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P98159

- NUDEL_DROME

UniProt

P98159 - NUDEL_DROME

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Protein

Serine protease nudel

Gene

ndl

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1185 – 11851Charge relay systemBy similarity
Active sitei1233 – 12331Charge relay systemBy similarity
Active sitei1332 – 13321Charge relay systemBy similarity

GO - Molecular functioni

  1. peptidase activity Source: FlyBase
  2. serine-type endopeptidase activity Source: FlyBase
  3. serine-type peptidase activity Source: FlyBase

GO - Biological processi

  1. dorsal/ventral axis specification Source: FlyBase
  2. egg activation Source: FlyBase
  3. eggshell chorion assembly Source: FlyBase
  4. maternal specification of dorsal/ventral axis, oocyte, soma encoded Source: FlyBase
  5. oocyte dorsal/ventral axis specification Source: FlyBase
  6. protein processing Source: FlyBase
  7. proteolysis Source: FlyBase
  8. Toll signaling pathway Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS01.013.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine protease nudel (EC:3.4.21.-)
Gene namesi
Name:ndl
ORF Names:CG10129
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0002926. ndl.

Subcellular locationi

Secretedextracellular spaceextracellular matrix 1 Publication

GO - Cellular componenti

  1. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4343Sequence AnalysisAdd
BLAST
Chaini44 – 26162573Serine protease nudelPRO_0000028136Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei215 – 2151Phosphoserine1 Publication
Modified residuei220 – 2201Phosphoserine1 Publication
Glycosylationi291 – 2911N-linked (GlcNAc...)Sequence Analysis
Glycosylationi347 – 3471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi379 – 3791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi417 – 4171N-linked (GlcNAc...)Sequence Analysis
Glycosylationi492 – 4921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi515 – 5151N-linked (GlcNAc...)Sequence Analysis
Modified residuei574 – 5741Phosphoserine1 Publication
Modified residuei581 – 5811Phosphoserine1 Publication
Glycosylationi598 – 5981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi794 – 7941O-linked (Xyl...) (glycosaminoglycan)Sequence Analysis
Glycosylationi827 – 8271N-linked (GlcNAc...)Sequence Analysis
Glycosylationi829 – 8291O-linked (Xyl...) (glycosaminoglycan)Sequence Analysis
Glycosylationi861 – 8611N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi891 ↔ 905By similarity
Disulfide bondi899 ↔ 918By similarity
Disulfide bondi912 ↔ 927By similarity
Disulfide bondi957 ↔ 982By similarity
Disulfide bondi964 ↔ 995By similarity
Glycosylationi975 – 9751N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi989 ↔ 1004By similarity
Glycosylationi1064 – 10641N-linked (GlcNAc...)Sequence Analysis
Modified residuei1134 – 11341Phosphoserine1 Publication
Modified residuei1136 – 11361Phosphoserine1 Publication
Disulfide bondi1170 ↔ 1186By similarity
Disulfide bondi1276 ↔ 1338Sequence Analysis
Disulfide bondi1305 ↔ 1317By similarity
Disulfide bondi1328 ↔ 1359By similarity
Disulfide bondi1396 ↔ 1408By similarity
Disulfide bondi1401 ↔ 1421By similarity
Disulfide bondi1415 ↔ 1430By similarity
Glycosylationi1445 – 14451N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1728 ↔ 1745By similarity
Disulfide bondi1734 ↔ 1764By similarity
Disulfide bondi1758 ↔ 1773By similarity
Disulfide bondi1776 ↔ 1789By similarity
Disulfide bondi1783 ↔ 1802By similarity
Disulfide bondi1796 ↔ 1811By similarity
Glycosylationi1878 – 18781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1956 – 19561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2023 – 20231N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2055 ↔ 2071By similarity
Glycosylationi2144 – 21441N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2173 – 21731N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2177 ↔ 2230By similarity
Glycosylationi2197 – 21971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2237 – 22371N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2269 – 22691N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2310 ↔ 2320By similarity
Disulfide bondi2315 ↔ 2333By similarity
Disulfide bondi2327 ↔ 2344By similarity
Disulfide bondi2351 ↔ 2364By similarity
Disulfide bondi2358 ↔ 2377By similarity
Disulfide bondi2371 ↔ 2387By similarity
Glycosylationi2420 – 24201N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2421 ↔ 2435By similarity
Disulfide bondi2428 ↔ 2448By similarity
Disulfide bondi2442 ↔ 2457By similarity
Glycosylationi2556 – 25561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2601 – 26011N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Requires cleavage for activation (presumably).1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

PaxDbiP98159.

Expressioni

Tissue specificityi

Follicle.1 Publication

Gene expression databases

BgeeiP98159.

Interactioni

Protein-protein interaction databases

BioGridi64189. 1 interaction.
STRINGi7227.FBpp0076693.

Structurei

3D structure databases

ProteinModelPortaliP98159.
SMRiP98159. Positions 897-1053, 1100-1379, 1727-1811, 2037-2151, 2311-2461.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati261 – 2699WIID 1
Repeati320 – 3289WIID 2
Repeati399 – 4079WIID 3
Repeati446 – 4549WIID 4
Repeati477 – 4859WIID 5
Repeati528 – 5369WIID 6
Domaini889 – 92941LDL-receptor class A 1PROSITE-ProRule annotationAdd
BLAST
Domaini929 – 95628LDL-receptor class A 2; truncatedPROSITE-ProRule annotationAdd
BLAST
Domaini955 – 100652LDL-receptor class A 3PROSITE-ProRule annotationAdd
BLAST
Domaini1145 – 1383239Peptidase S1 1PROSITE-ProRule annotationAdd
BLAST
Domaini1394 – 143239LDL-receptor class A 4PROSITE-ProRule annotationAdd
BLAST
Domaini1713 – 174331LDL-receptor class A 5; truncatedPROSITE-ProRule annotationAdd
BLAST
Domaini1745 – 177531LDL-receptor class A 6; truncatedPROSITE-ProRule annotationAdd
BLAST
Domaini1774 – 181340LDL-receptor class A 7PROSITE-ProRule annotationAdd
BLAST
Domaini2027 – 2301275Peptidase S1 2PROSITE-ProRule annotationAdd
BLAST
Domaini2308 – 234639LDL-receptor class A 8PROSITE-ProRule annotationAdd
BLAST
Domaini2349 – 238941LDL-receptor class A 9PROSITE-ProRule annotationAdd
BLAST
Domaini2387 – 241933LDL-receptor class A 10; truncatedPROSITE-ProRule annotationAdd
BLAST
Domaini2419 – 245941LDL-receptor class A 11PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1031 – 10333Cell attachment siteSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1489 – 1702214Ser/Thr-richAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 11 LDL-receptor class A domains.PROSITE-ProRule annotation
Contains 2 peptidase S1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000119008.
InParanoidiP98159.
OMAiPNGEDER.
OrthoDBiEOG75B84T.
PhylomeDBiP98159.

Family and domain databases

Gene3Di4.10.400.10. 7 hits.
InterProiIPR023415. 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]
PfamiPF09342. DUF1986. 1 hit.
PF00057. Ldl_recept_a. 4 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00192. LDLa. 9 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF57424. SSF57424. 7 hits.
PROSITEiPS01209. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P98159 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNYNMDEMEA TRLLRHPRRW WSIGFGKRIV AISILVIIVL LFSLVYHGLV
60 70 80 90 100
VEKIDQVQQI AALNARHQVL FNQPFEEDQS ALIVSPQTLH FKLLDEDMNK
110 120 130 140 150
DMEDSKNRRR KHMRQMLVKF RLNKKHRMRR DLHGLDLLDP VRMEANMQHL
160 170 180 190 200
YTKLRSKRAR EALSQLEHEF VRCKKHTPQD CMSAFLRMYK MAKEVTEKME
210 220 230 240 250
KMKAIMREQQ PKLESSSMES HEQKGTFSPA DLIQVTTAEA TTVAVHATEK
260 270 280 290 300
PARTKIKPSR ISWIIDGHDH DESPVYTDGA PKKETTKAPW NTTQLVEITT
310 320 330 340 350
TKIDATATER TTVESTTEKI SWILDHFDKP QEILRTTEGP GQRIIRNVTT
360 370 380 390 400
TSASSEPIVD TENTNSDHVP TTENGLVFNI TTDGPVETTK STAQRKLSFD
410 420 430 440 450
WILDGEENVE PEVKSTNTTT TTAATTTTGA TSETIIVTTE LPKITFDWII
460 470 480 490 500
DGREVVEPQE TTTEVTGTTE RLRKMPFDWI IDGEEVVEPQ ENVTTTTIAT
510 520 530 540 550
TVAVSTTEIN ERIHNSTAYP TKPKPVKFDW IIDGGESSGE VSTSSTSQPK
560 570 580 590 600
LTTREAISNP ESPRSSHPLD NPTSIENMLE SFEQHEEQKP ILRVLNANES
610 620 630 640 650
SSETVTDGYE RQLWLKKFED QARPNQNELI DTFGTALDAK ALDKMGPKIN
660 670 680 690 700
PLNGHTWNAA DAQILSLCER VALRMRNKVA TMSDGETKEK GETFTASPSV
710 720 730 740 750
QFTSRAPGGF PVSGETMKAS AQFMFNPNFG MPSIPVCFYM TPANFRMPMW
760 770 780 790 800
SNTPTFMGMQ GAHFGGSSNP GAGIFFVPQQ FGPSGNFFGG SGGSGAGGQG
810 820 830 840 850
ANIFSKNASP QKPTNGQQQV YCSYMQNQSG QGAGQSQTSS QQQQGGQSAF
860 870 880 890 900
SNANFKMRHA NQTNTANQQG QIIYASYAGL PQQPIQERSR CPEPDQFSCF
910 920 930 940 950
GQQECIPAAR WCDNVVDCSD GSDESACTCA DRVDEERLCD GYEDCPMGED
960 970 980 990 1000
ELGCFGCESL AYSCYENPQD FAKRNRSTIS MCYSRLERCD GFMNCLNGRD
1010 1020 1030 1040 1050
EEQCSMLVTD VADHMSHGAS ASEGYLYHNY RGDWHPVCNN GEKWAALACQ
1060 1070 1080 1090 1100
MDENSRMDHS ASLNVSFQTL TLPGPFIEPS LHAGVHFAQA CHGRNSHDSL
1110 1120 1130 1140 1150
VDHVAYVKCP PMQCGLPSKS SMLEHSKRVR RAVSDSKEIV GDGRIVGGSY
1160 1170 1180 1190 1200
TSALQWPFVV AIYRNGKFHC GGTIYSDRWI ISAAHCVINY GKYFYEVRAG
1210 1220 1230 1240 1250
LLRRSSYSPA TQIQPVSHVV VHQAYERRSM RNDLSLLRLL NPLQFNRWVK
1260 1270 1280 1290 1300
PICLPDKGRT TVGDDWIWGP VEHTLCTVVG WGAIREKGPS SDPMRQVIVP
1310 1320 1330 1340 1350
IRKKCTDPED QASEDICAGD PDGGRDACQG DSGGPLFCRS VSNPDEFYLA
1360 1370 1380 1390 1400
GVVSHGNGCA RPQEFGVYTR VTLYLDWLEM ATTPRLLPKL QPLQLCPGFI
1410 1420 1430 1440 1450
CVWGGKRCIA KRQRCDRNVD CLGGEDEVGC TYNFLPDMVG GVRQNISTTT
1460 1470 1480 1490 1500
ESDYHPVKES EEKSKMREVI PIDDEDLKAE QDEEDLLKST TSLGQTETTQ
1510 1520 1530 1540 1550
GPMDLSFAEQ ITSTTSDDLS ITDETTSTDF TVSDSATSPS TLLPTTTNPS
1560 1570 1580 1590 1600
TWLPSTNIET STFSFTTTES EASTKQETLP TTVAQTTTIP TSTEDLKKLT
1610 1620 1630 1640 1650
DLVTEFIEST TFETTMEVET TTLSLTSTDA PKLVTTEGVK ETTTTEDTTT
1660 1670 1680 1690 1700
