P48607 · SPZ_DROME
- ProteinProtein spaetzle
- Genespz
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids326 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
The activated form, spaetzle C-106, acts as a ligand for the Toll receptor (PubMed:12872120).
Binding to Toll activates the Toll signaling pathway and induces expression of the antifungal peptide drosomycin (PubMed:8808632).
Component of the extracellular signaling pathway that establishes dorsal-ventral polarity in the embryo (PubMed:11212919, PubMed:8124709).
Binding to Toll activates the Toll signaling pathway and induces expression of the antifungal peptide drosomycin (PubMed:8808632).
Component of the extracellular signaling pathway that establishes dorsal-ventral polarity in the embryo (PubMed:11212919, PubMed:8124709).
Miscellaneous
'Spaetzle' means 'noodles' in German.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 220-221 | Cleavage; by easter | ||||
Sequence: RV |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein spaetzle
- Cleaved into 1 chains
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionP48607
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Isoform 8.19
Note: Secreted in a cell culture system.
Isoform 8.29
Note: Secreted in a cell culture system.
Isoform 11.15
Note: Secreted in a cell culture system.
Isoform 11.6
Note: Secreted in a cell culture system.
Isoform 11.7
Note: Secreted in a cell culture system.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 220-221 | Not cleaved when expressed with activated SPE. | ||||
Sequence: RV → LN | ||||||
Mutagenesis | 234-235 | Abolishes signaling almost completely. | ||||
Sequence: RK → AA | ||||||
Mutagenesis | 275 | Strongly reduced signaling. | ||||
Sequence: D → R | ||||||
Mutagenesis | 318 | Reduced phenotypic rescue of a mutant. | ||||
Sequence: C → S or T |
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-25 | |||||
Sequence: MMTPMWISLFKVLLLLFAFFATYEA | ||||||
Chain | PRO_0000022406 | 26-326 | Protein spaetzle | |||
Sequence: KEYERIIKELFTITNDEGVVLFNTSADSAPFMPIPTQHDDPTQKQKQNQNQSPIPETNRHYHQYHSLIQPDQYFKVQRSPNGKLNLVFNDTFVSLQRTDTEVQSEQPIPPRHPSDTFVFPDSPIAKYRPPQSPARPLRNDTKEHNPCAKDESQHLRNFCTNVDDYPDLSGLTHKLKNNFAKFFSNDLQPTDVSSRVGGSDERFLCRSIRKLVYPKKGLRADDTWQLIVNNDEYKQAIQIEECEGADQPCDFAANFPQSYNPICKQHYTQQTLASIKSDGELDVVQNSFKIPSCCKCALKTG | ||||||
Glycosylation | 48 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 114 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 164 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Chain | PRO_0000022407 | 221-326 | Protein spaetzle C-106 | |||
Sequence: VGGSDERFLCRSIRKLVYPKKGLRADDTWQLIVNNDEYKQAIQIEECEGADQPCDFAANFPQSYNPICKQHYTQQTLASIKSDGELDVVQNSFKIPSCCKCALKTG | ||||||
Disulfide bond | 230↔288 | |||||
Sequence: CRSIRKLVYPKKGLRADDTWQLIVNNDEYKQAIQIEECEGADQPCDFAANFPQSYNPIC | ||||||
Disulfide bond | 267↔319 | |||||
Sequence: CEGADQPCDFAANFPQSYNPICKQHYTQQTLASIKSDGELDVVQNSFKIPSCC | ||||||
Disulfide bond | 274↔321 | |||||
Sequence: CDFAANFPQSYNPICKQHYTQQTLASIKSDGELDVVQNSFKIPSCCKC | ||||||
Disulfide bond | 318 | Interchain | ||||
Sequence: C |
Post-translational modification
During embryonic development, easter cleaves the signal peptide and also generates the C-terminal 12 kDa active fragment, C-106 (except for isoform 8.24 and isoform 11.27 as they do not contain the cleavage site) (PubMed:9533958).
