DLL4_RAT
ID DLL4_RAT Reviewed; 686 AA.
AC D3ZHH1;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 3.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Delta-like protein 4 {ECO:0000303|PubMed:25700513};
DE AltName: Full=Drosophila Delta homolog 4 {ECO:0000305};
DE Short=Delta4 {ECO:0000305};
DE Flags: Precursor;
GN Name=Dll4 {ECO:0000312|RGD:1309740};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0007744|PDB:4XL1, ECO:0007744|PDB:4XLW}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 28-284 OF SER-29/LEU-108/PRO-207
RP MUTANT IN COMPLEX WITH NOTCH1, FUNCTION, GLYCOSYLATION AT ASN-79; ASN-109
RP AND ASN-162, DISULFIDE BONDS, AND MUTAGENESIS OF HIS-65; TYR-66; PHE-196
RP AND TYR-217.
RX PubMed=25700513; DOI=10.1126/science.1261093;
RA Luca V.C., Jude K.M., Pierce N.W., Nachury M.V., Fischer S., Garcia K.C.;
RT "Structural biology. Structural basis for Notch1 engagement of Delta-like
RT 4.";
RL Science 347:847-853(2015).
CC -!- FUNCTION: Involved in the Notch signaling pathway as Notch ligand.
CC Activates NOTCH1 and NOTCH4 (PubMed:25700513). Involved in
CC angiogenesis; negatively regulates endothelial cell proliferation and
CC migration and angiogenic sprouting. Essential for retinal progenitor
CC proliferation. Required for suppressing rod fates in late retinal
CC progenitors as well as for proper generation of other retinal cell
CC types. During spinal cord neurogenesis, inhibits V2a interneuron fate
CC (By similarity). {ECO:0000250|UniProtKB:Q9JI71,
CC ECO:0000250|UniProtKB:Q9NR61, ECO:0000269|PubMed:25700513}.
CC -!- SUBUNIT: Interacts with NOTCH4 (By similarity). Interacts (via N-
CC terminal DSL and MNNL domains) with NOTCH1 (via EGF-like domains)
CC (PubMed:25700513). {ECO:0000250|UniProtKB:Q9JI71,
CC ECO:0000269|PubMed:25700513}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:25700513};
CC Single-pass type I membrane protein {ECO:0000255|RuleBase:RU280815}.
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DR EMBL; AC132987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006234827.1; XM_006234765.2.
DR PDB; 4XL1; X-ray; 2.30 A; B/E=28-253.
DR PDB; 4XLW; X-ray; 3.39 A; B/D/F/H=28-284.
DR PDBsum; 4XL1; -.
DR PDBsum; 4XLW; -.
DR AlphaFoldDB; D3ZHH1; -.
DR SMR; D3ZHH1; -.
DR IntAct; D3ZHH1; 2.
DR STRING; 10116.ENSRNOP00000018970; -.
DR GlyGen; D3ZHH1; 3 sites.
DR iPTMnet; D3ZHH1; -.
DR PaxDb; D3ZHH1; -.
DR Ensembl; ENSRNOT00000117478; ENSRNOP00000091766; ENSRNOG00000014011.
DR GeneID; 311332; -.
DR UCSC; RGD:1309740; rat.
DR CTD; 54567; -.
DR RGD; 1309740; Dll4.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000157441; -.
DR HOGENOM; CLU_012574_1_0_1; -.
DR InParanoid; D3ZHH1; -.
DR OMA; CTEQNGY; -.
DR OrthoDB; 406049at2759; -.
DR PhylomeDB; D3ZHH1; -.
DR TreeFam; TF351835; -.
DR Reactome; R-RNO-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus.
DR PRO; PR:D3ZHH1; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000014011; Expressed in lung and 18 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005112; F:Notch binding; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0072554; P:blood vessel lumenization; ISO:RGD.
DR GO; GO:0001974; P:blood vessel remodeling; ISO:RGD.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISO:RGD.
DR GO; GO:0003209; P:cardiac atrium morphogenesis; ISO:RGD.
DR GO; GO:0003208; P:cardiac ventricle morphogenesis; ISO:RGD.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; ISO:RGD.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISO:RGD.
DR GO; GO:0035912; P:dorsal aorta morphogenesis; ISO:RGD.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:1903588; P:negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; ISO:RGD.
DR GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0061314; P:Notch signaling involved in heart development; ISO:RGD.
DR GO; GO:0007219; P:Notch signaling pathway; ISO:RGD.
DR GO; GO:0003344; P:pericardium morphogenesis; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; ISO:RGD.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISO:RGD.
DR GO; GO:0061074; P:regulation of neural retina development; ISO:RGD.
DR GO; GO:0050767; P:regulation of neurogenesis; ISO:RGD.
DR GO; GO:0030217; P:T cell differentiation; ISO:RGD.
DR GO; GO:0060579; P:ventral spinal cord interneuron fate commitment; ISO:RGD.
DR GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; ISO:RGD.
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 Pfam; PF01414; DSL; 1.
DR Pfam; PF00008; EGF; 4.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF07657; MNNL; 1.
DR SMART; SM00051; DSL; 1.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 6.
DR SUPFAM; SSF57184; SSF57184; 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 3D-structure; Cell membrane; Developmental protein; Disulfide bond;
KW EGF-like domain; Glycoprotein; Membrane; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..686
FT /note="Delta-like protein 4"
FT /id="PRO_5003053341"
FT TOPO_DOM 28..530
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 552..686
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
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 256..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 363..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:0000269|PubMed:25700513"
FT REGION 192..196
FT /note="Interaction with Notch1"
FT /evidence="ECO:0000269|PubMed:25700513"
FT SITE 111
FT /note="Interaction with Notch1"
FT /evidence="ECO:0000269|PubMed:25700513"
FT SITE 217
FT /note="Interaction with Notch1"
FT /evidence="ECO:0000269|PubMed:25700513"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25700513,
FT ECO:0007744|PDB:4XL1"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25700513,
FT ECO:0007744|PDB:4XL1"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25700513,
FT ECO:0007744|PDB:4XL1"
FT DISULFID 51..55
FT /evidence="ECO:0000269|PubMed:25700513,
FT ECO:0007744|PDB:4XL1, ECO:0007744|PDB:4XLW"
FT DISULFID 62..75
FT /evidence="ECO:0000269|PubMed:25700513,
FT ECO:0007744|PDB:4XL1, ECO:0007744|PDB:4XLW"
FT DISULFID 176..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00377,
FT ECO:0000269|PubMed:25700513, ECO:0007744|PDB:4XL1,
FT ECO:0007744|PDB:4XLW"
FT DISULFID 189..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00377,
FT ECO:0000269|PubMed:25700513, ECO:0007744|PDB:4XL1,
FT ECO:0007744|PDB:4XLW"
FT DISULFID 209..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00377,
FT ECO:0000269|PubMed:25700513, ECO:0007744|PDB:4XL1,
FT ECO:0007744|PDB:4XLW"
FT DISULFID 223..234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000269|PubMed:25700513, ECO:0007744|PDB:4XL1,
FT ECO:0007744|PDB:4XLW"
FT DISULFID 227..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000269|PubMed:25700513, ECO:0007744|PDB:4XL1,
FT ECO:0007744|PDB:4XLW"
FT DISULFID 242..251
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000269|PubMed:25700513, ECO:0007744|PDB:4XL1,
FT ECO:0007744|PDB:4XLW"
FT DISULFID 254..265
FT /evidence="ECO:0000269|PubMed:25700513,
FT ECO:0007744|PDB:4XLW"
FT DISULFID 260..271
FT /evidence="ECO:0000269|PubMed:25700513,
FT ECO:0007744|PDB:4XLW"
FT DISULFID 273..282
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000269|PubMed:25700513, ECO:0007744|PDB:4XLW"
FT DISULFID 289..301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 295..311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 313..322
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 329..340
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 334..349
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 351..360
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 367..378
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 372..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 391..400
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 407..418
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 412..427
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 429..438
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 445..456
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 450..465
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 467..476
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 485..496
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 490..507
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 509..518
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT MUTAGEN 65
FT /note="H->A: Strongly decreased binding to Notch1."
FT /evidence="ECO:0000269|PubMed:25700513"
FT MUTAGEN 66
FT /note="Y->A: Decreased binding to Notch1."
FT /evidence="ECO:0000269|PubMed:25700513"
FT MUTAGEN 196
FT /note="F->A: Strongly decreased binding to Notch1."
FT /evidence="ECO:0000269|PubMed:25700513"
FT MUTAGEN 217
FT /note="Y->A: No binding to Notch1."
FT /evidence="ECO:0000269|PubMed:25700513"
FT STRAND 29..39
FT /evidence="ECO:0007829|PDB:4XL1"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:4XL1"
FT STRAND 56..64
FT /evidence="ECO:0007829|PDB:4XL1"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:4XLW"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:4XL1"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:4XL1"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:4XL1"
FT STRAND 114..124
FT /evidence="ECO:0007829|PDB:4XL1"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:4XL1"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:4XL1"
FT STRAND 139..149
FT /evidence="ECO:0007829|PDB:4XL1"
FT STRAND 157..165
FT /evidence="ECO:0007829|PDB:4XL1"
FT STRAND 167..176
FT /evidence="ECO:0007829|PDB:4XL1"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:4XL1"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:4XL1"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:4XL1"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:4XL1"
FT TURN 248..251
FT /evidence="ECO:0007829|PDB:4XL1"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:4XLW"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:4XLW"
FT TURN 279..282
FT /evidence="ECO:0007829|PDB:4XLW"
SQ SEQUENCE 686 AA; 74961 MW; BB6B5EDC50CA8498 CRC64;
MTPGSRSACR WALLLLAVLW PQQRAAGSGI FQLRLQEFAN ERGMLANGRP CEPGCRTFFR
ICLKHYQATF SEGPCTFGNV STPVLGTNSF VIRDKNSGSG RNPLQLPFNF TWPGTFSLNI
QAWHTPGDDL RPETSPGNSL ISQIIIQGSL AVGKNWKSDE QNNTLTRLRY SYRVVCSDNY
YGDSCSRLCK KRDDHFGHYE CQPDGSLSCL PGWTGKYCDQ PICLSGCHEQ NGYCSKPDEC
NCRPGWQGPL CNECIPHNGC RHGTCTIPWQ CACDEGWGGL FCDQDLNYCT HHSPCKNGST
CSNSGPRGYT CTCLPGYTGE HCELELSKCA SNPCRNGGSC KDHENSYHCL CPPGYYGQHC
EHSTLTCADS PCFNGGSCRE RNQGASYACE CPPNFTGSNC EKKVDRCTSN PCANGGQCLN
RGPSRTCRCR PGFTGTHCEL HISDCARSPC AHGGTCHDLE NGPVCTCPAG FSGRRCEVRI
TNDACASGPC FNGATCYTGL SPNNFVCNCP YGFVGSRCEF PVGLPPSFPW VAVSLGVGLV
VLLVLLVMVA VAVRQLRLRR PDDDSREAMN NLSDFQKDNL IPAAQLKNTN QKKELEVDCG
LDKSNCGKLQ NHTLDYNLAP GFLGRGSTPG KYPHSDKSLG EKVPLRLHSE KPACRISAIC
SPRDSMYQSV CLISEERNEC VIATEV
