Reviewed, UniProtKB/Swiss-Prot P98159 (NUDEL_DROME)

Names and origin

Protein names

Recommended name:
    Serine protease nudel
    EC=3.4.21.-

Gene names

Name:	ndl
ORF Names:	CG10129

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	2616 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Component of the extracellular signaling pathway that establishes the dorsal-ventral pathway of the embryo. Three proteases; ndl, gd and snk process easter to create active easter. Active easter defines cell identities along the dorsal-ventral continuum by activating the spz ligand for the Tl receptor in the ventral region of the embryo. Nudel, pipe and windbeutel together trigger the protease cascade within the extraembryonic perivitelline compartment which induces dorsoventral polarity of the Drosophila embryo. Ref.1
Subcellular location	Secreted › extracellular space › extracellular matrix. Ref.1
Tissue specificity	Follicle. Ref.1
Post-translational modification	Requires cleavage for activation (presumably).
Sequence similarities	Belongs to the peptidase S1 family. Contains 11 LDL-receptor class A domains. Contains 2 peptidase S1 domains.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Domain	Repeat Signal
Molecular function	Developmental protein Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Phosphoprotein Zymogen
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	Toll signaling pathway Traceable author statement. Source: FlyBase egg activation Inferred from mutant phenotype. Source: FlyBase eggshell chorion assembly Inferred from mutant phenotype. Source: FlyBase maternal specification of dorsal/ventral axis, oocyte, soma encoded Traceable author statement. Source: FlyBase protein processing Inferred from genetic interaction. Source: FlyBase proteolysis Traceable author statement. Source: FlyBase
Cellular component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	serine-type endopeptidase activity Non-traceable author statement. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 43	43	Potential
	Chain	44 – 2616	2573	Serine protease nudel		PRO_0000028136
Regions
	Repeat	261 – 269	9	WIID 1
	Repeat	320 – 328	9	WIID 2
	Repeat	399 – 407	9	WIID 3
	Repeat	446 – 454	9	WIID 4
	Repeat	477 – 485	9	WIID 5
	Repeat	528 – 536	9	WIID 6
	Domain	889 – 929	41	LDL-receptor class A 1
	Domain	929 – 956	28	LDL-receptor class A 2; truncated
	Domain	955 – 1006	52	LDL-receptor class A 3
	Domain	1145 – 1383	239	Peptidase S1 1
	Domain	1394 – 1432	39	LDL-receptor class A 4
	Domain	1713 – 1743	31	LDL-receptor class A 5; truncated
	Domain	1745 – 1775	31	LDL-receptor class A 6; truncated
	Domain	1774 – 1813	40	LDL-receptor class A 7
	Domain	2027 – 2301	275	Peptidase S1 2
	Domain	2308 – 2346	39	LDL-receptor class A 8
	Domain	2349 – 2389	41	LDL-receptor class A 9
	Domain	2387 – 2419	33	LDL-receptor class A 10; truncated
	Domain	2419 – 2459	41	LDL-receptor class A 11
	Motif	1031 – 1033	3	Cell attachment site Potential
	Compositional bias	1489 – 1702	214	Ser/Thr-rich
Sites
	Active site	1185	1	Charge relay system By similarity
	Active site	1233	1	Charge relay system By similarity
	Active site	1332	1	Charge relay system By similarity
Amino acid modifications
	Modified residue	215	1	Phosphoserine Ref.5
	Modified residue	220	1	Phosphoserine Ref.5
	Modified residue	574	1	Phosphoserine Ref.5
	Modified residue	581	1	Phosphoserine Ref.5
	Modified residue	1134	1	Phosphoserine Ref.5
	Modified residue	1136	1	Phosphoserine Ref.5
	Glycosylation	291	1	N-linked (GlcNAc...) Potential
	Glycosylation	347	1	N-linked (GlcNAc...) Potential
	Glycosylation	379	1	N-linked (GlcNAc...) Potential
	Glycosylation	417	1	N-linked (GlcNAc...) Potential
	Glycosylation	492	1	N-linked (GlcNAc...) Potential
	Glycosylation	515	1	N-linked (GlcNAc...) Potential
	Glycosylation	598	1	N-linked (GlcNAc...) Potential
	Glycosylation	794	1	O-linked (Xyl...) (glycosaminoglycan) Potential
	Glycosylation	827	1	N-linked (GlcNAc...) Potential
	Glycosylation	829	1	O-linked (Xyl...) (glycosaminoglycan) Potential
	Glycosylation	861	1	N-linked (GlcNAc...) Potential
	Glycosylation	975	1	N-linked (GlcNAc...) Potential
	Glycosylation	1064	1	N-linked (GlcNAc...) Potential
	Glycosylation	1445	1	N-linked (GlcNAc...) Potential
	Glycosylation	1878	1	N-linked (GlcNAc...) Potential
	Glycosylation	1956	1	N-linked (GlcNAc...) Potential
	Glycosylation	2023	1	N-linked (GlcNAc...) Potential
	Glycosylation	2144	1	N-linked (GlcNAc...) Potential
	Glycosylation	2173	1	N-linked (GlcNAc...) Potential
	Glycosylation	2197	1	N-linked (GlcNAc...) Potential
	Glycosylation	2237	1	N-linked (GlcNAc...) Potential
	Glycosylation	2269	1	N-linked (GlcNAc...) Potential
	Glycosylation	2420	1	N-linked (GlcNAc...) Potential
	Glycosylation	2556	1	N-linked (GlcNAc...) Potential
	Glycosylation	2601	1	N-linked (GlcNAc...) Potential
	Disulfide bond	891 ↔ 905		By similarity
	Disulfide bond	899 ↔ 918		By similarity
	Disulfide bond	912 ↔ 927		By similarity
	Disulfide bond	957 ↔ 982		By similarity
	Disulfide bond	964 ↔ 995		By similarity
	Disulfide bond	989 ↔ 1004		By similarity
	Disulfide bond	1170 ↔ 1186		By similarity
	Disulfide bond	1276 ↔ 1338		Potential
	Disulfide bond	1305 ↔ 1317		By similarity
	Disulfide bond	1328 ↔ 1359		By similarity
	Disulfide bond	1396 ↔ 1408		By similarity
	Disulfide bond	1401 ↔ 1421		By similarity
	Disulfide bond	1415 ↔ 1430		By similarity
	Disulfide bond	1728 ↔ 1745		By similarity
	Disulfide bond	1734 ↔ 1764		By similarity
	Disulfide bond	1758 ↔ 1773		By similarity
	Disulfide bond	1776 ↔ 1789		By similarity
	Disulfide bond	1783 ↔ 1802		By similarity
	Disulfide bond	1796 ↔ 1811		By similarity
	Disulfide bond	2055 ↔ 2071		By similarity
	Disulfide bond	2177 ↔ 2230		By similarity
	Disulfide bond	2310 ↔ 2320		By similarity
	Disulfide bond	2315 ↔ 2333		By similarity
	Disulfide bond	2327 ↔ 2344		By similarity
	Disulfide bond	2351 ↔ 2364		By similarity
	Disulfide bond	2358 ↔ 2377		By similarity
	Disulfide bond	2371 ↔ 2387		By similarity
	Disulfide bond	2421 ↔ 2435		By similarity
	Disulfide bond	2428 ↔ 2448		By similarity
	Disulfide bond	2442 ↔ 2457		By similarity
Experimental info
	Sequence conflict	83	1	I → T in AAA83086. Ref.1
	Sequence conflict	120	1	F → L in AAA83086. Ref.1
	Sequence conflict	363	1	N → T in AAA83086. Ref.1
	Sequence conflict	831	1	Q → R in AAA83086. Ref.1
	Sequence conflict	864	1	N → S in AAA83086. Ref.1
	Sequence conflict	1150	1	Y → H in AAA83086. Ref.1
	Sequence conflict	1344	1	P → A in AAA83086. Ref.1
	Sequence conflict	1410	1	A → S in AAA83086. Ref.1
	Sequence conflict	1607	1	I → M in AAA83086. Ref.1
	Sequence conflict	1632	1	K → I in AAA83086. Ref.1
	Sequence conflict	1670	1	L → P in AAA83086. Ref.1
	Sequence conflict	1794	1	S → K in AAA83086. Ref.1
	Sequence conflict	1863	1	D → N in AAA83086. Ref.1
	Sequence conflict	1886 – 1888	3	HEM → QEK in AAA83086. Ref.1
	Sequence conflict	1903	1	S → A in AAA83086. Ref.1
	Sequence conflict	2147	1	H → N in AAA83086. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P98159-1 [UniParc]. Last modified May 10, 2004. Version 2. Checksum: 052F92CBAE9EB163	FASTA	2,616	292,492
	10 20 30 40 50 60 MNYNMDEMEA TRLLRHPRRW WSIGFGKRIV AISILVIIVL LFSLVYHGLV VEKIDQVQQI 70 80 90 100 110 120 AALNARHQVL FNQPFEEDQS ALIVSPQTLH FKLLDEDMNK DMEDSKNRRR KHMRQMLVKF 130 140 150 160 170 180 RLNKKHRMRR DLHGLDLLDP VRMEANMQHL YTKLRSKRAR EALSQLEHEF VRCKKHTPQD 190 200 210 220 230 240 CMSAFLRMYK MAKEVTEKME KMKAIMREQQ PKLESSSMES HEQKGTFSPA DLIQVTTAEA 250 260 270 280 290 300 TTVAVHATEK PARTKIKPSR ISWIIDGHDH DESPVYTDGA PKKETTKAPW NTTQLVEITT 310 320 330 340 350 360 TKIDATATER TTVESTTEKI SWILDHFDKP QEILRTTEGP GQRIIRNVTT TSASSEPIVD 370 380 390 400 410 420 TENTNSDHVP TTENGLVFNI TTDGPVETTK STAQRKLSFD WILDGEENVE PEVKSTNTTT 430 440 450 460 470 480 TTAATTTTGA TSETIIVTTE LPKITFDWII DGREVVEPQE TTTEVTGTTE RLRKMPFDWI 490 500 510 520 530 540 IDGEEVVEPQ ENVTTTTIAT TVAVSTTEIN ERIHNSTAYP TKPKPVKFDW IIDGGESSGE 550 560 570 580 590 600 VSTSSTSQPK LTTREAISNP ESPRSSHPLD NPTSIENMLE SFEQHEEQKP ILRVLNANES 610 620 630 640 650 660 SSETVTDGYE RQLWLKKFED QARPNQNELI DTFGTALDAK ALDKMGPKIN PLNGHTWNAA 670 680 690 700 710 720 DAQILSLCER VALRMRNKVA TMSDGETKEK GETFTASPSV QFTSRAPGGF PVSGETMKAS 730 740 750 760 770 780 AQFMFNPNFG MPSIPVCFYM