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P98159

- NUDEL_DROME

UniProt

P98159 - NUDEL_DROME

Protein

Serine protease nudel

Gene

ndl

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (10 May 2004)
      Previous versions | rss
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    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

    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-SubCell

    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.
    GeneTreeiENSGT00740000115494.
    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.

    P98159-1 [UniParc]FASTAAdd to Basket

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    MNYNMDEMEA TRLLRHPRRW WSIGFGKRIV AISILVIIVL LFSLVYHGLV     50
    VEKIDQVQQI AALNARHQVL FNQPFEEDQS ALIVSPQTLH FKLLDEDMNK 100
    DMEDSKNRRR KHMRQMLVKF RLNKKHRMRR DLHGLDLLDP VRMEANMQHL 150
    YTKLRSKRAR EALSQLEHEF VRCKKHTPQD CMSAFLRMYK MAKEVTEKME 200
    KMKAIMREQQ PKLESSSMES HEQKGTFSPA DLIQVTTAEA TTVAVHATEK 250
    PARTKIKPSR ISWIIDGHDH DESPVYTDGA PKKETTKAPW NTTQLVEITT 300
    TKIDATATER TTVESTTEKI SWILDHFDKP QEILRTTEGP GQRIIRNVTT 350
    TSASSEPIVD TENTNSDHVP TTENGLVFNI TTDGPVETTK STAQRKLSFD 400
    WILDGEENVE PEVKSTNTTT TTAATTTTGA TSETIIVTTE LPKITFDWII 450
    DGREVVEPQE TTTEVTGTTE RLRKMPFDWI IDGEEVVEPQ ENVTTTTIAT 500
    TVAVSTTEIN ERIHNSTAYP TKPKPVKFDW IIDGGESSGE VSTSSTSQPK 550
    LTTREAISNP ESPRSSHPLD NPTSIENMLE SFEQHEEQKP ILRVLNANES 600
    SSETVTDGYE RQLWLKKFED QARPNQNELI DTFGTALDAK ALDKMGPKIN 650
    PLNGHTWNAA DAQILSLCER VALRMRNKVA TMSDGETKEK GETFTASPSV 700
    QFTSRAPGGF PVSGETMKAS AQFMFNPNFG MPSIPVCFYM TPANFRMPMW 750
    SNTPTFMGMQ GAHFGGSSNP GAGIFFVPQQ FGPSGNFFGG SGGSGAGGQG 800
    ANIFSKNASP QKPTNGQQQV YCSYMQNQSG QGAGQSQTSS QQQQGGQSAF 850
    SNANFKMRHA NQTNTANQQG QIIYASYAGL PQQPIQERSR CPEPDQFSCF 900
    GQQECIPAAR WCDNVVDCSD GSDESACTCA DRVDEERLCD GYEDCPMGED 950
    ELGCFGCESL AYSCYENPQD FAKRNRSTIS MCYSRLERCD GFMNCLNGRD 1000
    EEQCSMLVTD VADHMSHGAS ASEGYLYHNY RGDWHPVCNN GEKWAALACQ 1050
    MDENSRMDHS ASLNVSFQTL TLPGPFIEPS LHAGVHFAQA CHGRNSHDSL 1100
    VDHVAYVKCP PMQCGLPSKS SMLEHSKRVR RAVSDSKEIV GDGRIVGGSY 1150
    TSALQWPFVV AIYRNGKFHC GGTIYSDRWI ISAAHCVINY GKYFYEVRAG 1200
    LLRRSSYSPA TQIQPVSHVV VHQAYERRSM RNDLSLLRLL NPLQFNRWVK 1250
    PICLPDKGRT TVGDDWIWGP VEHTLCTVVG WGAIREKGPS SDPMRQVIVP 1300
    IRKKCTDPED QASEDICAGD PDGGRDACQG DSGGPLFCRS VSNPDEFYLA 1350
    GVVSHGNGCA RPQEFGVYTR VTLYLDWLEM ATTPRLLPKL QPLQLCPGFI 1400
    CVWGGKRCIA KRQRCDRNVD CLGGEDEVGC TYNFLPDMVG GVRQNISTTT 1450
    ESDYHPVKES EEKSKMREVI PIDDEDLKAE QDEEDLLKST TSLGQTETTQ 1500
    GPMDLSFAEQ ITSTTSDDLS ITDETTSTDF TVSDSATSPS TLLPTTTNPS 1550
    TWLPSTNIET STFSFTTTES EASTKQETLP TTVAQTTTIP TSTEDLKKLT 1600
    DLVTEFIEST TFETTMEVET TTLSLTSTDA PKLVTTEGVK ETTTTEDTTT 1650
    ISSIVTLTTT PLATISTTIL TTEKHVAVTT LAPTTTTESA KTTTTHSSST 1700
    HSEKDQIQIP NKFVCKKMSQ IVDIMMRCDR KVDCEDGTDE LDCTCKDYLK 1750
    GSLKGLICDG KADCEDLTDE QNCVECQSNE FRCPLSKTCL PLSSRCDNKV 1800
    DCKFKEDEKD CFALTNGHDV HFDVHQQPKF SSTGIFSRNG HGVWRVVCAH 1850
    ETGYHEHQAK TADAVCALLG FNGAHYFNSS EFVTQHEMQP ITPELKGGRN 1900
    RMSAQIHSMV GDNVQFTENE VIIPELGHPS ASRPEKDRLL PRKCVGIYVE 1950
    CNPYSNKTTP LKTFSAGQVV KEKPIEQVPV LSPTIETHNT PNVHFKPQIP 2000
    AMVVNKKDEI LDRLDKLIKS KKNKTILVNE QLHEAIEELH WPWLADVYMN 2050
    GDLWCIGVLI DKHWVMVHES CLSGIDLETH YVSVLLGGGK TKRSAHRSNH 2100
    EQIRRVDCFE GVPKSNVLLL HLERPVRFTH HVLPTFLPDS SHQNQSHARQ 2150
    CISVLHDDAT GRIKTVAITR IHNATNCDSC YKLQEKQPPA NLMRLLNVSA 2200
    EDMASISEEV ELINGVAPTE LPAITKFTTC NQFGLKNVSD AHHNPSDQGV 2250
    LVCRDSHTGW FPTALFNYNN SDCQSFKQPF GIRTLELVYK SLQDIIDKPS 2300
    CKMLLPAPDC STHRCPLGTC LPQAAMCNGR SDCHDGSDEE ETKCRQQKQQ 2350
    CAPGEMKCRT SFKCVPKSKF CDHVPDCEDM TDEPTICSCF TYLQATDPSK 2400
    ICDGKRNCWD KSDESSVLCN CTADHFQCSS SPEDCIPRDF VCDKEKDCPN 2450
    GEDERYCFGI EHPLHLQKKD FWTNSQHTQP EIAPQYGQVI EQTYGIWHTK 2500
    CFPKSKPPQV DEVREICKKL GYNPYRQPSY RLIDDEENKP VHTYELADRQ 2550
    GRSFSNESLM GKYRDSTKAL IISKFSPLQL NERLTLFLKS SRPIAELVRW 2600
    NATDSSMCYR LEIRCA 2616
    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 ENSGT00740000115494.
    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

    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 1, 2014
    This is version 123 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