ID JAG1_MOUSE Reviewed; 1218 AA. AC Q9QXX0; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 204. DE RecName: Full=Protein jagged-1; DE Short=Jagged1; DE AltName: CD_antigen=CD339; DE Flags: Precursor; GN Name=Jag1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH NOTHC1; NOTHC2 AND NOTCH3. RC STRAIN=Swiss Webster / NIH; RX PubMed=10551863; DOI=10.1074/jbc.274.46.32961; RA Shimizu K., Chiba S., Kumano K., Hosoya N., Takahashi T., Kanda Y., RA Hamada Y., Yazaki Y., Hirai H.; RT "Mouse Jagged1 physically interacts with Notch2 and other Notch receptors: RT assessment by quantitative methods."; RL J. Biol. Chem. 274:32961-32969(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP TISSUE SPECIFICITY. RX PubMed=10556292; DOI=10.1093/hmg/8.13.2443; RA Loomes K.M., Underkoffler L.A., Morabito J., Gottlieb S., Piccoli D.A., RA Spinner N.B., Baldwin H.S., Oakey R.J.; RT "The expression of Jagged1 in the developing mammalian heart correlates RT with cardiovascular disease in Alagille syndrome."; RL Hum. Mol. Genet. 8:2443-2449(1999). RN [4] RP MUTAGENESIS OF SER-577. RX PubMed=32065591; DOI=10.1172/jci128152; RA Sullivan J.M., Motley W.W., Johnson J.O., Aisenberg W.H., Marshall K.L., RA Barwick K.E., Kong L., Huh J.S., Saavedra-Rivera P.C., McEntagart M.M., RA Marion M.H., Hicklin L.A., Modarres H., Baple E.L., Farah M.H., RA Zuberi A.R., Lutz C.M., Gaudet R., Traynor B.J., Crosby A.H., Sumner C.J.; RT "Dominant mutations of the Notch ligand Jagged1 cause peripheral RT neuropathy."; RL J. Clin. Invest. 130:1506-1512(2020). CC -!- FUNCTION: Ligand for multiple Notch receptors and involved in the CC mediation of Notch signaling. May be involved in cell-fate decisions CC during hematopoiesis. Seems to be involved in early and late stages of CC mammalian cardiovascular development. Inhibits myoblast differentiation CC (By similarity). May regulate fibroblast growth factor-induced CC angiogenesis. {ECO:0000250}. CC -!- SUBUNIT: Interacts with NOTCH1, NOTCH2 and NOTCH3. CC {ECO:0000269|PubMed:10551863}. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. CC Cell membrane {ECO:0000250|UniProtKB:P78504}. CC -!- TISSUE SPECIFICITY: Widely expressed in many tissues, with highest CC expression in brain, heart, muscle and thymus. CC {ECO:0000269|PubMed:10556292}. CC -!- DEVELOPMENTAL STAGE: At 8.75-9.75 dpc expression was detected in CC structures that include those destined to contribute to the CC cardiovascular system of the adult heart. Expression was also detected CC in the mesencephalon and rhombencephalon. CC -!- DOMAIN: The DSL domain is indispensable and sufficient for binding to CC NOTCH2. 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; AF171092; AAF15505.1; -; mRNA. DR EMBL; BC058675; AAH58675.1; -; mRNA. DR CCDS; CCDS16797.1; -. DR RefSeq; NP_038850.1; NM_013822.5. DR AlphaFoldDB; Q9QXX0; -. DR BMRB; Q9QXX0; -. DR SASBDB; Q9QXX0; -. DR SMR; Q9QXX0; -. DR BioGRID; 200854; 6. DR STRING; 10090.ENSMUSP00000028735; -. DR GlyConnect; 2632; 1 N-Linked glycan (1 site). DR GlyCosmos; Q9QXX0; 9 sites, 1 glycan. DR GlyGen; Q9QXX0; 9 sites, 1 N-linked glycan (1 site). DR iPTMnet; Q9QXX0; -. DR PhosphoSitePlus; Q9QXX0; -. DR SwissPalm; Q9QXX0; -. DR MaxQB; Q9QXX0; -. DR PaxDb; 10090-ENSMUSP00000028735; -. DR ProteomicsDB; 269418; -. DR Pumba; Q9QXX0; -. DR ABCD; Q9QXX0; 1 sequenced antibody. DR Antibodypedia; 4153; 1058 antibodies from 43 providers. DR DNASU; 16449; -. DR Ensembl; ENSMUST00000028735.8; ENSMUSP00000028735.8; ENSMUSG00000027276.8. DR GeneID; 16449; -. DR KEGG; mmu:16449; -. DR UCSC; uc008moz.2; mouse. DR AGR; MGI:1095416; -. DR CTD; 182; -. DR MGI; MGI:1095416; Jag1. DR VEuPathDB; HostDB:ENSMUSG00000027276; -. DR eggNOG; KOG1217; Eukaryota. DR GeneTree; ENSGT00940000160148; -. DR HOGENOM; CLU_004732_0_0_1; -. DR InParanoid; Q9QXX0; -. DR OMA; MAIGPCI; -. DR OrthoDB; 5475408at2759; -. DR PhylomeDB; Q9QXX0; -. DR TreeFam; TF351835; -. DR Reactome; R-MMU-9013149; RAC1 GTPase cycle. DR Reactome; R-MMU-9013423; RAC3 GTPase cycle. DR Reactome; R-MMU-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus. DR BioGRID-ORCS; 16449; 1 hit in 78 CRISPR screens. DR ChiTaRS; Jag1; mouse. DR PRO; PR:Q9QXX0; -. DR Proteomes; UP000000589; Chromosome 2. DR RNAct; Q9QXX0; Protein. DR Bgee; ENSMUSG00000027276; Expressed in secondary oocyte and 334 other cell types or tissues. DR ExpressionAtlas; Q9QXX0; baseline and differential. DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB. DR GO; GO:0045177; C:apical part of cell; IDA:UniProtKB. DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB. DR GO; GO:0060090; F:molecular adaptor activity; ISO:MGI. DR GO; GO:0005112; F:Notch binding; IPI:UniProtKB. DR GO; GO:0005543; F:phospholipid binding; ISO:MGI. DR GO; GO:0048018; F:receptor ligand activity; ISO:MGI. DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI. DR GO; GO:0035909; P:aorta morphogenesis; IMP:BHF-UCL. DR GO; GO:0001974; P:blood vessel remodeling; IMP:MGI. DR GO; GO:0043010; P:camera-type eye development; IMP:MGI. DR GO; GO:0061309; P:cardiac neural crest cell development involved in outflow tract morphogenesis; IMP:BHF-UCL. DR GO; GO:0003215; P:cardiac right ventricle morphogenesis; IMP:BHF-UCL. DR GO; GO:0060411; P:cardiac septum morphogenesis; IMP:BHF-UCL. DR GO; GO:0061073; P:ciliary body morphogenesis; IMP:MGI. DR GO; GO:0072017; P:distal tubule development; IEP:UniProtKB. DR GO; GO:0061444; P:endocardial cushion cell development; IMP:BHF-UCL. DR GO; GO:0002085; P:inhibition of neuroepithelial cell differentiation; IMP:MGI. DR GO; GO:0042491; P:inner ear auditory receptor cell differentiation; IMP:MGI. DR GO; GO:0048839; P:inner ear development; IMP:UniProtKB. DR GO; GO:0072070; P:loop of Henle development; IEP:UniProtKB. DR GO; GO:0002011; P:morphogenesis of an epithelial sheet; IMP:MGI. DR GO; GO:0045596; P:negative regulation of cell differentiation; ISO:MGI. DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI. DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISO:MGI. DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISO:MGI. DR GO; GO:0045602; P:negative regulation of endothelial cell differentiation; IDA:BHF-UCL. DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IDA:MGI. DR GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:MGI. DR GO; GO:2000737; P:negative regulation of stem cell differentiation; ISO:MGI. DR GO; GO:0072006; P:nephron development; IMP:UniProtKB. DR GO; GO:0061101; P:neuroendocrine cell differentiation; IMP:MGI. DR GO; GO:0030182; P:neuron differentiation; IMP:MGI. DR GO; GO:0097150; P:neuronal stem cell population maintenance; IEA:Ensembl. DR GO; GO:0007219; P:Notch signaling pathway; IDA:MGI. DR GO; GO:0072015; P:podocyte development; IMP:UniProtKB. DR GO; GO:0062043; P:positive regulation of cardiac epithelial to mesenchymal transition; ISO:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI. DR GO; GO:0045639; P:positive regulation of myeloid cell differentiation; IDA:MGI. DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:UniProtKB. DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL. DR GO; GO:0061156; P:pulmonary artery morphogenesis; ISS:BHF-UCL. DR GO; GO:0003184; P:pulmonary valve morphogenesis; ISS:BHF-UCL. DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:MGI. DR GO; GO:0050678; P:regulation of epithelial cell proliferation; IGI:MGI. DR GO; GO:2000241; P:regulation of reproductive process; IGI:MGI. DR GO; GO:0032495; P:response to muramyl dipeptide; IDA:BHF-UCL. DR GO; GO:0002456; P:T cell mediated immunity; ISO:MGI. DR CDD; cd00054; EGF_CA; 13. DR Gene3D; 2.10.25.140; -; 1. DR Gene3D; 2.60.40.3510; -; 1. DR Gene3D; 2.10.25.10; Laminin; 15. DR InterPro; IPR001774; DSL. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site. DR InterPro; IPR018097; EGF_Ca-bd_CS. DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf. DR InterPro; IPR026219; Jagged/Serrate. DR InterPro; IPR011651; Notch_ligand_N. DR InterPro; IPR001007; VWF_dom. DR PANTHER; PTHR24049; CRUMBS FAMILY MEMBER; 1. DR PANTHER; PTHR24049:SF29; NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1; 1. DR Pfam; PF21700; DL-JAG_EGF-like; 1. DR Pfam; PF01414; DSL; 1. DR Pfam; PF00008; EGF; 9. DR Pfam; PF12661; hEGF; 3. DR Pfam; PF07657; MNNL; 1. DR PRINTS; PR00010; EGFBLOOD. DR PRINTS; PR02059; JAGGEDFAMILY. DR SMART; SM00051; DSL; 1. DR SMART; SM00181; EGF; 16. DR SMART; SM00179; EGF_CA; 14. DR SMART; SM00214; VWC; 1. DR SMART; SM00215; VWC_out; 1. DR SUPFAM; SSF57196; EGF/Laminin; 4. DR SUPFAM; SSF57184; Growth factor receptor domain; 3. DR PROSITE; PS00010; ASX_HYDROXYL; 10. DR PROSITE; PS51051; DSL; 1. DR PROSITE; PS00022; EGF_1; 16. DR PROSITE; PS01186; EGF_2; 12. DR PROSITE; PS50026; EGF_3; 15. DR PROSITE; PS01187; EGF_CA; 8. DR Genevisible; Q9QXX0; MM. PE 1: Evidence at protein level; KW Calcium; Cell membrane; Developmental protein; Disulfide bond; KW EGF-like domain; Glycoprotein; Membrane; Notch signaling pathway; KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..33 FT /evidence="ECO:0000255" FT CHAIN 34..1218 FT /note="Protein jagged-1" FT /id="PRO_0000007626" FT TOPO_DOM 34..1067 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1068..1093 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1094..1218 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 185..229 FT /note="DSL" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00377" FT DOMAIN 230..263 FT /note="EGF-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 264..294 FT /note="EGF-like 2; atypical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 296..334 FT /note="EGF-like 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 336..372 FT /note="EGF-like 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 374..410 FT /note="EGF-like 5; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 412..448 FT /note="EGF-like 6; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 450..485 FT /note="EGF-like 7; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 487..523 FT /note="EGF-like 8; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 525..561 FT /note="EGF-like 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 586..627 FT /note="EGF-like 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 629..665 FT /note="EGF-like 11; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 667..703 FT /note="EGF-like 12; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 705..741 FT /note="EGF-like 13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 744..780 FT /note="EGF-like 14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 782..818 FT /note="EGF-like 15; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 820..856 FT /note="EGF-like 16; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT REGION 199..207 FT /note="Important for interaction with NOTCH1" FT /evidence="ECO:0000250" FT REGION 1181..1218 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1190..1209 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 143 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 217 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 382 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 559 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 745 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 960 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 991 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1045 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1064 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 187..196 FT /evidence="ECO:0000250" FT DISULFID 200..212 FT /evidence="ECO:0000250" FT DISULFID 220..229 FT /evidence="ECO:0000250" FT DISULFID 234..245 FT /evidence="ECO:0000250" FT DISULFID 238..251 FT /evidence="ECO:0000250" FT DISULFID 253..262 FT /evidence="ECO:0000250" FT DISULFID 265..276 FT /evidence="ECO:0000250" FT DISULFID 271..282 FT /evidence="ECO:0000250" FT DISULFID 284..293 FT /evidence="ECO:0000250" FT DISULFID 300..312 FT /evidence="ECO:0000250" FT DISULFID 306..322 FT /evidence="ECO:0000250" FT DISULFID 324..333 FT /evidence="ECO:0000250" FT DISULFID 340..351 FT /evidence="ECO:0000250" FT DISULFID 345..360 FT /evidence="ECO:0000250" FT DISULFID 362..371 FT /evidence="ECO:0000250" FT DISULFID 378..389 FT /evidence="ECO:0000250" FT DISULFID 383..398 FT /evidence="ECO:0000250" FT DISULFID 400..409 FT /evidence="ECO:0000250" FT DISULFID 416..427 FT /evidence="ECO:0000250" FT DISULFID 421..436 FT /evidence="ECO:0000250" FT DISULFID 438..447 FT /evidence="ECO:0000250" FT DISULFID 454..464 FT /evidence="ECO:0000250" FT DISULFID 458..473 FT /evidence="ECO:0000250" FT DISULFID 475..484 FT /evidence="ECO:0000250" FT DISULFID 491..502 FT /evidence="ECO:0000250" FT DISULFID 496..511 FT /evidence="ECO:0000250" FT DISULFID 513..522 FT /evidence="ECO:0000250" FT DISULFID 529..540 FT /evidence="ECO:0000250" FT DISULFID 534..549 FT /evidence="ECO:0000250" FT DISULFID 551..560 FT /evidence="ECO:0000250" FT DISULFID 578..605 FT /evidence="ECO:0000250" FT DISULFID 599..615 FT /evidence="ECO:0000250" FT DISULFID 617..626 FT /evidence="ECO:0000250" FT DISULFID 633..644 FT /evidence="ECO:0000250" FT DISULFID 638..653 FT /evidence="ECO:0000250" FT DISULFID 655..664 FT /evidence="ECO:0000250" FT DISULFID 671..682 FT /evidence="ECO:0000250" FT DISULFID 676..691 FT /evidence="ECO:0000250" FT DISULFID 693..702 FT /evidence="ECO:0000250" FT DISULFID 709..720 FT /evidence="ECO:0000250" FT DISULFID 714..729 FT /evidence="ECO:0000250" FT DISULFID 731..740 FT /evidence="ECO:0000250" FT DISULFID 748..759 FT /evidence="ECO:0000250" FT DISULFID 753..768 FT /evidence="ECO:0000250" FT DISULFID 770..779 FT /evidence="ECO:0000250" FT DISULFID 786..797 FT /evidence="ECO:0000250" FT DISULFID 791..806 FT /evidence="ECO:0000250" FT DISULFID 808..817 FT /evidence="ECO:0000250" FT DISULFID 824..835 FT /evidence="ECO:0000250" FT DISULFID 829..844 FT /evidence="ECO:0000250" FT DISULFID 846..855 FT /evidence="ECO:0000250" FT MUTAGEN 577 FT /note="S->R: Heterozygous mutant mice exhibit mild FT peripheral neuropathy. Homozygous expression results in FT embryonic lethality by midgestation." FT /evidence="ECO:0000269|PubMed:32065591" SQ SEQUENCE 1218 AA; 134164 MW; 77739F8928BB793C CRC64; MRSPRTRGRP GRPLSLLLAL LCALRAKVCG ASGQFELEIL SMQNVNGELQ NGNCCGGVRN PGDRKCTRDE CDTYFKVCLK EYQSRVTAGG PCSFGSGSTP VIGGNTFNLK ASRGNDRNRI VLPFSFAWPR SYTLLVEAWD SSNDTIQPDS IIEKASHSGM INPSRQWQTL KQNTGIAHFE YQIRVTCDDH YYGFGCNKFC RPRDDFFGHY ACDQNGNKTC MEGWMGPDCN KAICRQGCSP KHGSCKLPGD CRCQYGWQGL YCDKCIPHPG CVHGTCNEPW QCLCETNWGG QLCDKDLNYC GTHQPCLNRG TCSNTGPDKY QCSCPEGYSG PNCEIAEHAC LSDPCHNRGS CKETSSGFEC ECSPGWTGPT CSTNIDDCSP NNCSHGGTCQ DLVNGFKCVC PPQWTGKTCQ LDANECEAKP CVNARSCKNL IASYYCDCLP GWMGQNCDIN INDCLGQCQN DASCRDLVNG YRCICPPGYA GDHCERDIDE CASNPCLNGG HCQNEINRFQ CLCPTGFSGN LCQLDIDYCE PNPCQNGAQC YNRASDYFCK CPEDYEGKNC SHLKDHCRTT TCEVIDSCTV AMASNDTPEG VRYISSNVCG PHGKCKSQSG GKFTCDCNKG FTGTYCHENI NDCESNPCKN GGTCIDGVNS YKCICSDGWE GAHCENNIND CSQNPCHYGG TCRDLVNDFY CDCKNGWKGK TCHSRDSQCD EATCNNGGTC YDEVDTFKCM CPGGWEGTTC NIARNSSCLP NPCHNGGTCV VNGDSFTCVC KEGWEGPICT QNTNDCSPHP CYNSGTCVDG DNWYRCECAP GFAGPDCRIN INECQSSPCA FGATCVDEIN GYQCICPPGH SGAKCHEVSG RSCITMGRVI LDGAKWDDDC NTCQCLNGRV ACSKVWCGPR PCRLHKSHNE CPSGQSCIPV LDDQCFVRPC TGVGECRSSS LQPVKTKCTS DSYYQDNCAN ITFTFNKEMM SPGLTTEHIC SELRNLNILK NVSAEYSIYI ACEPSLSANN EIHVAISAED IRDDGNPVKE ITDKIIDLVS KRDGNSSLIA AVAEVRVQRR PLKNRTDFLV PLLSSVLTVA WVCCLVTAFY WCVRKRRKPS SHTHSAPEDN TTNNVREQLN QIKNPIEKHG ANTVPIKDYE NKNSKMSKIR THNSEVEEDD MDKHQQKVRF AKQPVYTLVD REEKAPSGTP TKHPNWTNKQ DNRDLESAQS LNRMEYIV //