TPANFRMPMW SNTPTFMGMQ GAHFGGSSNP GAGIFFVPQQ 790 800 810 820 830 840 FGPSGNFFGG SGGSGAGGQG ANIFSKNASP QKPTNGQQQV YCSYMQNQSG QGAGQSQTSS 850 860 870 880 890 900 QQQQGGQSAF SNANFKMRHA NQTNTANQQG QIIYASYAGL PQQPIQERSR CPEPDQFSCF 910 920 930 940 950 960 GQQECIPAAR WCDNVVDCSD GSDESACTCA DRVDEERLCD GYEDCPMGED ELGCFGCESL 970 980 990 1000 1010 1020 AYSCYENPQD FAKRNRSTIS MCYSRLERCD GFMNCLNGRD EEQCSMLVTD VADHMSHGAS 1030 1040 1050 1060 1070 1080 ASEGYLYHNY RGDWHPVCNN GEKWAALACQ MDENSRMDHS ASLNVSFQTL TLPGPFIEPS 1090 1100 1110 1120 1130 1140 LHAGVHFAQA CHGRNSHDSL VDHVAYVKCP PMQCGLPSKS SMLEHSKRVR RAVSDSKEIV 1150 1160 1170 1180 1190 1200 GDGRIVGGSY TSALQWPFVV AIYRNGKFHC GGTIYSDRWI ISAAHCVINY GKYFYEVRAG 1210 1220 1230 1240 1250 1260 LLRRSSYSPA TQIQPVSHVV VHQAYERRSM RNDLSLLRLL NPLQFNRWVK PICLPDKGRT 1270 1280 1290 1300 1310 1320 TVGDDWIWGP VEHTLCTVVG WGAIREKGPS SDPMRQVIVP IRKKCTDPED QASEDICAGD 1330 1340 1350 1360 1370 1380 PDGGRDACQG DSGGPLFCRS VSNPDEFYLA GVVSHGNGCA RPQEFGVYTR VTLYLDWLEM 1390 1400 1410 1420 1430 1440 ATTPRLLPKL QPLQLCPGFI CVWGGKRCIA KRQRCDRNVD CLGGEDEVGC TYNFLPDMVG 1450 1460 1470 1480 1490 1500 GVRQNISTTT ESDYHPVKES EEKSKMREVI PIDDEDLKAE QDEEDLLKST TSLGQTETTQ 1510 1520 1530 1540 1550 1560 GPMDLSFAEQ ITSTTSDDLS ITDETTSTDF TVSDSATSPS TLLPTTTNPS TWLPSTNIET 1570 1580 1590 1600 1610 1620 STFSFTTTES EASTKQETLP TTVAQTTTIP TSTEDLKKLT DLVTEFIEST TFETTMEVET 1630 1640 1650 1660 1670 1680 TTLSLTSTDA PKLVTTEGVK ETTTTEDTTT ISSIVTLTTT PLATISTTIL TTEKHVAVTT 1690 1700 1710 1720 1730 1740 LAPTTTTESA KTTTTHSSST HSEKDQIQIP NKFVCKKMSQ IVDIMMRCDR KVDCEDGTDE 1750 1760 1770 1780 1790 1800 LDCTCKDYLK GSLKGLICDG KADCEDLTDE QNCVECQSNE FRCPLSKTCL PLSSRCDNKV 1810 1820 1830 1840 1850 1860 DCKFKEDEKD CFALTNGHDV HFDVHQQPKF SSTGIFSRNG HGVWRVVCAH ETGYHEHQAK 1870 1880 1890 1900 1910 1920 TADAVCALLG FNGAHYFNSS EFVTQHEMQP ITPELKGGRN RMSAQIHSMV GDNVQFTENE 1930 1940 1950 1960 1970 1980 VIIPELGHPS ASRPEKDRLL PRKCVGIYVE CNPYSNKTTP LKTFSAGQVV KEKPIEQVPV 1990 2000 2010 2020 2030 2040 LSPTIETHNT PNVHFKPQIP AMVVNKKDEI LDRLDKLIKS KKNKTILVNE QLHEAIEELH 2050 2060 2070 2080 2090 2100 WPWLADVYMN GDLWCIGVLI DKHWVMVHES CLSGIDLETH YVSVLLGGGK TKRSAHRSNH 2110 2120 2130 2140 2150 2160 EQIRRVDCFE GVPKSNVLLL HLERPVRFTH HVLPTFLPDS SHQNQSHARQ CISVLHDDAT 2170 2180 2190 2200 2210 2220 GRIKTVAITR IHNATNCDSC YKLQEKQPPA NLMRLLNVSA EDMASISEEV ELINGVAPTE 2230 2240 2250 2260 2270 2280 LPAITKFTTC NQFGLKNVSD AHHNPSDQGV LVCRDSHTGW FPTALFNYNN SDCQSFKQPF 2290 2300 2310 2320 2330 2340 GIRTLELVYK SLQDIIDKPS CKMLLPAPDC STHRCPLGTC LPQAAMCNGR SDCHDGSDEE 2350 2360 2370 2380 2390 2400 ETKCRQQKQQ CAPGEMKCRT SFKCVPKSKF CDHVPDCEDM TDEPTICSCF TYLQATDPSK 2410 2420 2430 2440 2450 2460 ICDGKRNCWD KSDESSVLCN CTADHFQCSS SPEDCIPRDF VCDKEKDCPN GEDERYCFGI 2470 2480 2490 2500 2510 