.Phillimore B.Porter K.Rice C.M.Rogosin A.Ross M.T.Sarafidou T.Sehra H.K.Shownkeen R.Skuce C.D.Smith M.Standring L.Sycamore N.Tester J.Thorpe A.Torcasso W.Tracey A.Tromans A.Tsolas J.Wall M.Walsh J.Wang H.Weinstock K.West A.P.Willey D.L.Whitehead S.L.Wilming L.Wray P.W.Young L.Chen Y.Lovering R.C.Moschonas N.K.Siebert R.Fechtel K.Bentley D.Durbin R.M.Hubbard T.Doucette-Stamm L.Beck S.Smith D.R.Rogers J.doi:10.1038/nature024622004Nature429375-381NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).The MGC Project Teamdoi:10.1101/gr.25965042004Genome Res.142121-2127NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)VARIANT LEU-234ProstateOrganization of the human gene encoding the cytoskeletal protein vinculin and the sequence of the vinculin promoter.Moiseyeva E.P.Weller P.A.Zhidkova N.I.Corben E.B.Patel B.Jasinska I.Koteliansky V.E.Critchley D.R.doi:10.1016/s0021-9258(18)53612-71993J. Biol. Chem.2684318-4325NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56ALTERNATIVE SPLICING (ISOFORMS 1 AND 2)Lubec G.Chen W.-Q.Sun Y.2008-12UniProtKBPROTEIN SEQUENCE OF 114-132; 247-261; 327-339; 353-366; 465-476 AND 548-561IDENTIFICATION BY MASS SPECTROMETRYFetal brain cortexAn additional exon in the human vinculin gene specifically encodes meta-vinculin-specific difference peptide. Cross-species comparison reveals variable and conserved motifs in the meta-vinculin insert.Koteliansky V.E.Ogryzko E.P.Zhidkova N.I.Weller P.A.Critchley D.R.Vancompernolle K.Vandekerckhove J.Strasser P.Way M.Gimona M.Small J.V.doi:10.1111/j.1432-1033.1992.tb16692.x1992Eur. J. Biochem.204767-772NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 854-1051ALTERNATIVE SPLICING (ISOFORM 2)UterusExploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.Gevaert K.Goethals M.Martens L.Van Damme J.Staes A.Thomas G.R.Vandekerckhove J.doi:10.1038/nbt8102003Nat. Biotechnol.21566-569PROTEIN SEQUENCE OF 2-7 (ISOFORMS 1/2)PlateletFunctional analysis of Shigella VirG domains essential for interaction with vinculin and actin-based motility.Suzuki T.Saga S.Sasakawa C.doi:10.1074/jbc.271.36.218781996J. Biol. Chem.27121878-21885INTERACTION WITH S.FLEXNERI ICSA (MICROBIAL INFECTION)The phosphorylation of vinculin on tyrosine residues 100 and 1065, mediated by SRC kinases, affects cell spreading.Zhang Z.Izaguirre G.Lin S.-Y.Lee H.Y.Schaefer E.Haimovich B.doi:10.1091/mbc.e04-03-02642004Mol. Biol. Cell154234-4247PHOSPHORYLATION AT TYR-1133IDENTIFICATION BY MASS SPECTROMETRYGlobal, in vivo, and site-specific phosphorylation dynamics in signaling networks.Olsen J.V.Blagoev B.Gnad F.Macek B.Kumar C.Mortensen P.Mann M.doi:10.1016/j.cell.2006.09.0262006Cell127635-648PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-721IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Cervix carcinomaHuman alpha-synemin interacts directly with vinculin and metavinculin.Sun N.Critchley D.R.Paulin D.Li Z.Robson R.M.doi:10.1042/bj200711882008Biochem. J.409657-667INTERACTION WITH SYNMA quantitative atlas of mitotic phosphorylation.Dephoure N.Zhou C.Villen J.Beausoleil S.A.Bakalarski C.E.Elledge S.J.Gygi S.P.doi:10.1073/pnas.08051391052008Proc. Natl. Acad. Sci. U.S.A.10510762-10767PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290; SER-721 AND TYR-822IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Lysine acetylation targets protein complexes and co-regulates major cellular functions.Choudhary C.Kumar C.Gnad F.Nielsen M.L.Rehman M.Walther T.C.Olsen J.V.Mann M.doi:10.1126/science.11753712009Science325834-840ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-173 AND LYS-496IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Vinculin is a dually regulated actin filament barbed end-capping and side-binding protein.Le Clainche C.Dwivedi S.P.Didry D.Carlier M.F.doi:10.1074/jbc.m110.1028302010J. Biol. Chem.28523420-23432FUNCTIONDOMAINQuantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.Olsen J.V.Vermeulen M.Santamaria A.Kumar C.Miller M.L.Jensen L.J.Gnad F.Cox J.Jensen T.S.Nigg E.A.Brunak S.Mann M.doi:10.1126/scisignal.20004752010Sci. Signal.3RA3PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288; SER-290 AND SER-721IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Initial characterization of the human central proteome.Burkard T.R.Planyavsky M.Kaupe I.Breitwieser F.P.Buerckstuemmer T.Bennett K.L.Superti-Furga G.Colinge J.doi:10.1186/1752-0509-5-172011BMC Syst. Biol.517IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.Rigbolt K.T.Prokhorova T.A.Akimov V.Henningsen J.Johansen P.T.Kratchmarova I.Kassem M.Mann M.Olsen J.V.Blagoev B.doi:10.1126/scisignal.20015702011Sci. Signal.4RS3PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290; SER-346; SER-434 AND SER-721IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]The C-terminal tail domain of metavinculin, vinculin's splice variant, severs actin filaments.Janssen M.E.Liu H.Volkmann N.Hanein D.doi:10.1083/jcb.2011110462012J. Cell Biol.197585-593FUNCTION (ISOFORM 2)Toward a comprehensive characterization of a human cancer cell phosphoproteome.Zhou H.Di Palma S.Preisinger C.Peng M.Polat A.N.Heck A.J.Mohammed S.doi:10.1021/pr300630k2013J. Proteome Res.12260-271PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288; THR-672 AND SER-721IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]ErythroleukemiaAn enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y.Song C.Cheng K.Dong M.Wang F.Huang J.Sun D.Wang L.Ye M.Zou H.doi:10.1016/j.jprot.2013.11.0142014J. Proteomics96253-262PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260; SER-275; SER-288; SER-290; SER-346; SER-579; SER-600; THR-604; SER-721; SER-795 AND SER-809IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]LiverN-terminome analysis of the human mitochondrial proteome.Vaca Jacome A.S.Rabilloud T.Schaeffer-Reiss C.Rompais M.Ayoub D.Lane L.Bairoch A.Van Dorsselaer A.Carapito C.doi:10.1002/pmic.2014006172015Proteomics152519-2524IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Mutations in CTNNA1 cause butterfly-shaped pigment dystrophy and perturbed retinal pigment epithelium integrity.Saksens N.T.Krebs M.P.Schoenmaker-Koller F.E.Hicks W.Yu M.Shi L.Rowe L.Collin G.B.Charette J.R.Letteboer S.J.Neveling K.van Moorsel T.W.Abu-Ltaif S.De Baere E.Walraedt S.Banfi S.Simonelli F.Cremers F.P.Boon C.J.Roepman R.Leroy B.P.Peachey N.S.Hoyng C.B.Nishina P.M.den Hollander A.I.doi:10.1038/ng.34742016Nat. Genet.48144-151INTERACTION WITH CTNNA1The Intracranial Aneurysm Gene THSD1 Connects Endosome Dynamics to Nascent Focal Adhesion Assembly.Rui Y.N.Xu Z.Fang X.Menezes M.R.Balzeau J.Niu A.Hagan J.P.Kim D.H.doi:10.1159/0004842982017Cell. Physiol. Biochem.432200-2211SUBUNITStructural basis for amplifying vinculin activation by talin.Izard T.Vonrhein C.doi:10.1074/jbc.m4030762002004J. Biol. Chem.27927667-27678X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 1-258 IN COMPLEX WITH TLN1Vinculin activation by talin through helical bundle conversion.Izard T.Evans G.Borgon R.A.Rush C.L.Bricogne G.Bois P.R.J.doi:10.1038/nature022812004Nature427171-175X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-258 IN COMPLEX WITH TLN1Structural dynamics of alpha-actinin-vinculin interactions.Bois P.R.J.Borgon R.A.Vonrhein C.Izard T.doi:10.1128/mcb.25.14.6112-6122.20052005Mol. Cell. Biol.256112-6122X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-258 IN COMPLEX WITH ACTN4INTERACTION WITH ACTN4Metavinculin mutations alter actin interaction in dilated cardiomyopathy.Olson T.M.Illenberger S.Kishimoto N.Y.Huttelmaier S.Keating M.T.Jockusch B.M.doi:10.1161/hc0402.1029302002Circulation105431-437VARIANTS CMD1W LEU-954 DEL AND TRP-975CHARACTERIZATION OF VARIANT CMD1W TRP-975Identification of a metavinculin missense mutation, R975W, associated with both hypertrophic and dilated cardiomyopathy.Vasile V.C.Will M.L.Ommen S.R.Edwards W.D.Olson T.M.Ackerman M.J.doi:10.1016/j.ymgme.2005.08.0062006Mol. Genet. Metab.87169-174VARIANT CMD1W TRP-975VARIANTS VAL-934 AND ALA-943A missense mutation in a ubiquitously expressed protein, vinculin, confers susceptibility to hypertrophic cardiomyopathy.Vasile V.C.Ommen S.R.Edwards W.D.Ackerman M.J.doi:10.1016/j.bbrc.2006.04.1512006Biochem. Biophys. Res. Commun.345998-1003VARIANT CMH15 MET-277Wikipedia; Vinculin entry2.70A=1-2582.35A=1-258B=882-11342.42A=1-2582.90A/B=1-11341.80A=1-2582.72A=1-2583.97A=1-2583.20A=1-2582.75A/C=879-11342.90A/B/C/D=879-11348.20M=858-11292.20A=959-11301.61A/B=1-2581.97A/B=1-2521.99A=1-2552.76A=1-2572.54A=856-11342.25A=1-2582.66A=1-2521.00B=857-8671.41B=870-8793.20A/B/C/D/E/F=891-11343.10A/B/C/D=959-11342.75A/B/C/D=959-11302.76A/B=959-11343.40A/B/C/D=959-11342.90A=959-11342.45A=959-11344.00A/B=969-1134A=854-8703.00A=1-11342.90L/M=1-11344.17A=1-11344.15A=1-11344.50A=1-11344.27A=1-1134269Talin-1-Vinculin focal adhesion activation complex681 site, 1 O-linked glycan (1 site)1088 antibodies from 45 providershumanVCLLow tissue specificitygenephenotypephenotypeFamilial isolated dilated cardiomyopathyNON RARE IN EUROPE: Familial isolated hypertrophic cardiomyopathyEukaryotaPlatelet degranulationSmooth Muscle ContractionMAP2K and MAPK activationNeutrophil degranulationSignaling by moderate kinase activity BRAF mutantsSignaling by high-kinase activity BRAF mutantsSignaling by BRAF and RAF1 fusionsParadoxical activation of RAF signaling by kinase inactive BRAFSignaling downstream of RAS mutantsSignaling by RAF1 mutantsSignaling by ALK fusions and activated point mutants122 hits in 1153 CRISPR screenshumanTbioProteinExpressed in saphenous vein and 211 other cell types or tissuesbaseline and differentialAlpha-catenin/vinculin-likeVinculin, Vh2 four-helix bundleAlpha-catenin/vinculin-like_sfVinculinVinculin/cateninVinculin_CSVINCULINVINCULINVinculinVINCULINalpha-catenin/vinculin-likeVINCULIN_1VINCULIN_2HSVinculinMetavinculinMVVCLActin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.Exhibits self-association properties. Part of a complex composed of THSD1, PTK2/FAK1, TLN1 and VCL (PubMed:29069646). Interacts with APBB1IP and NRAP (By similarity). Interacts with TLN1. Interacts with CTNNB1 and this interaction is necessary for its localization to the cell-cell junctions and for its function in regulating cell surface expression of E-cadherin (By similarity). Interacts with SYNM. Interacts with SORBS1 (By similarity). Interacts with CTNNA1 (PubMed:26691986). Binds to ACTN4; this interaction triggers conformational changes (PubMed:15988023).(Microbial infection) Interacts via its globular head domain with the central portion of S.flexneri IcsA (also called VirG).Recruitment to cell-cell junctions occurs in a myosin II-dependent manner. Interaction with CTNNB1 is necessary for its localization to the cell-cell junctions.Metavinculin is muscle-specific.Exists in at least two conformations. When in the closed, 'inactive' conformation, extensive interactions between the head and tail domains prevent detectable binding to most of its ligands. It takes on an 'active' conformation after cooperative and simultaneous binding of two different ligands. This activation involves displacement of the head-tail interactions and leads to a significant accumulation of ternary complexes. The active form then binds a number of proteins that have both signaling and structural roles that are essential for cell adhesion.The N-terminal globular head (Vh) comprises of subdomains D1-D4. The C-terminal tail (Vt) binds F-actin and cross-links actin filaments into bundles. In isoform 2 (metavinculin) a 68 residue insertion in the tail domain promotes actin severing instead of bundling. An intramolecular interaction between Vh and Vt masks the F-actin-binding domain located in Vt. The binding of talin and alpha-actinin to the D1 subdomain of vinculin induces a helical bundle conversion of this subdomain, leading to the disruption of the intramolecular interaction and the exposure of the cryptic F-actin-binding domain of Vt. Vt inhibits actin filament barbed end elongation without affecting the critical concentration of actin assembly.Phosphorylated; on serines, threonines and tyrosines. Phosphorylation on Tyr-1133 in activated platelets affects head-tail interactions and cell spreading but has no effect on actin binding nor on localization to focal adhesion plaques (By similarity).Acetylated; mainly by myristic acid but also by a small amount of palmitic acid.The disease is caused by variants affecting the gene represented in this entry.The disease is caused by variants affecting the gene represented in this entry.Belongs to the vinculin/alpha-catenin family.Vinculin12379911134125936923704793480589N-terminal globular head835Talin-interaction1682083 X 112 AA tandem repeatsInteraction with ACTN4741764Linker (Pro-rich)836878Disordered857887C-terminal tail879Facilitates phospholipid membrane insertion10031046Facilitates phospholipid membrane insertion1120Pro residues859873Phosphoserine97N6-acetyllysine173Phosphoserine260Phosphoserine272Phosphoserine275Phosphoserine288Phosphoserine290Phosphoserine346Phosphoserine434N6-acetyllysine496Phosphotyrosine537Phosphoserine574Phosphoserine579Phosphoserine600Phosphothreonine604Phosphothreonine672Phosphoserine721Phosphoserine795Phosphoserine809Phosphotyrosine822Phosphotyrosine; by