JAG1_MOUSE
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 03-AUG-2022, entry version 195.
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.
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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; 5.
DR STRING; 10090.ENSMUSP00000028735; -.
DR GlyConnect; 2632; 1 N-Linked glycan (1 site).
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; Q9QXX0; -.
DR PRIDE; Q9QXX0; -.
DR ProteomicsDB; 269418; -.
DR ABCD; Q9QXX0; 1 sequenced antibody.
DR Antibodypedia; 4153; 924 antibodies from 43 providers.
DR DNASU; 16449; -.
DR Ensembl; ENSMUST00000028735; ENSMUSP00000028735; ENSMUSG00000027276.
DR GeneID; 16449; -.
DR KEGG; mmu:16449; -.
DR UCSC; uc008moz.2; mouse.
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; GWGGVTC; -.
DR OrthoDB; 72177at2759; -.
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 73 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 332 other tissues.
DR ExpressionAtlas; Q9QXX0; baseline and differential.
DR Genevisible; Q9QXX0; MM.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
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:0061314; P:Notch signaling involved in heart development; IMP:BHF-UCL.
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 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; IPR033108; Jag1.
DR InterPro; IPR026219; Jagged/Serrate.
DR InterPro; IPR011651; Notch_ligand_N.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR24049:SF18; PTHR24049:SF18; 3.
DR Pfam; PF01414; DSL; 1.
DR Pfam; PF00008; EGF; 11.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF07657; MNNL; 1.
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; SSF57184; SSF57184; 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.
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