ISSIVTLTTT PLATISTTIL TTEKHVAVTT LAPTTTTESA KTTTTHSSST
1710 1720 1730 1740 1750
HSEKDQIQIP NKFVCKKMSQ IVDIMMRCDR KVDCEDGTDE LDCTCKDYLK
1760 1770 1780 1790 1800
GSLKGLICDG KADCEDLTDE QNCVECQSNE FRCPLSKTCL PLSSRCDNKV
1810 1820 1830 1840 1850
DCKFKEDEKD CFALTNGHDV HFDVHQQPKF SSTGIFSRNG HGVWRVVCAH
1860 1870 1880 1890 1900
ETGYHEHQAK TADAVCALLG FNGAHYFNSS EFVTQHEMQP ITPELKGGRN
1910 1920 1930 1940 1950
RMSAQIHSMV GDNVQFTENE VIIPELGHPS ASRPEKDRLL PRKCVGIYVE
1960 1970 1980 1990 2000
CNPYSNKTTP LKTFSAGQVV KEKPIEQVPV LSPTIETHNT PNVHFKPQIP
2010 2020 2030 2040 2050
AMVVNKKDEI LDRLDKLIKS KKNKTILVNE QLHEAIEELH WPWLADVYMN
2060 2070 2080 2090 2100
GDLWCIGVLI DKHWVMVHES CLSGIDLETH YVSVLLGGGK TKRSAHRSNH
2110 2120 2130 2140 2150
EQIRRVDCFE GVPKSNVLLL HLERPVRFTH HVLPTFLPDS SHQNQSHARQ
2160 2170 2180 2190 2200
CISVLHDDAT GRIKTVAITR IHNATNCDSC YKLQEKQPPA NLMRLLNVSA
2210 2220 2230 2240 2250
EDMASISEEV ELINGVAPTE LPAITKFTTC NQFGLKNVSD AHHNPSDQGV
2260 2270 2280 2290 2300
LVCRDSHTGW FPTALFNYNN SDCQSFKQPF GIRTLELVYK SLQDIIDKPS
2310 2320 2330 2340 2350
CKMLLPAPDC STHRCPLGTC LPQAAMCNGR SDCHDGSDEE ETKCRQQKQQ
2360 2370 2380 2390 2400
CAPGEMKCRT SFKCVPKSKF CDHVPDCEDM TDEPTICSCF TYLQATDPSK
2410 2420 2430 2440 2450
ICDGKRNCWD KSDESSVLCN CTADHFQCSS SPEDCIPRDF VCDKEKDCPN
2460 2470 2480 2490 2500
GEDERYCFGI EHPLHLQKKD FWTNSQHTQP EIAPQYGQVI EQTYGIWHTK
2510 2520 2530 2540 2550
CFPKSKPPQV DEVREICKKL GYNPYRQPSY RLIDDEENKP VHTYELADRQ
2560 2570 2580 2590 2600
GRSFSNESLM GKYRDSTKAL IISKFSPLQL NERLTLFLKS SRPIAELVRW
2610
NATDSSMCYR LEIRCA
Length:2,616
Mass (Da):292,492
Last modified:May 10, 2004 - v2
Checksum:i052F92CBAE9EB163
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831I → T in AAA83086. (PubMed:7671306)Curated
Sequence conflicti120 – 1201F → L in AAA83086. (PubMed:7671306)Curated
Sequence conflicti363 – 3631N → T in AAA83086. (PubMed:7671306)Curated
Sequence conflicti831 – 8311Q → R in AAA83086. (PubMed:7671306)Curated
Sequence conflicti864 – 8641N → S in AAA83086. (PubMed:7671306)Curated
Sequence conflicti1150 – 11501Y → H in AAA83086. (PubMed:7671306)Curated
Sequence conflicti1344 – 13441P → A in AAA83086. (PubMed:7671306)Curated
Sequence conflicti1410 – 14101A → S in AAA83086. (PubMed:7671306)Curated
Sequence conflicti1607 – 16071I → M in AAA83086. (PubMed:7671306)Curated
Sequence conflicti1632 – 16321K → I in AAA83086. (PubMed:7671306)Curated
Sequence conflicti1670 – 16701L → P in AAA83086. (PubMed:7671306)Curated
Sequence conflicti1794 – 17941S → K in AAA83086. (PubMed:7671306)Curated
Sequence conflicti1863 – 18631D → N in AAA83086. (PubMed:7671306)Curated
Sequence conflicti1886 – 18883HEM → QEK in AAA83086. (PubMed:7671306)Curated
Sequence conflicti1903 – 19031S → A in AAA83086. (PubMed:7671306)Curated
Sequence conflicti2147 – 21471H → N in AAA83086. (PubMed:7671306)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U29153 mRNA. Translation: AAA83086.1.
AE014296 Genomic DNA. Translation: AAF50656.1.
PIRiA57096.
RefSeqiNP_523947.2. NM_079223.2.
UniGeneiDm.2737.

Genome annotation databases

EnsemblMetazoaiFBtr0076984; FBpp0076693; FBgn0002926.
GeneIDi38738.
KEGGidme:Dmel_CG10129.
UCSCiCG10129-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U29153 mRNA. Translation: AAA83086.1 .
AE014296 Genomic DNA. Translation: AAF50656.1 .
PIRi A57096.
RefSeqi NP_523947.2. NM_079223.2.
UniGenei Dm.2737.

3D structure databases

ProteinModelPortali P98159.
SMRi P98159. Positions 897-1053, 1100-1379, 1727-1811, 2037-2151, 2311-2461.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 64189. 1 interaction.
STRINGi 7227.FBpp0076693.

Protein family/group databases

MEROPSi S01.013.

Proteomic databases

PaxDbi P98159.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0076984 ; FBpp0076693 ; FBgn0002926 .
GeneIDi 38738.
KEGGi dme:Dmel_CG10129.
UCSCi CG10129-RA. d. melanogaster.

Organism-specific databases

CTDi 38738.
FlyBasei FBgn0002926. ndl.

Phylogenomic databases

eggNOGi COG5640.
GeneTreei ENSGT00760000119008.
InParanoidi P98159.
OMAi PNGEDER.
OrthoDBi EOG75B84T.
PhylomeDBi P98159.

Miscellaneous databases

GenomeRNAii 38738.
NextBioi 810123.

Gene expression databases

Bgeei P98159.

Family and domain databases

Gene3Di 4.10.400.10. 7 hits.
InterProi IPR023415. 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 ]
Pfami PF09342. DUF1986. 1 hit.
PF00057. Ldl_recept_a. 4 hits.
PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00261. LDLRECEPTOR.
SMARTi SM00192. LDLa. 9 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 2 hits.
SSF57424. SSF57424. 7 hits.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiNUDEL_DROME
AccessioniPrimary (citable) accession number: P98159
Secondary accession number(s): Q9VRX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 10, 2004
Last modified: October 29, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3