P98159 (NUDEL_DROME) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 113.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Serine protease nudel EC=3.4.21.- | ||||
| Gene names |
| ||||
| Organism | Drosophila melanogaster (Fruit fly) [Reference proteome] | ||||
| Taxonomic identifier | 7227 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Ecdysozoa › 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
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
| ||||||||||||||||||
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. 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. 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, 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. |
| PIR | A57096. |
| RefSeq | NP_523947.2. NM_079223.2. |
| UniGene | Dm.2737. |
3D structure databases | |
| ProteinModelPortal | P98159. |
| SMR | P98159. Positions 891-1053, 1100-1379, 1727-1811, 2265-2461. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 7227.FBpp0076693. |
Protein family/group databases | |
| MEROPS | S01.013. |
Proteomic databases | |
| PaxDb | P98159. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblMetazoa | FBtr0076984; FBpp0076693; FBgn0002926. |
| GeneID | 38738. |
| KEGG | dme:Dmel_CG10129. |
| UCSC | CG10129-RA. d. melanogaster. |
Organism-specific databases | |
| CTD | 38738. |
| FlyBase | FBgn0002926. ndl. |
Phylogenomic databases | |
| eggNOG | COG5640. |
| GeneTree | ENSGT00700000104440. |
| InParanoid | P98159. |
| OMA | PNGEDER. |
| OrthoDB | EOG47SQVP. |
| PhylomeDB | P98159. |
Gene expression databases | |
| Bgee | P98159. |
| GermOnline | CG10129. Drosophila melanogaster. |
Family and domain databases | |
| Gene3D | 4.10.400.10. 7 hits. |
| InterPro | 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] |
| Pfam | PF09342. DUF1986. 1 hit. PF00057. Ldl_recept_a. 4 hits. PF00089. Trypsin. 1 hit. [Graphical view] |
| SMART | SM00192. LDLa. 9 hits. SM00020. Tryp_SPc. 1 hit. [Graphical view] |
| SUPFAM | SSF57424. LDL_rcpt_classA_cys-rich. 7 hits. SSF50494. Pept_Ser_Cys. 2 hits. |
| 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 | |
| GenomeRNAi | 38738. |
| NextBio | 810123. |
Entry information
| Entry name | NUDEL_DROME | ||||||||
| Accession | Primary (citable) accession number: P98159 Secondary accession number(s): Q9VRX5 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Drosophila annotation project | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| Drosophila Drosophila: entries, gene names and cross-references to FlyBase |
| SIMILARITY comments Index of protein domains and families |

Clusters with
