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P98159 (NUDEL_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine protease nudel

EC=3.4.21.-
Gene names
Name:ndl
ORF Names:CG10129
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length2616 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Secretedextracellular spaceextracellular 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 componentExtracellular matrix
Secreted
   DomainRepeat
Signal
   Molecular functionDevelopmental protein
Hydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processToll signaling pathway

Traceable author statement PubMed 1425342PubMed 8844153. Source: FlyBase

dorsal/ventral axis specification

Inferred from mutant phenotype PubMed 1904007PubMed 8844153. Source: FlyBase

egg activation

Inferred from mutant phenotype PubMed 12871909. Source: FlyBase

eggshell chorion assembly

Inferred from mutant phenotype PubMed 8844153. Source: FlyBase

maternal specification of dorsal/ventral axis, oocyte, soma encoded

Traceable author statement PubMed 1425342. Source: FlyBase

oocyte dorsal/ventral axis specification

Non-traceable author statement PubMed 10449356. Source: FlyBase

protein processing

Inferred from genetic interaction PubMed 1425342. Source: FlyBase

proteolysis

Non-traceable author statement PubMed 12568721. Source: FlyBase

   Cellular_componentproteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpeptidase activity

Traceable author statement PubMed 11700289. Source: FlyBase

serine-type endopeptidase activity

Non-traceable author statement PubMed 12568721. Source: FlyBase

serine-type peptidase activity

Non-traceable author statement PubMed 10449356. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4343 Potential
Chain44 – 26162573Serine protease nudel
PRO_0000028136

Regions

Repeat261 – 2699WIID 1
Repeat320 – 3289WIID 2
Repeat399 – 4079WIID 3
Repeat446 – 4549WIID 4
Repeat477 – 4859WIID 5
Repeat528 – 5369WIID 6
Domain889 – 92941LDL-receptor class A 1
Domain929 – 95628LDL-receptor class A 2; truncated
Domain955 – 100652LDL-receptor class A 3
Domain1145 – 1383239Peptidase S1 1
Domain1394 – 143239LDL-receptor class A 4
Domain1713 – 174331LDL-receptor class A 5; truncated
Domain1745 – 177531LDL-receptor class A 6; truncated
Domain1774 – 181340LDL-receptor class A 7
Domain2027 – 2301275Peptidase S1 2
Domain2308 – 234639LDL-receptor class A 8
Domain2349 – 238941LDL-receptor class A 9
Domain2387 – 241933LDL-receptor class A 10; truncated
Domain2419 – 245941LDL-receptor class A 11
Motif1031 – 10333Cell attachment site Potential
Compositional bias1489 – 1702214Ser/Thr-rich

Sites

Active site11851Charge relay system By similarity
Active site12331Charge relay system By similarity
Active site13321Charge relay system By similarity

Amino acid modifications

Modified residue2151Phosphoserine Ref.5
Modified residue2201Phosphoserine Ref.5
Modified residue5741Phosphoserine Ref.5
Modified residue5811Phosphoserine Ref.5
Modified residue11341Phosphoserine Ref.5
Modified residue11361Phosphoserine Ref.5
Glycosylation2911N-linked (GlcNAc...) Potential
Glycosylation3471N-linked (GlcNAc...) Potential
Glycosylation3791N-linked (GlcNAc...) Potential
Glycosylation4171N-linked (GlcNAc...) Potential
Glycosylation4921N-linked (GlcNAc...) Potential
Glycosylation5151N-linked (GlcNAc...) Potential
Glycosylation5981N-linked (GlcNAc...) Potential
Glycosylation7941O-linked (Xyl...) (glycosaminoglycan) Potential
Glycosylation8271N-linked (GlcNAc...) Potential
Glycosylation8291O-linked (Xyl...) (glycosaminoglycan) Potential
Glycosylation8611N-linked (GlcNAc...) Potential
Glycosylation9751N-linked (GlcNAc...) Potential
Glycosylation10641N-linked (GlcNAc...) Potential
Glycosylation14451N-linked (GlcNAc...) Potential
Glycosylation18781N-linked (GlcNAc...) Potential
Glycosylation19561N-linked (GlcNAc...) Potential
Glycosylation20231N-linked (GlcNAc...) Potential
Glycosylation21441N-linked (GlcNAc...) Potential
Glycosylation21731N-linked (GlcNAc...) Potential
Glycosylation21971N-linked (GlcNAc...) Potential
Glycosylation22371N-linked (GlcNAc...) Potential
Glycosylation22691N-linked (GlcNAc...) Potential
Glycosylation24201N-linked (GlcNAc...) Potential
Glycosylation25561N-linked (GlcNAc...) Potential
Glycosylation26011N-linked (GlcNAc...) Potential
Disulfide bond891 ↔ 905 By similarity
Disulfide bond899 ↔ 918 By similarity
Disulfide bond912 ↔ 927 By similarity
Disulfide bond957 ↔ 982 By similarity
Disulfide bond964 ↔ 995 By similarity
Disulfide bond989 ↔ 1004 By similarity
Disulfide bond1170 ↔ 1186 By similarity
Disulfide bond1276 ↔ 1338 Potential
Disulfide bond1305 ↔ 1317 By similarity
Disulfide bond1328 ↔ 1359 By similarity
Disulfide bond1396 ↔ 1408 By similarity
Disulfide bond1401 ↔ 1421 By similarity
Disulfide bond1415 ↔ 1430 By similarity
Disulfide bond1728 ↔ 1745 By similarity
Disulfide bond1734 ↔ 1764 By similarity
Disulfide bond1758 ↔ 1773 By similarity
Disulfide bond1776 ↔ 1789 By similarity
Disulfide bond1783 ↔ 1802 By similarity
Disulfide bond1796 ↔ 1811 By similarity
Disulfide bond2055 ↔ 2071 By similarity
Disulfide bond2177 ↔ 2230 By similarity
Disulfide bond2310 ↔ 2320 By similarity
Disulfide bond2315 ↔ 2333 By similarity
Disulfide bond2327 ↔ 2344 By similarity
Disulfide bond2351 ↔ 2364 By similarity
Disulfide bond2358 ↔ 2377 By similarity
Disulfide bond2371 ↔ 2387 By similarity
Disulfide bond2421 ↔ 2435 By similarity
Disulfide bond2428 ↔ 2448 By similarity
Disulfide bond2442 ↔ 2457 By similarity

