Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9VET0 (NPF_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neuropeptide F

Short name=NPF
Alternative name(s):
dNPF
Gene names
Name:NPF
ORF Names:CG10342
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length102 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Subcellular location

Secreted Ref.1.

Tissue specificity

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. Ref.1 Ref.5 Ref.7 Ref.8 Ref.9 Ref.10

Developmental stage

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. Ref.6

Disruption phenotype

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. Ref.7 Ref.9 Ref.10

Sequence similarities

Belongs to the NPY family.

Sequence caution

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

Ontologies

Keywords
   Biological processBehavior
Digestion
Stress response
   Cellular componentSecreted
   DomainSignal
   Molecular functionHormone
Neuropeptide
   PTMAmidation
Cleavage on pair of basic residues
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 11897397. Source: FlyBase

circadian behavior

Inferred from direct assay PubMed 21826659. Source: FlyBase

circadian rhythm

Inferred from expression pattern PubMed 19565664. Source: FlyBase

digestion

Inferred from electronic annotation. Source: UniProtKB-KW

larval feeding behavior

Inferred from mutant phenotype Ref.6. Source: FlyBase

larval foraging behavior

Inferred from mutant phenotype Ref.1. Source: UniProtKB

larval locomotory behavior

Traceable author statement PubMed 12848927. Source: FlyBase

locomotor rhythm

Inferred from mutant phenotype PubMed 16894172. Source: FlyBase

male courtship behavior

Inferred from mutant phenotype PubMed 16894172. Source: FlyBase

neuropeptide signaling pathway

Inferred from direct assay PubMed 14555656. Source: FlyBase

regulation of response to food

Inferred from mutant phenotype Ref.1. Source: UniProtKB

response to stress

Inferred from electronic annotation. Source: UniProtKB-KW

social behavior

Inferred from mutant phenotype Ref.1. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionneuropeptide F receptor binding

Inferred from physical interaction PubMed 11897397PubMed 14555656. Source: FlyBase

neuropeptide hormone activity

Inferred from mutant phenotype Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Propeptide27 – 326 Ref.1
PRO_0000283079
Peptide35 – 6228Neuropeptide F Ref.1
PRO_0000283080
Propeptide66 – 10237 Ref.1
PRO_0000283081

Amino acid modifications

Modified residue621Phenylalanine amide Ref.1

Experimental info

Sequence conflict591R → A AA sequence Ref.1
Sequence conflict611R → V AA sequence Ref.1
Sequence conflict701D → E in AAD42053. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9VET0 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: D6403F3C5DA7D79F

FASTA10211,465
        10         20         30         40         50         60 
MCQTMRCILV ACVALALLAA GCRVEASNSR PPRKNDVNTM ADAYKFLQDL DTYYGDRARV 

        70         80         90        100 
RFGKRGSLMD ILRNHEMDNI NLGKNANNGG EFARGFNEEE IF 

« Hide

References

« Hide 'large scale' references
[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-R.
[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. expand/collapse author list , 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]"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. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
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: Berkeley.
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.
+Additional computationally mapped references.

Web resources

Protein Spotlight

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF117896 Genomic DNA. Translation: AAD42053.1. Sequence problems.
AE014297 Genomic DNA. Translation: AAF55339.1.
BT023797 mRNA. Translation: AAZ41806.1.
RefSeqNP_001262642.1. NM_001275713.1.
NP_001262643.1. NM_001275714.1.
NP_536741.1. NM_080493.3.
UniGeneDm.5729.

3D structure databases

ProteinModelPortalQ9VET0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7227.FBpp0082778.

Proteomic databases

PRIDEQ9VET0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0083328; FBpp0082778; FBgn0027109.
FBtr0331685; FBpp0304074; FBgn0027109.
FBtr0331686; FBpp0304075; FBgn0027109.
GeneID42018.
KEGGdme:Dmel_CG10342.

Organism-specific databases

CTD42018.
FlyBaseFBgn0027109. NPF.

Phylogenomic databases

eggNOGNOG266214.
InParanoidQ9VET0.
OMAPPRNNEI.
OrthoDBEOG7W41F1.
PhylomeDBQ9VET0.

Gene expression databases

BgeeQ9VET0.

Family and domain databases

ProtoNetSearch...

Other

GenomeRNAi42018.
NextBio826764.

Entry information

Entry nameNPF_DROME
AccessionPrimary (citable) accession number: Q9VET0
Secondary accession number(s): Q9Y1K3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase