Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9VET0

- NPF_DROME

UniProt

Q9VET0 - NPF_DROME

Protein

Neuropeptide F

Gene

NPF

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

    Integral part of the sensory system that mediates food signaling, providing the neural basis for the regulation of food response; coordinates larval foraging and social behavior changes during development. Required in dopaminergic (DA) neurons that innervate the mushroom body for satiety to suppress appetitive memory performance; a key factor in the internal state of hunger in the brain. NPF neurons coordinately modulate diverse sensory and motor neurons important for feeding, flight, and locomotion. NPF/NPFR pathway exerts its suppressive effect on larval aversion to diverse stressful stimuli (chemical stress and noxious heat) through attenuation of TRP channel-induced neuronal excitation. NPF neural signaling system plays a physiological role in acute modulation of alcohol sensitivity in adults, rather than a general response to intoxication by sedative agents. Activation and inhibition of the NPF system reduces and enhances ethanol preference, respectively. Sexual experience, the NPF system activity and ethanol consumption are all linked; sexual deprivation is a major contributor to enhanced ethanol preference.7 Publications

    GO - Molecular functioni

    1. neuropeptide F receptor binding Source: FlyBase
    2. neuropeptide hormone activity Source: UniProtKB

    GO - Biological processi

    1. circadian behavior Source: FlyBase
    2. circadian rhythm Source: FlyBase
    3. digestion Source: UniProtKB-KW
    4. G-protein coupled receptor signaling pathway Source: FlyBase
    5. larval feeding behavior Source: FlyBase
    6. larval foraging behavior Source: UniProtKB
    7. larval locomotory behavior Source: FlyBase
    8. locomotor rhythm Source: FlyBase
    9. male courtship behavior Source: FlyBase
    10. neuropeptide signaling pathway Source: FlyBase
    11. regulation of response to food Source: UniProtKB
    12. response to stress Source: UniProtKB-KW
    13. social behavior Source: UniProtKB

    Keywords - Molecular functioni

    Hormone, Neuropeptide

    Keywords - Biological processi

    Behavior, Digestion, Stress response

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neuropeptide F
    Short name:
    NPF
    Alternative name(s):
    dNPF
    Gene namesi
    Name:NPF
    ORF Names:CG10342
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0027109. NPF.

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Disruption phenotypei

    Increased NPF or NPFR activity dominantly suppresses PAIN-mediated food aversion in postfeeding larvae. Deficiency in NPF/NPFR signaling causes decreased alcohol sensitivity and overexpression causes a hypersensitive response to alcohol sedation. Controlled functional disruption of NPF or NPFR neurons rapidly triggers acute resistance to ethanol sedation.3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Propeptidei27 – 3261 PublicationPRO_0000283079
    Peptidei35 – 6228Neuropeptide F1 PublicationPRO_0000283080Add
    BLAST
    Propeptidei66 – 102371 PublicationPRO_0000283081Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei62 – 621Phenylalanine amide1 Publication

    Keywords - PTMi

    Amidation, Cleavage on pair of basic residues

    Proteomic databases

    PRIDEiQ9VET0.

    Expressioni

    Tissue specificityi

    Expressed in midgut, brain lobes and ventral nerve cord of larvae. Predominantly expressed in two pairs of protocerebral neurons in the larval CNS (at protein level). Intense expression is also seen in the fan-shaped body of the central complex and two lateral areas of the lower part of the central brain that appear to harbor the giant commissural interneurons of the giant fiber pathway (at protein level). Upon glucose feeding, two additional dNPFergic neurons are consistently detected on the ventromedial surface of the subesophageal ganglion (SEG) of third instars larvae. Expressed in a subset of sugar-responsive PAIN neurons in the thoracic body but is absent from other peripheral PAIN neurons.6 Publications

    Developmental stagei

    Expression is high in larvae seeking food and is down-regulated in late embryos coinciding with the onset of the behavior of older larvae, including food aversion, hypermobility, and cooperative burrowing. In males, expression is increased by mating and reduced by sexual deprivation.1 Publication

    Gene expression databases

    BgeeiQ9VET0.

    Interactioni

    Protein-protein interaction databases

    STRINGi7227.FBpp0082778.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9VET0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the NPY family.Sequence Analysis

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG266214.
    InParanoidiQ9VET0.
    OMAiPPRNNEI.
    OrthoDBiEOG7W41F1.
    PhylomeDBiQ9VET0.

    Sequencei

    Sequence statusi: Complete.

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

    Q9VET0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCQTMRCILV ACVALALLAA GCRVEASNSR PPRKNDVNTM ADAYKFLQDL    50
    DTYYGDRARV RFGKRGSLMD ILRNHEMDNI NLGKNANNGG EFARGFNEEE 100
    IF 102
    Length:102
    Mass (Da):11,465
    Last modified:May 1, 2000 - v1
    Checksum:iD6403F3C5DA7D79F
    GO

    Sequence cautioni

    The sequence AAD42053.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti59 – 591R → A AA sequence (PubMed:10499420)Curated
    Sequence conflicti61 – 611R → V AA sequence (PubMed:10499420)Curated
    Sequence conflicti70 – 701D → E in AAD42053. (PubMed:10499420)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF117896 Genomic DNA. Translation: AAD42053.1. Sequence problems.
    AE014297 Genomic DNA. Translation: AAF55339.1.
    BT023797 mRNA. Translation: AAZ41806.1.
    RefSeqiNP_001262642.1. NM_001275713.1.
    NP_001262643.1. NM_001275714.1.
    NP_536741.1. NM_080493.3.
    UniGeneiDm.5729.

    Genome annotation databases

    EnsemblMetazoaiFBtr0083328; FBpp0082778; FBgn0027109.
    FBtr0331685; FBpp0304074; FBgn0027109.
    FBtr0331686; FBpp0304075; FBgn0027109.
    GeneIDi42018.
    KEGGidme:Dmel_CG10342.

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    On sex, drugs and satisfaction - Issue 138 of May 2012

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF117896 Genomic DNA. Translation: AAD42053.1 . Sequence problems.
    AE014297 Genomic DNA. Translation: AAF55339.1 .
    BT023797 mRNA. Translation: AAZ41806.1 .
    RefSeqi NP_001262642.1. NM_001275713.1.
    NP_001262643.1. NM_001275714.1.
    NP_536741.1. NM_080493.3.
    UniGenei Dm.5729.

    3D structure databases

    ProteinModelPortali Q9VET0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 7227.FBpp0082778.

    Proteomic databases

    PRIDEi Q9VET0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0083328 ; FBpp0082778 ; FBgn0027109 .
    FBtr0331685 ; FBpp0304074 ; FBgn0027109 .
    FBtr0331686 ; FBpp0304075 ; FBgn0027109 .
    GeneIDi 42018.
    KEGGi dme:Dmel_CG10342.

    Organism-specific databases

    CTDi 42018.
    FlyBasei FBgn0027109. NPF.

    Phylogenomic databases

    eggNOGi NOG266214.
    InParanoidi Q9VET0.
    OMAi PPRNNEI.
    OrthoDBi EOG7W41F1.
    PhylomeDBi Q9VET0.

    Miscellaneous databases

    GenomeRNAii 42018.
    NextBioi 826764.

    Gene expression databases

    Bgeei Q9VET0.

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "Identification of a Drosophila brain-gut peptide related to the neuropeptide Y family."
      Brown M.R., Crim J.W., Arata R.C., Cai H.N., Chun C., Shen P.
      Peptides 20:1035-1042(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 35-62, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AMIDATION AT PHE-62.
      Strain: Oregon-R1 Publication.
    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: Berkeley1 Publication.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: BerkeleyImported.
      Tissue: Head.
    5. "Drosophila neuropeptide F mediates integration of chemosensory stimulation and conditioning of the nervous system by food."
      Shen P., Cai H.N.
      J. Neurobiol. 47:16-25(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    6. "Developmental control of foraging and social behavior by the Drosophila neuropeptide Y-like system."
      Wu Q., Wen T., Lee G., Park J.H., Cai H.N., Shen P.
      Neuron 39:147-161(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DEVELOPMENTAL STAGE.
    7. "Drosophila neuropeptide F and its receptor, NPFR1, define a signaling pathway that acutely modulates alcohol sensitivity."
      Wen T., Parrish C.A., Xu D., Wu Q., Shen P.
      Proc. Natl. Acad. Sci. U.S.A. 102:2141-2146(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    8. "A neural circuit mechanism integrating motivational state with memory expression in Drosophila."
      Krashes M.J., DasGupta S., Vreede A., White B., Armstrong J.D., Waddell S.
      Cell 139:416-427(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    9. "A G-protein-coupled neuropeptide Y-like receptor suppresses behavioral and sensory response to multiple stressful stimuli in Drosophila."
      Xu J., Li M., Shen P.
      J. Neurosci. 30:2504-2512(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    10. "Sexual deprivation increases ethanol intake in Drosophila."
      Shohat-Ophir G., Kaun K.R., Azanchi R., Heberlein U.
      Science 335:1351-1355(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiNPF_DROME
    AccessioniPrimary (citable) accession number: Q9VET0
    Secondary accession number(s): Q9Y1K3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2007
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 69 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3