During the immune response, cleaved in the same manner by SPE (PubMed:16399077).
During the immune response, cleaved in the same manner by SPE (PubMed:16399077).
Extracellular forms of isoform 8.19 and isoform 11.7 are glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Developmental stage
Expressed both maternally and zygotically. All isoforms, except isoform 8.20, are rapidly degraded on cellularisation of the blastoderm embryo.
Gene expression databases
Interaction
Subunit
Homodimer; disulfide-linked (PubMed:12872120, PubMed:9533958).
In the presence of Tl, crystal structures show one Tl molecule bound to a spaetzle C-106 homodimer (PubMed:24282309, PubMed:24733933).
However, the active complex probably consists of two Tl molecules bound to a spaetzle C-106 homodimer (PubMed:24282309, PubMed:24733933).
This is supported by in vitro experiments which also show binding of the spaetzle C-106 dimer to 2 Tl receptors (PubMed:12872120).
Ligand binding induces conformational changes in the extracellular domain of Tl (PubMed:24282309).
This may enable a secondary homodimerization interface at the C-terminus of the Tl extracellular domain (PubMed:24282309).
In the presence of Tl, crystal structures show one Tl molecule bound to a spaetzle C-106 homodimer (PubMed:24282309, PubMed:24733933).
However, the active complex probably consists of two Tl molecules bound to a spaetzle C-106 homodimer (PubMed:24282309, PubMed:24733933).
This is supported by in vitro experiments which also show binding of the spaetzle C-106 dimer to 2 Tl receptors (PubMed:12872120).
Ligand binding induces conformational changes in the extracellular domain of Tl (PubMed:24282309).
This may enable a secondary homodimerization interface at the C-terminus of the Tl extracellular domain (PubMed:24282309).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 56-82 | Disordered | ||||
Sequence: FMPIPTQHDDPTQKQKQNQNQSPIPET | ||||||
Compositional bias | 63-82 | Polar residues | ||||
Sequence: HDDPTQKQKQNQNQSPIPET | ||||||
Region | 152-174 | Disordered | ||||
Sequence: YRPPQSPARPLRNDTKEHNPCAK | ||||||
Domain | 228-322 | Spaetzle | ||||
Sequence: FLCRSIRKLVYPKKGLRADDTWQLIVNNDEYKQAIQIEECEGADQPCDFAANFPQSYNPICKQHYTQQTLASIKSDGELDVVQNSFKIPSCCKCA |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 10 isoforms produced by Alternative splicing.
P48607-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name8.19
- SynonymsA
- Length326
- Mass (Da)37,447
- Last updated2002-08-02 v3
- Checksum3252389129CFB1E0
P48607-2
- Name8.20
- SynonymsI
- Differences from canonical
- 23-121: Missing
P48607-4
- Name8.24
P48607-5
- Name8.29
- SynonymsD
P48607-10
- Name11.15
P48607-6
- Name11.27
P48607-7
- Name11.32
P48607-8
- Name11.5
- Differences from canonical
- 23-185: Missing
P48607-3
- Name11.6
- SynonymsB, 8.23
- Differences from canonical
- 23-48: Missing
P48607-9
- Name11.7
- SynonymsC, 23 kDa
- Differences from canonical
- 49-121: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_004418 | 23-48 | in isoform 8.24, isoform 11.32 and isoform 11.6 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_004419 | 23-67 | in isoform 8.29 | |||
Sequence: YEAKEYERIIKELFTITNDEGVVLFNTSADSAPFMPIPTQHDDPT → IVYINIELTKRHEAEVRAEKTVADYKALLATINNGGPGKSASNHL | ||||||
Alternative sequence | VSP_004420 | 23-121 | in isoform 8.20 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_004421 | 23-185 | in isoform 11.5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_004422 | 49-121 | in isoform 11.15, isoform 11.27 and isoform 11.7 | |||
Sequence: Missing | ||||||
Sequence conflict | 50 | in Ref. 2; AAF98130 | ||||
Sequence: S → T | ||||||
Sequence conflict | 53 | in Ref. 2; AAF98124 | ||||
Sequence: S → T | ||||||
Compositional bias | 63-82 | Polar residues | ||||
Sequence: HDDPTQKQKQNQNQSPIPET | ||||||
Alternative sequence | VSP_004423 | 65-189 | in isoform 11.32 | |||
Sequence: Missing | ||||||
Sequence conflict | 67 | in Ref. 5; AAL25517 | ||||
Sequence: T → P | ||||||
Alternative sequence | VSP_004424 | 68-120 | in isoform 8.29 | |||
Sequence: Missing | ||||||
Sequence conflict | 75 | in Ref. 2; AAF98130/AAF98131/AAF98126 | ||||
Sequence: N → D | ||||||
Alternative sequence | VSP_004425 | 101-121 | in isoform 8.24 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_010257 | 142-151 | in isoform 11.15 | |||
Sequence: Missing | ||||||
Sequence conflict | 147 | in Ref. 2; AAF98132 | ||||
Sequence: S → F | ||||||
Sequence conflict | 163 | in Ref. 2; AAF98129 | ||||
Sequence: R → T | ||||||
Sequence conflict | 172 | in Ref. 2; AAF98129 | ||||
Sequence: C → S | ||||||
Alternative sequence | VSP_004426 | 189-225 | in isoform 11.27 | |||
Sequence: Missing | ||||||
Sequence conflict | 197 | in Ref. 2; AAF98125 | ||||
Sequence: T → R | ||||||
Alternative sequence | VSP_004427 | 197-226 | in isoform 8.24 | |||
Sequence: THKLKNNFAKFFSNDLQPTDVSSRVGGSDE → RRAIPLQEHQEAGVPKKGLEGGRHLAVNCQ | ||||||
Sequence conflict | 206 | in Ref. 2; AAF98129 | ||||
Sequence: K → N | ||||||
Alternative sequence | VSP_004428 | 227-326 | in isoform 8.24 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U05850 EMBL· GenBank· DDBJ | AAA17887.1 EMBL· GenBank· DDBJ | Unassigned DNA | ||
AF237964 EMBL· GenBank· DDBJ | AAF98123.1 EMBL· GenBank· DDBJ | mRNA | ||
AF237965 EMBL· GenBank· DDBJ | AAF98124.1 EMBL· GenBank· DDBJ | mRNA | ||
AF237966 EMBL· GenBank· DDBJ | AAF98125.1 EMBL· GenBank· DDBJ | mRNA | ||
AF237967 EMBL· GenBank· DDBJ | AAF98126.1 EMBL· GenBank· DDBJ | mRNA | ||
AF237968 EMBL· GenBank· DDBJ | AAF98127.1 EMBL· GenBank· DDBJ | mRNA | ||
AF237969 EMBL· GenBank· DDBJ | AAF98128.1 EMBL· GenBank· DDBJ | mRNA | ||
AF237970 EMBL· GenBank· DDBJ | AAF98129.1 EMBL· GenBank· DDBJ | mRNA | ||
AF237971 EMBL· GenBank· DDBJ | AAF98130.1 EMBL· GenBank· DDBJ | mRNA | ||
AF237972 EMBL· GenBank· DDBJ | AAF98131.1 EMBL· GenBank· DDBJ | mRNA | ||
AF237973 EMBL· GenBank· DDBJ | AAF98132.1 EMBL· GenBank· DDBJ | mRNA | ||
AF237974 EMBL· GenBank· DDBJ | AAF82745.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAF56658.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAN14388.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAN14391.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAN14394.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAN14395.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY060478 EMBL· GenBank· DDBJ | AAL25517.1 EMBL· GenBank· DDBJ | mRNA |