ID DLL4_MOUSE Reviewed; 686 AA.
AC Q9JI71; Q9DBU9; Q9JHZ7;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 27-MAR-2024, entry version 188.
DE RecName: Full=Delta-like protein 4;
DE AltName: Full=Drosophila Delta homolog 4;
DE Short=Delta4;
DE Flags: Precursor;
GN Name=Dll4;
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].
RC TISSUE=Adipose tissue;
RX PubMed=10837024;
RA Shutter J.R., Scully S., Fan W., Richards W.G., Kitajewski J.,
RA Deblandre G.A., Kintner C.R., Stark K.L.;
RT "Dll4, a novel Notch ligand expressed in arterial endothelium.";
RL Genes Dev. 14:1313-1318(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=11134954; DOI=10.1093/oxfordjournals.jbchem.a002832;
RA Yoneya T., Tahara T., Nagao K., Yamada Y., Yamamoto T., Miyatani S.,
RA Nishikawa M.;
RT "Molecular cloning of Delta-4, a new mouse and human Notch ligand.";
RL J. Biochem. 129:27-34(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/Ola;
RA Mailhos C., Lewis J., Ish-Horowicz D.;
RT "A novel Notch ligand expressed in embryonic and tumour vasculation.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and Mammary tumor;
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 [7]
RP FUNCTION IN RETINAL DEVELOPMENT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=22323600; DOI=10.1073/pnas.1115767109;
RA Luo H., Jin K., Xie Z., Qiu F., Li S., Zou M., Cai L., Hozumi K.,
RA Shima D.T., Xiang M.;
RT "Forkhead box N4 (Foxn4) activates Dll4-Notch signaling to suppress
RT photoreceptor cell fates of early retinal progenitors.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E553-E562(2012).
CC -!- FUNCTION: Involved in the Notch signaling pathway as Notch ligand
CC (PubMed:11134954). Activates NOTCH1 and NOTCH4. Involved in
CC angiogenesis; negatively regulates endothelial cell proliferation and
CC migration and angiogenic sprouting (By similarity). Essential for
CC retinal progenitor proliferation. Required for suppressing rod fates in
CC late retinal progenitors as well as for proper generation of other
CC retinal cell types (PubMed:22323600). During spinal cord neurogenesis,
CC inhibits V2a interneuron fate (By similarity).
CC {ECO:0000250|UniProtKB:Q9NR61, ECO:0000269|PubMed:11134954,
CC ECO:0000269|PubMed:22323600}.
CC -!- SUBUNIT: Interacts with NOTCH4. Interacts (via N-terminal DSL and MNNL
CC domains) with NOTCH1 (via EGF-like domains).
CC {ECO:0000250|UniProtKB:D3ZHH1}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in vascular endothelium. Expressed in
CC retina at least during embryogenesis. {ECO:0000269|PubMed:22323600}.
CC -!- DEVELOPMENTAL STAGE: At 14.5, expressed within the retina outer
CC neuroblastic layer. {ECO:0000269|PubMed:22323600}.
CC -!- DISRUPTION PHENOTYPE: Conditional knockdowns in retinal progenitors
CC have thinner retinas with occasional regions abnormally organized into
CC rosette-like structures in the outer nuclear layer and an optic nerve
CC with a reduced diameter. {ECO:0000269|PubMed:22323600}.
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; AF253469; AAF76428.1; -; mRNA.
DR EMBL; AF273454; AAF78785.1; -; mRNA.
DR EMBL; AB043893; BAB18580.1; -; mRNA.
DR EMBL; AK004739; BAB23520.1; -; mRNA.
DR EMBL; AL929318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC042497; AAH42497.1; -; mRNA.
DR EMBL; BC049130; AAH49130.1; -; mRNA.
DR CCDS; CCDS16600.1; -.
DR PIR; JC7569; JC7569.
DR RefSeq; NP_062327.2; NM_019454.3.
DR AlphaFoldDB; Q9JI71; -.
DR SMR; Q9JI71; -.
DR BioGRID; 207669; 3.
DR IntAct; Q9JI71; 4.
DR STRING; 10090.ENSMUSP00000099575; -.
DR GlyCosmos; Q9JI71; 5 sites, No reported glycans.
DR GlyGen; Q9JI71; 5 sites.
DR iPTMnet; Q9JI71; -.
DR PhosphoSitePlus; Q9JI71; -.
DR PaxDb; 10090-ENSMUSP00000099575; -.
DR ProteomicsDB; 277468; -.
DR ABCD; Q9JI71; 3 sequenced antibodies.
DR Antibodypedia; 5995; 1013 antibodies from 45 providers.
DR DNASU; 54485; -.
DR Ensembl; ENSMUST00000102517.4; ENSMUSP00000099575.4; ENSMUSG00000027314.7.
DR GeneID; 54485; -.
DR KEGG; mmu:54485; -.
DR UCSC; uc008ltr.2; mouse.
DR AGR; MGI:1859388; -.
DR CTD; 54567; -.
DR MGI; MGI:1859388; Dll4.
DR VEuPathDB; HostDB:ENSMUSG00000027314; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000157441; -.
DR HOGENOM; CLU_012574_1_0_1; -.
DR InParanoid; Q9JI71; -.
DR OMA; ICLAGCT; -.
DR OrthoDB; 5475408at2759; -.
DR PhylomeDB; Q9JI71; -.
DR TreeFam; TF351835; -.
DR Reactome; R-MMU-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus.
DR BioGRID-ORCS; 54485; 2 hits in 78 CRISPR screens.
DR PRO; PR:Q9JI71; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9JI71; Protein.
DR Bgee; ENSMUSG00000027314; Expressed in interventricular septum and 168 other cell types or tissues.
DR Genevisible; Q9JI71; MM.
DR GO; GO:0005886; C:plasma membrane; ISS:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005112; F:Notch binding; IDA:MGI.
DR GO; GO:0048018; F:receptor ligand activity; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR GO; GO:0003180; P:aortic valve morphogenesis; ISO:MGI.
DR GO; GO:0072554; P:blood vessel lumenization; IMP:BHF-UCL.
DR GO; GO:0001974; P:blood vessel remodeling; IMP:BHF-UCL.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:BHF-UCL.
DR GO; GO:0003209; P:cardiac atrium morphogenesis; IMP:BHF-UCL.
DR GO; GO:0003208; P:cardiac ventricle morphogenesis; IMP:BHF-UCL.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0035912; P:dorsal aorta morphogenesis; IMP:BHF-UCL.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IDA:MGI.
DR GO; GO:1903588; P:negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
DR GO; GO:0003344; P:pericardium morphogenesis; IMP:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IMP:UniProtKB.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:UniProtKB.
DR GO; GO:0061074; P:regulation of neural retina development; IMP:UniProtKB.
DR GO; GO:0050767; P:regulation of neurogenesis; IMP:MGI.
DR GO; GO:0030217; P:T cell differentiation; IDA:UniProtKB.
DR GO; GO:0060579; P:ventral spinal cord interneuron fate commitment; ISS:UniProtKB.
DR GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IMP:BHF-UCL.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 5.
DR Gene3D; 2.10.25.140; -; 1.
DR Gene3D; 2.60.40.3510; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 7.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR011651; Notch_ligand_N.
DR PANTHER; PTHR12916; CYTOCHROME C OXIDASE POLYPEPTIDE VIC-2; 1.
DR PANTHER; PTHR12916:SF4; NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1-RELATED; 1.
DR Pfam; PF01414; DSL; 1.
DR Pfam; PF00008; EGF; 4.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF21795; JAG1-like_EGF2; 1.
DR Pfam; PF07657; MNNL; 1.
DR PRINTS; PR00010; EGFBLOOD.
DR SMART; SM00051; DSL; 1.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 6.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS51051; DSL; 1.
DR PROSITE; PS00022; EGF_1; 8.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 8.
PE 1: Evidence at protein level;
KW Angiogenesis; Cell membrane; Developmental protein; Differentiation;
KW Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Neurogenesis;
KW Notch signaling pathway; Reference proteome; Repeat; Sensory transduction;
KW Signal; Transmembrane; Transmembrane helix; Vision.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..686
FT /note="Delta-like protein 4"
FT /id="PRO_0000007513"
FT TOPO_DOM 27..532
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 533..553
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 554..686
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 174..218
FT /note="DSL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00377"
FT DOMAIN 219..252
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 253..283
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 285..323
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 325..361
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 364..401
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 403..439
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 441..477
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 481..519
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 186..188
FT /note="Interaction with Notch1"
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1"
FT REGION 192..196
FT /note="Interaction with Notch1"
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1"
FT SITE 111
FT /note="Interaction with Notch1"
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1"
FT SITE 217
FT /note="Interaction with Notch1"
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..55
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1"
FT DISULFID 62..75
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1"
FT DISULFID 176..185
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1,
FT ECO:0000255|PROSITE-ProRule:PRU00377"
FT DISULFID 189..201
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1,
FT ECO:0000255|PROSITE-ProRule:PRU00377"
FT DISULFID 209..218
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1,
FT ECO:0000255|PROSITE-ProRule:PRU00377"
FT DISULFID 223..234
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 227..240
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 242..251
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 254..265
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1"
FT DISULFID 260..271
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1"
FT DISULFID 273..282
FT /evidence="ECO:0000250|UniProtKB:D3ZHH1,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 289..301
FT /evidence="ECO:0000250"
FT DISULFID 295..311
FT /evidence="ECO:0000250"
FT DISULFID 313..322
FT /evidence="ECO:0000250"
FT DISULFID 329..340
FT /evidence="ECO:0000250"
FT DISULFID 334..349
FT /evidence="ECO:0000250"
FT DISULFID 351..360
FT /evidence="ECO:0000250"
FT DISULFID 367..378
FT /evidence="ECO:0000250"
FT DISULFID 372..389
FT /evidence="ECO:0000250"
FT DISULFID 391..400
FT /evidence="ECO:0000250"
FT DISULFID 407..418
FT /evidence="ECO:0000250"
FT DISULFID 412..427
FT /evidence="ECO:0000250"
FT DISULFID 429..438
FT /evidence="ECO:0000250"
FT DISULFID 445..456
FT /evidence="ECO:0000250"
FT DISULFID 450..465
FT /evidence="ECO:0000250"
FT DISULFID 467..476
FT /evidence="ECO:0000250"
FT DISULFID 485..496
FT /evidence="ECO:0000250"
FT DISULFID 490..507
FT /evidence="ECO:0000250"
FT DISULFID 509..518
FT /evidence="ECO:0000250"
FT CONFLICT 419
FT /note="Q -> L (in Ref. 1; AAF76428 and 3; AAF78785)"
FT /evidence="ECO:0000305"
FT CONFLICT 527..528
FT /note="SF -> CS (in Ref. 3; AAF78785)"
FT /evidence="ECO:0000305"
FT CONFLICT 627
FT /note="G -> S (in Ref. 1; AAF76428 and 3; AAF78785)"
FT /evidence="ECO:0000305"
FT CONFLICT 639..649
FT /note="LGEKVPLRLHS -> IGQGATSVTH (in Ref. 3; AAF78785)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 686 AA; 74991 MW; E7DD4FC15C4AFFBA CRC64;
MTPASRSACR WALLLLAVLW PQQRAAGSGI FQLRLQEFVN QRGMLANGQS CEPGCRTFFR
ICLKHFQATF SEGPCTFGNV STPVLGTNSF VVRDKNSGSG RNPLQLPFNF TWPGTFSLNI
QAWHTPGDDL RPETSPGNSL ISQIIIQGSL AVGKIWRTDE QNDTLTRLSY SYRVICSDNY
YGESCSRLCK KRDDHFGHYE CQPDGSLSCL PGWTGKYCDQ PICLSGCHEQ NGYCSKPDEC
ICRPGWQGRL CNECIPHNGC RHGTCSIPWQ CACDEGWGGL FCDQDLNYCT HHSPCKNGST
CSNSGPKGYT CTCLPGYTGE HCELGLSKCA SNPCRNGGSC KDQENSYHCL CPPGYYGQHC
EHSTLTCADS PCFNGGSCRE RNQGSSYACE CPPNFTGSNC EKKVDRCTSN PCANGGQCQN
RGPSRTCRCR PGFTGTHCEL HISDCARSPC AHGGTCHDLE NGPVCTCPAG FSGRRCEVRI
THDACASGPC FNGATCYTGL SPNNFVCNCP YGFVGSRCEF PVGLPPSFPW VAVSLGVGLV
VLLVLLVMVV VAVRQLRLRR PDDESREAMN NLSDFQKDNL IPAAQLKNTN QKKELEVDCG
LDKSNCGKLQ NHTLDYNLAP GLLGRGGMPG KYPHSDKSLG EKVPLRLHSE KPECRISAIC
SPRDSMYQSV CLISEERNEC VIATEV
//