Experimental info

Sequence conflict831I → T in AAA83086. Ref.1
Sequence conflict1201F → L in AAA83086. Ref.1
Sequence conflict3631N → T in AAA83086. Ref.1
Sequence conflict8311Q → R in AAA83086. Ref.1
Sequence conflict8641N → S in AAA83086. Ref.1
Sequence conflict11501Y → H in AAA83086. Ref.1
Sequence conflict13441P → A in AAA83086. Ref.1
Sequence conflict14101A → S in AAA83086. Ref.1
Sequence conflict16071I → M in AAA83086. Ref.1
Sequence conflict16321K → I in AAA83086. Ref.1
Sequence conflict16701L → P in AAA83086. Ref.1
Sequence conflict17941S → K in AAA83086. Ref.1
Sequence conflict18631D → N in AAA83086. Ref.1
Sequence conflict1886 – 18883HEM → QEK in AAA83086. Ref.1
Sequence conflict19031S → A in AAA83086. Ref.1
Sequence conflict21471H → N in AAA83086. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P98159 [UniParc].

Last modified May 10, 2004. Version 2.
Checksum: 052F92CBAE9EB163

FASTA2,616292,492
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-220; SER-574; SER-581; SER-1134 AND SER-1136, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U29153 mRNA. Translation: AAA83086.1.
AE014296 Genomic DNA. Translation: AAF50656.1.
PIRA57096.
RefSeqNP_523947.2. NM_079223.2.
UniGeneDm.2737.

3D structure databases

ProteinModelPortalP98159.
SMRP98159. Positions 897-1053, 1100-1379, 1727-1811, 2037-2151, 2311-2461.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid64189. 1 interaction.
STRING7227.FBpp0076693.

Protein family/group databases

MEROPSS01.013.

Proteomic databases

PaxDbP98159.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0076984; FBpp0076693; FBgn0002926.
GeneID38738.
KEGGdme:Dmel_CG10129.
UCSCCG10129-RA. d. melanogaster.

Organism-specific databases

CTD38738.
FlyBaseFBgn0002926. ndl.

Phylogenomic databases

eggNOGCOG5640.
GeneTreeENSGT00740000115494.
InParanoidP98159.
OMAPNGEDER.
OrthoDBEOG75B84T.
PhylomeDBP98159.

Gene expression databases

BgeeP98159.

Family and domain databases

Gene3D4.10.400.10. 7 hits.
InterProIPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR015420. Peptidase_S1A_nudel.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF09342. DUF1986. 1 hit.
PF00057. Ldl_recept_a. 4 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00261. LDLRECEPTOR.
SMARTSM00192. LDLa. 9 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 2 hits.
SSF57424. SSF57424. 7 hits.
PROSITEPS01209. 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]
ProtoNetSearch...

Other

GenomeRNAi38738.
NextBio810123.

Entry information

Entry nameNUDEL_DROME
AccessionPrimary (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: July 9, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase