Q9VIQ0 · SNPF_DROME
- ProteinShort neuropeptide F
- GenesNPF
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids281 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays a role in controlling food intake and regulating body size.
Miscellaneous
Flies overexpressing sNPF are heavier and bigger than wild-type. But loss-of-function flies are not smaller than wild-type.
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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Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Cellular Component | neuronal cell body | |
Molecular Function | neuropeptide hormone activity | |
Molecular Function | neuropeptide receptor binding | |
Molecular Function | receptor ligand activity | |
Biological Process | adult feeding behavior | |
Biological Process | circadian rhythm | |
Biological Process | determination of adult lifespan | |
Biological Process | larval feeding behavior | |
Biological Process | multicellular organism growth | |
Biological Process | neuropeptide signaling pathway | |
Biological Process | positive regulation of cell size | |
Biological Process | positive regulation of ERK1 and ERK2 cascade | |
Biological Process | positive regulation of multicellular organism growth | |
Biological Process | regulation of glucose metabolic process | |
Biological Process | regulation of multicellular organism growth | |
Biological Process | regulation of response to food |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameShort neuropeptide F
- Cleaved into 6 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 accessionQ9VIQ0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, propeptide, peptide, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-30 | |||||
Sequence: MFHLKRELSQGCALALICLVSLQMQQPAQA | ||||||
Propeptide | PRO_0000022379 | 31-64 | ||||
Sequence: EVSSAQGTPLSNLYDNLLQREYAGPVVFPNHQVE | ||||||
Peptide | PRO_0000284135 | 67-77 | RLRF peptide 1 | |||
Sequence: AQRSPSLRLRF | ||||||
Modified residue | 77 | Phenylalanine amide | ||||
Sequence: F | ||||||
Peptide | PRO_0000022380 | 80-90 | sNPF-associated peptide | |||
Sequence: SDPDMLNSIVE | ||||||
Peptide | PRO_0000022381 | 93-102 | sNPF peptide 2 | |||
Sequence: WFGDVNQKPI | ||||||
Peptide | PRO_0000284136 | 104-111 | RLRF peptide 2 | |||
Sequence: SPSLRLRF | ||||||
Modified residue | 111 | Phenylalanine amide | ||||
Sequence: F | ||||||
Propeptide | PRO_0000435014 | 115-165 | ||||
Sequence: DPSLPQMRRTAYDDLLERELTLNSQQQQQQLGTEPDSDLGADYDGLYERVV | ||||||
Peptide | PRO_0000435015 | 167-173 | sNPF peptide 3 | |||
Sequence: KPQRLRW | ||||||
Modified residue | 173 | Tryptophan amide | ||||
Sequence: W | ||||||
Propeptide | PRO_0000435016 | 176-246 | ||||
Sequence: SVPQFEANNADNEQIERSQWYNSLLNSDKMRRMLVALQQQYEIPENVASYANDEDTDTDLNNDTSEFQREV | ||||||
Peptide | PRO_0000435017 | 248-254 | sNPF peptide 4 | |||
Sequence: KPMRLRW | ||||||
Modified residue | 254 | Tryptophan amide | ||||
Sequence: W | ||||||
Propeptide | PRO_0000022382 | 257-281 | ||||
Sequence: STGKAPSEQKHTPEETSSIPPKTQN |
Keywords
- PTM
Proteomic databases
Expression
Tissue specificity
Stage 17 embryos show expression in the two brain hemispheres (neural cells located in the dorsal posterior region), the connected ventral ganglion (pairs of neural cells along the ventral midline) and the peripheral nervous system (expressed in the antennal-maxillary sensory cells). In the brain hemispheres of the feeding third instar larva, expression in neural cells is located in the dorsal-anterior region of the protocerebrum. In the larval ventral ganglion, expression is seen in the neural cells located in the subesophagial region, along the ventral midline and in thoracic and abdominal segments. In the adult brain, expression is seen in the medulla and the mushroom body calyx (at protein level).
Developmental stage
Expressed throughout development from embryo to adult.
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 137-156 | Disordered | ||||
Sequence: NSQQQQQQLGTEPDSDLGAD | ||||||
Region | 226-281 | Disordered | ||||
Sequence: ANDEDTDTDLNNDTSEFQREVRKPMRLRWGRSTGKAPSEQKHTPEETSSIPPKTQN | ||||||
Compositional bias | 237-252 | Basic and acidic residues | ||||
Sequence: NDTSEFQREVRKPMRL |
Sequence similarities
Belongs to the NPY family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length281
- Mass (Da)32,545
- Last updated2014-05-14 v4
- Checksum030B73E32F3875D5
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 8 | in Ref. 4; AAN71535 | ||||
Sequence: L → Q | ||||||
Sequence conflict | 100 | in Ref. 4; AAN71535 | ||||
Sequence: K → R | ||||||
Sequence conflict | 130 | in Ref. 1; AAU87571 | ||||
Sequence: L → P | ||||||
Sequence conflict | 144 | in Ref. 1; AAU87571 | ||||
Sequence: Missing | ||||||
Sequence conflict | 147 | in Ref. 1; AAU87571 | ||||
Sequence: T → S | ||||||
Sequence conflict | 150-151 | in Ref. 1; AAU87571 | ||||
Sequence: DS → NF | ||||||
Sequence conflict | 182 | in Ref. 1; AAU87571 | ||||
Sequence: A → S | ||||||
Sequence conflict | 233 | in Ref. 1; AAU87571 | ||||
Sequence: T → A | ||||||
Compositional bias | 237-252 | Basic and acidic residues | ||||
Sequence: NDTSEFQREVRKPMRL | ||||||
Sequence conflict | 247 | in Ref. 4; AAN71535 | ||||
Sequence: R → G |
Mass Spectrometry
sNPF peptide 2
Molecular mass is 1,203.62 Da. Determined by MALDI.RLRF peptide 2
Molecular mass is 974.59 Da. Determined by MALDI.sNPF peptide 3
Molecular mass is 982.61 Da. Determined by MALDI.sNPF peptide 4
Molecular mass is 985.59 Da. Determined by MALDI.Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY626808 EMBL· GenBank· DDBJ | AAU87571.1 EMBL· GenBank· DDBJ | mRNA | ||
AE014134 EMBL· GenBank· DDBJ | AAN11060.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT001780 EMBL· GenBank· DDBJ | AAN71535.1 EMBL· GenBank· DDBJ | mRNA | ||
AY117427 EMBL· GenBank· DDBJ | AAR12637.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. |