2520 EHPLHLQKKD FWTNSQHTQP EIAPQYGQVI EQTYGIWHTK CFPKSKPPQV DEVREICKKL 2530 2540 2550 2560 2570 2580 GYNPYRQPSY RLIDDEENKP VHTYELADRQ GRSFSNESLM GKYRDSTKAL IISKFSPLQL 2590 2600 2610 NERLTLFLKS SRPIAELVRW NATDSSMCYR LEIRCA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"An unusual mosaic protein with a protease domain, encoded by the nudel gene, is involved in defining embryonic dorsoventral polarity in Drosophila." Hong C.C., Hashimoto C. Cell 82:785-794(1995) [PubMed: 7671306] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Strain: Oregon-R. Tissue: Ovary.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[4]	"Positive and negative regulation of Easter, a member of the serine protease family that controls dorsal-ventral patterning in the Drosophila embryo." Misra S., Hecht P., Maeda R., Anderson K.V. Development 125:1261-1267(1998) [PubMed: 9477324] [Abstract] Cited for: CLEAVAGE OF EASTER.
[5]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-220; SER-574; SER-581; SER-1134 AND SER-1136, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U29153 mRNA. Translation: AAA83086.1. AE014296 Genomic DNA. Translation: AAF50656.1.
PIR	A57096.
RefSeq	NP_523947.2.
UniGene	Dm.2737
3D structure databases
HSSP	HSSP built from PDB template 1FDP based on UniProtKB P00746.
ModBase	Search...
Protein-protein interaction databases
IntAct	P98159. 1 interaction.
Protein family/group databases
MEROPS	S01.013.
Genome annotation databases
Ensembl	FBgn0002926. Drosophila melanogaster. [Contig view]
GeneID	38738.
KEGG	dme:Dmel_CG10129.
NMPDR	fig|7227.3.peg.8553.
Organism-specific databases
FlyBase	FBgn0002926. ndl.
Phylogenomic databases
HOGENOM	P98159.
OMA	P98159. ASEDICA.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-015462-MON.
Gene expression databases
ArrayExpress	P98159.
GermOnline	CG10129. Drosophila melanogaster.
Family and domain databases
InterPro	IPR015420. DUF1986. IPR002172. LDL_rcpt_classA_cys-rich. IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view]
Gene3D	G3DSA:4.10.400.10. LDL_rcpt_classA_cys-rich. 5 hits.
Pfam	PF09342. DUF1986. 1 hit. PF00057. Ldl_recept_a. 5 hits. PF00089. Trypsin. 1 hit. [Graphical view]
PRINTS	PR00722. CHYMOTRYPSIN. PR00261. LDLRECEPTOR.
SMART	SM00192. LDLa. 9 hits. SM00020. Tryp_SPc. 1 hit. [Graphical view]
PROSITE	PS01209. LDLRA_1. 6 hits. PS50068. LDLRA_2. 8 hits. PS50240. TRYPSIN_DOM. 2 hits. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	810123.

Entry information

Entry name

NUDEL_DROME

Accession

Primary (citable) accession number: P98159
Secondary accession number(s): Q9VRX5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	May 10, 2004
Last modified:	June 16, 2009
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project