SRC-type Tyr-kinases1133In isoform 3.73In isoform 3.VRVLSGEISKIPNSPWLGVLIGTCLILYLVIFVA262295In isoform 3.296In isoform 1.916983L234In CMH15.M277V934A943In CMD1W.954In CMD1W; significantly alters metavinculin-mediated cross-linking of actin filaments.W97546713162628303335384041646810214514615015417918521822022222324825325525827428428528729431031533833934234334534735135339339439640242042544744845045545846048249350551453053556156456656857759861462062462565065568169071471974374677277779279480681181381483389690996497798610051009101110121037104310531056107210731076107710791081111311141117112211281130false3false2false3true7true4true6true3false3false2false3false3false3false3false6false3false3false3true2ABI2ARPC2TEKT1ipaAipaARrIowa_0797Sorbs1BCAR1CTNNA1FUSLPXNNEBLOPTNPRKNRAVER1SAPCD2SORBS3ACTA12007-01-234123799b2385af45cf68a62681c6fe17d3e8c6d2MetavinculinMPVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVAAVQAAVSNLVRVGKETVQTTEDQILKRDMPPAFIKVENACTKLVQAAQMLQSDPYSVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNSKNQGIEEALKNRNFTVEKMSAEINEIIRVLQLTSWDEDAWASKDTEAMKRALASIDSKLNQAKGWLRDPSASPGDAGEQAIRQILDEAGKVGELCAGKERREILGTCKMLGQMTDQVADLRARGQGSSPVAMQKAQQVSQGLDVLTAKVENAARKLEAMTNSKQSIAKKIDAAQNWLADPNGGPEGEEQIRGALAEARKIAELCDDPKERDDILRSLGEISALTSKLADLRRQGKGDSPEARALAKQVATALQNLQTKTNRAVANSRPAKAAVHLEGKIEQAQRWIDNPTVDDRGVGQAAIRGLVAEGHRLANVMMGPYRQDLLAKCDRVDQLTAQLADLAARGEGESPQARALASQLQDSLKDLKARMQEAMTQEVSDVFSDTTTPIKLLAVAATAPPDAPNREEVFDERAANFENHSGKLGATAEKAAAVGTANKSTVEGIQASVKTARELTPQVVSAARILLRNPGNQAAYEHFETMKNQWIDNVEKMTGLVDEAIDTKSLLDASEEAIKKDLDKCKVAMANIQPQMLVAGATSIARRANRILLVAKREVENSEDPKFREAVKAASDELSKTISPMVMDAKAVAGNISDPGLQKSFLDSGYRILGAVAKVREAFQPQEPDFPPPPPDLEQLRLTDELAPPKPPLPEGEVPPPRPPPPEEKDEEFPEQKAGEVINQPMMMAARQLHDEARKWSSKPGIPAAEVGIGVVAEADAADAAGFPVPPDMEDDYEPELLLMPSNQPVNQPILAAAQSLHREATKWSSKGNDIIAAAKRMALLMAEMSRLVRGGSGTKRALIQCAKDIAKASDEVTRLAKEVAKQCTDKRIRTNLLQVCERIPTISTQLKILSTVKATMLGRTNISDEESEQATEMLVHNAQNLMQSVKETVREAEAASIKIRTDAGFTLRWVRKTPWYQ1VinculinMPVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVAAVQAAVSNLVRVGKETVQTTEDQILKRDMPPAFIKVENACTKLVQAAQMLQSDPYSVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNSKNQGIEEALKNRNFTVEKMSAEINEIIRVLQLTSWDEDAWASKDTEAMKRALASIDSKLNQAKGWLRDPSASPGDAGEQAIRQILDEAGKVGELCAGKERREILGTCKMLGQMTDQVADLRARGQGSSPVAMQKAQQVSQGLDVLTAKVENAARKLEAMTNSKQSIAKKIDAAQNWLADPNGGPEGEEQIRGALAEARKIAELCDDPKERDDILRSLGEISALTSKLADLRRQGKGDSPEARALAKQVATALQNLQTKTNRAVANSRPAKAAVHLEGKIEQAQRWIDNPTVDDRGVGQAAIRGLVAEGHRLANVMMGPYRQDLLAKCDRVDQLTAQLADLAARGEGESPQARALASQLQDSLKDLKARMQEAMTQEVSDVFSDTTTPIKLLAVAATAPPDAPNREEVFDERAANFENHSGKLGATAEKAAAVGTANKSTVEGIQASVKTARELTPQVVSAARILLRNPGNQAAYEHFETMKNQWIDNVEKMTGLVDEAIDTKSLLDASEEAIKKDLDKCKVAMANIQPQMLVAGATSIARRANRILLVAKREVENSEDPKFREAVKAASDELSKTISPMVMDAKAVAGNISDPGLQKSFLDSGYRILGAVAKVREAFQPQEPDFPPPPPDLEQLRLTDELAPPKPPLPEGEVPPPRPPPPEEKDEEFPEQKAGEVINQPMMMAARQLHDEARKWSSKGNDIIAAAKRMALLMAEMSRLVRGGSGTKRALIQCAKDIAKASDEVTRLAKEVAKQCTDKRIRTNLLQVCERIPTISTQLKILSTVKATMLGRTNISDEESEQATEMLVHNAQNLMQSVKETVREAEAASIKIRTDAGFTLRWVRKTPWYQ3MPPAFIKVENACTKLVQAAQMLQSDPYSVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNSKNQGIEEALKNRNFTVEKMSAEINEIIRVLQLTSWDEDAWASKVRVLSGEISKIPNSPWLGVLIGTCLILYLVIFVAtruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetrue