ID NUDEL_DROME Reviewed; 2616 AA.
AC P98159; Q9VRX5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 01-MAY-2013, entry version 113.
DE RecName: Full=Serine protease nudel;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=ndl; ORFNames=CG10129;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Oregon-R; TISSUE=Ovary;
RX PubMed=7671306; DOI=10.1016/0092-8674(95)90475-1;
RA Hong C.C., Hashimoto C.;
RT "An unusual mosaic protein with a protease domain, encoded by the
RT nudel gene, is involved in defining embryonic dorsoventral polarity in
RT Drosophila.";
RL Cell 82:785-794(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a
RT systematic review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP CLEAVAGE OF EASTER.
RX PubMed=9477324;
RA Misra S., Hecht P., Maeda R., Anderson K.V.;
RT "Positive and negative regulation of Easter, a member of the serine
RT protease family that controls dorsal-ventral patterning in the
RT Drosophila embryo.";
RL Development 125:1261-1267(1998).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-220; SER-574;
RP SER-581; SER-1134 AND SER-1136, AND MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Component of the extracellular signaling pathway that
CC establishes the dorsal-ventral pathway of the embryo. Three
CC proteases; ndl, gd and snk process easter to create active easter.
CC Active easter defines cell identities along the dorsal-ventral
CC continuum by activating the spz ligand for the Tl receptor in the
CC ventral region of the embryo. Nudel, pipe and windbeutel together
CC trigger the protease cascade within the extraembryonic
CC perivitelline compartment which induces dorsoventral polarity of
CC the Drosophila embryo.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- TISSUE SPECIFICITY: Follicle.
CC -!- PTM: Requires cleavage for activation (presumably).
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC -!- SIMILARITY: Contains 11 LDL-receptor class A domains.
CC -!- SIMILARITY: Contains 2 peptidase S1 domains.
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DR EMBL; U29153; AAA83086.1; -; mRNA.
DR EMBL; AE014296; AAF50656.1; -; Genomic_DNA.
DR PIR; A57096; A57096.
DR RefSeq; NP_523947.2; NM_079223.2.
DR UniGene; Dm.2737; -.
DR ProteinModelPortal; P98159; -.
DR SMR; P98159; 891-1053, 1100-1379, 1727-1811, 2265-2461.
DR STRING; 7227.FBpp0076693; -.
DR MEROPS; S01.013; -.
DR PaxDb; P98159; -.
DR EnsemblMetazoa; FBtr0076984; FBpp0076693; FBgn0002926.
DR GeneID; 38738; -.
DR KEGG; dme:Dmel_CG10129; -.
DR UCSC; CG10129-RA; d. melanogaster.
DR CTD; 38738; -.
DR FlyBase; FBgn0002926; ndl.
DR eggNOG; COG5640; -.
DR GeneTree; ENSGT00700000104440; -.
DR InParanoid; P98159; -.
DR OMA; PNGEDER; -.
DR OrthoDB; EOG47SQVP; -.
DR PhylomeDB; P98159; -.
DR GenomeRNAi; 38738; -.
DR NextBio; 810123; -.
DR Bgee; P98159; -.
DR GermOnline; CG10129; Drosophila melanogaster.
DR GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; NAS:FlyBase.
DR GO; GO:0007343; P:egg activation; IMP:FlyBase.
DR GO; GO:0007306; P:eggshell chorion assembly; IMP:FlyBase.
DR GO; GO:0007313; P:maternal specification of dorsal/ventral axis, oocyte, soma encoded; TAS:FlyBase.
DR GO; GO:0016485; P:protein processing; IGI:FlyBase.
DR GO; GO:0006508; P:proteolysis; NAS:FlyBase.
DR GO; GO:0008063; P:Toll signaling pathway; TAS:FlyBase.
DR Gene3D; 4.10.400.10; -; 7.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR001254; Peptidase_S1.
DR InterPro; IPR018114; Peptidase_S1_AS.
DR InterPro; IPR015420; Peptidase_S1A_nudel.
DR InterPro; IPR009003; Trypsin-like_Pept_dom.
DR Pfam; PF09342; DUF1986; 1.
DR Pfam; PF00057; Ldl_recept_a; 4.
DR Pfam; PF00089; Trypsin; 1.
DR SMART; SM00192; LDLa; 9.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57424; LDL_rcpt_classA_cys-rich; 7.
DR SUPFAM; SSF50494; Pept_Ser_Cys; 2.
DR PROSITE; PS01209; LDLRA_1; 6.
DR PROSITE; PS50068; LDLRA_2; 8.
DR PROSITE; PS50240; TRYPSIN_DOM; 2.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Developmental protein; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydrolase; Phosphoprotein;
KW Protease; Reference proteome; Repeat; Secreted; Serine protease;
KW Signal; Zymogen.
FT SIGNAL 1 43 Potential.
FT CHAIN 44 2616 Serine protease nudel.
FT /FTId=PRO_0000028136.
FT REPEAT 261 269 WIID 1.
FT REPEAT 320 328 WIID 2.
FT REPEAT 399 407 WIID 3.
FT REPEAT 446 454 WIID 4.
FT REPEAT 477 485 WIID 5.
FT REPEAT 528 536 WIID 6.
FT DOMAIN 889 929 LDL-receptor class A 1.
FT DOMAIN 929 956 LDL-receptor class A 2; truncated.
FT DOMAIN 955 1006 LDL-receptor class A 3.
FT DOMAIN 1145 1383 Peptidase S1 1.
FT DOMAIN 1394 1432 LDL-receptor class A 4.
FT DOMAIN 1713 1743 LDL-receptor class A 5; truncated.
FT DOMAIN 1745 1775 LDL-receptor class A 6; truncated.
FT DOMAIN 1774 1813 LDL-receptor class A 7.
FT DOMAIN 2027 2301 Peptidase S1 2.
FT DOMAIN 2308 2346 LDL-receptor class A 8.
FT DOMAIN 2349 2389 LDL-receptor class A 9.
FT DOMAIN 2387 2419 LDL-receptor class A 10; truncated.
FT DOMAIN 2419 2459 LDL-receptor class A 11.
FT MOTIF 1031 1033 Cell attachment site (Potential).
FT COMPBIAS 1489 1702 Ser/Thr-rich.
FT ACT_SITE 1185 1185 Charge relay system (By similarity).
FT ACT_SITE 1233 1233 Charge relay system (By similarity).
FT ACT_SITE 1332 1332 Charge relay system (By similarity).
FT MOD_RES 215 215 Phosphoserine.
FT MOD_RES 220 220 Phosphoserine.
FT MOD_RES 574 574 Phosphoserine.
FT MOD_RES 581 581 Phosphoserine.
FT MOD_RES 1134 1134 Phosphoserine.
FT MOD_RES 1136 1136 Phosphoserine.
FT CARBOHYD 291 291 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 347 347 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 379 379 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 417 417 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 492 492 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 515 515 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 598 598 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 794 794 O-linked (Xyl...) (glycosaminoglycan)
FT (Potential).
FT CARBOHYD 827 827 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 829 829 O-linked (Xyl...) (glycosaminoglycan)
FT (Potential).
FT CARBOHYD 861 861 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 975 975 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1064 1064 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1445 1445 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1878 1878 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1956 1956 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 2023 2023 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 2144 2144 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 2173 2173 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 2197 2197 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 2237 2237 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 2269 2269 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 2420 2420 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 2556 2556 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 2601 2601 N-linked (GlcNAc...) (Potential).
FT DISULFID 891 905 By similarity.
FT DISULFID 899 918 By similarity.
FT DISULFID 912 927 By similarity.
FT DISULFID 957 982 By similarity.
FT DISULFID 964 995 By similarity.
FT DISULFID 989 1004 By similarity.
FT DISULFID 1170 1186 By similarity.
FT DISULFID 1276 1338 Potential.
FT DISULFID 1305 1317 By similarity.
FT DISULFID 1328 1359 By similarity.
FT DISULFID 1396 1408 By similarity.
FT DISULFID 1401 1421 By similarity.
FT DISULFID 1415 1430 By similarity.
FT DISULFID 1728 1745 By similarity.
FT DISULFID 1734 1764 By similarity.
FT DISULFID 1758 1773 By similarity.
FT DISULFID 1776 1789 By similarity.
FT DISULFID 1783 1802 By similarity.
FT DISULFID 1796 1811 By similarity.
FT DISULFID 2055 2071 By similarity.
FT DISULFID 2177 2230 By similarity.
FT DISULFID 2310 2320 By similarity.
FT DISULFID 2315 2333 By similarity.
FT DISULFID 2327 2344 By similarity.
FT DISULFID 2351 2364 By similarity.
FT DISULFID 2358 2377 By similarity.
FT DISULFID 2371 2387 By similarity.
FT DISULFID 2421 2435 By similarity.
FT DISULFID 2428 2448 By similarity.
FT DISULFID 2442 2457 By similarity.
FT CONFLICT 83 83 I -> T (in Ref. 1; AAA83086).
FT CONFLICT 120 120 F -> L (in Ref. 1; AAA83086).
FT CONFLICT 363 363 N -> T (in Ref. 1; AAA83086).
FT CONFLICT 831 831 Q -> R (in Ref. 1; AAA83086).
FT CONFLICT 864 864 N -> S (in Ref. 1; AAA83086).
FT CONFLICT 1150 1150 Y -> H (in Ref. 1; AAA83086).
FT CONFLICT 1344 1344 P -> A (in Ref. 1; AAA83086).
FT CONFLICT 1410 1410 A -> S (in Ref. 1; AAA83086).
FT CONFLICT 1607 1607 I -> M (in Ref. 1; AAA83086).
FT CONFLICT 1632 1632 K -> I (in Ref. 1; AAA83086).
FT CONFLICT 1670 1670 L -> P (in Ref. 1; AAA83086).
FT CONFLICT 1794 1794 S -> K (in Ref. 1; AAA83086).
FT CONFLICT 1863 1863 D -> N (in Ref. 1; AAA83086).
FT CONFLICT 1886 1888 HEM -> QEK (in Ref. 1; AAA83086).
FT CONFLICT 1903 1903 S -> A (in Ref. 1; AAA83086).
FT CONFLICT 2147 2147 H -> N (in Ref. 1; AAA83086).
SQ SEQUENCE 2616 AA; 292492 MW; 052F92CBAE9EB163 CRC64;
MNYNMDEMEA TRLLRHPRRW WSIGFGKRIV AISILVIIVL LFSLVYHGLV VEKIDQVQQI
AALNARHQVL FNQPFEEDQS ALIVSPQTLH FKLLDEDMNK DMEDSKNRRR KHMRQMLVKF
RLNKKHRMRR DLHGLDLLDP VRMEANMQHL YTKLRSKRAR EALSQLEHEF VRCKKHTPQD
CMSAFLRMYK MAKEVTEKME KMKAIMREQQ PKLESSSMES HEQKGTFSPA DLIQVTTAEA
TTVAVHATEK PARTKIKPSR ISWIIDGHDH DESPVYTDGA PKKETTKAPW NTTQLVEITT
TKIDATATER TTVESTTEKI SWILDHFDKP QEILRTTEGP GQRIIRNVTT TSASSEPIVD
TENTNSDHVP TTENGLVFNI TTDGPVETTK STAQRKLSFD WILDGEENVE PEVKSTNTTT
TTAATTTTGA TSETIIVTTE LPKITFDWII DGREVVEPQE TTTEVTGTTE RLRKMPFDWI
IDGEEVVEPQ ENVTTTTIAT TVAVSTTEIN ERIHNSTAYP TKPKPVKFDW IIDGGESSGE
VSTSSTSQPK LTTREAISNP ESPRSSHPLD NPTSIENMLE SFEQHEEQKP ILRVLNANES
SSETVTDGYE RQLWLKKFED QARPNQNELI DTFGTALDAK ALDKMGPKIN PLNGHTWNAA
DAQILSLCER VALRMRNKVA TMSDGETKEK GETFTASPSV QFTSRAPGGF PVSGETMKAS
AQFMFNPNFG MPSIPVCFYM TPANFRMPMW SNTPTFMGMQ GAHFGGSSNP GAGIFFVPQQ
FGPSGNFFGG SGGSGAGGQG ANIFSKNASP QKPTNGQQQV YCSYMQNQSG QGAGQSQTSS
QQQQGGQSAF SNANFKMRHA NQTNTANQQG QIIYASYAGL PQQPIQERSR CPEPDQFSCF
GQQECIPAAR WCDNVVDCSD GSDESACTCA DRVDEERLCD GYEDCPMGED ELGCFGCESL
AYSCYENPQD FAKRNRSTIS MCYSRLERCD GFMNCLNGRD EEQCSMLVTD VADHMSHGAS
ASEGYLYHNY RGDWHPVCNN GEKWAALACQ MDENSRMDHS ASLNVSFQTL TLPGPFIEPS
LHAGVHFAQA CHGRNSHDSL VDHVAYVKCP PMQCGLPSKS SMLEHSKRVR RAVSDSKEIV
GDGRIVGGSY TSALQWPFVV AIYRNGKFHC GGTIYSDRWI ISAAHCVINY GKYFYEVRAG
LLRRSSYSPA TQIQPVSHVV VHQAYERRSM RNDLSLLRLL NPLQFNRWVK PICLPDKGRT
TVGDDWIWGP VEHTLCTVVG WGAIREKGPS SDPMRQVIVP IRKKCTDPED QASEDICAGD
PDGGRDACQG DSGGPLFCRS VSNPDEFYLA GVVSHGNGCA RPQEFGVYTR VTLYLDWLEM
ATTPRLLPKL QPLQLCPGFI CVWGGKRCIA KRQRCDRNVD CLGGEDEVGC TYNFLPDMVG
GVRQNISTTT ESDYHPVKES EEKSKMREVI PIDDEDLKAE QDEEDLLKST TSLGQTETTQ
GPMDLSFAEQ ITSTTSDDLS ITDETTSTDF TVSDSATSPS TLLPTTTNPS TWLPSTNIET
STFSFTTTES EASTKQETLP TTVAQTTTIP TSTEDLKKLT DLVTEFIEST TFETTMEVET
TTLSLTSTDA PKLVTTEGVK ETTTTEDTTT ISSIVTLTTT PLATISTTIL TTEKHVAVTT
LAPTTTTESA KTTTTHSSST HSEKDQIQIP NKFVCKKMSQ IVDIMMRCDR KVDCEDGTDE
LDCTCKDYLK GSLKGLICDG KADCEDLTDE QNCVECQSNE FRCPLSKTCL PLSSRCDNKV
DCKFKEDEKD CFALTNGHDV HFDVHQQPKF SSTGIFSRNG HGVWRVVCAH ETGYHEHQAK
TADAVCALLG FNGAHYFNSS EFVTQHEMQP ITPELKGGRN RMSAQIHSMV GDNVQFTENE
VIIPELGHPS ASRPEKDRLL PRKCVGIYVE CNPYSNKTTP LKTFSAGQVV KEKPIEQVPV
LSPTIETHNT PNVHFKPQIP AMVVNKKDEI LDRLDKLIKS KKNKTILVNE QLHEAIEELH
WPWLADVYMN GDLWCIGVLI DKHWVMVHES CLSGIDLETH YVSVLLGGGK TKRSAHRSNH
EQIRRVDCFE GVPKSNVLLL HLERPVRFTH HVLPTFLPDS SHQNQSHARQ CISVLHDDAT
GRIKTVAITR IHNATNCDSC YKLQEKQPPA NLMRLLNVSA EDMASISEEV ELINGVAPTE
LPAITKFTTC NQFGLKNVSD AHHNPSDQGV LVCRDSHTGW FPTALFNYNN SDCQSFKQPF
GIRTLELVYK SLQDIIDKPS CKMLLPAPDC STHRCPLGTC LPQAAMCNGR SDCHDGSDEE
ETKCRQQKQQ CAPGEMKCRT SFKCVPKSKF CDHVPDCEDM TDEPTICSCF TYLQATDPSK
ICDGKRNCWD KSDESSVLCN CTADHFQCSS SPEDCIPRDF VCDKEKDCPN GEDERYCFGI
EHPLHLQKKD FWTNSQHTQP EIAPQYGQVI EQTYGIWHTK CFPKSKPPQV DEVREICKKL
GYNPYRQPSY RLIDDEENKP VHTYELADRQ GRSFSNESLM GKYRDSTKAL IISKFSPLQL
NERLTLFLKS SRPIAELVRW NATDSSMCYR LEIRCA
//
