NPF_DROME
ID NPF_DROME Reviewed; 102 AA.
AC Q9VET0; Q9Y1K3;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Neuropeptide F;
DE Short=NPF;
DE AltName: Full=dNPF;
DE Flags: Precursor;
GN Name=NPF; ORFNames=CG10342;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAD42053.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 35-62, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND AMIDATION AT PHE-62.
RC STRAIN=Oregon-R {ECO:0000269|PubMed:10499420};
RX PubMed=10499420; DOI=10.1016/s0196-9781(99)00097-2;
RA Brown M.R., Crim J.W., Arata R.C., Cai H.N., Chun C., Shen P.;
RT "Identification of a Drosophila brain-gut peptide related to the
RT neuropeptide Y family.";
RL Peptides 20:1035-1042(1999).
RN [2] {ECO:0000312|EMBL:AAF55339.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAF55339.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000312|EMBL:AAZ41806.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAZ41806.1}; TISSUE=Head;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11257610; DOI=10.1002/neu.1012;
RA Shen P., Cai H.N.;
RT "Drosophila neuropeptide F mediates integration of chemosensory stimulation
RT and conditioning of the nervous system by food.";
RL J. Neurobiol. 47:16-25(2001).
RN [6] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=12848939; DOI=10.1016/s0896-6273(03)00396-9;
RA Wu Q., Wen T., Lee G., Park J.H., Cai H.N., Shen P.;
RT "Developmental control of foraging and social behavior by the Drosophila
RT neuropeptide Y-like system.";
RL Neuron 39:147-161(2003).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15677721; DOI=10.1073/pnas.0406814102;
RA Wen T., Parrish C.A., Xu D., Wu Q., Shen P.;
RT "Drosophila neuropeptide F and its receptor, NPFR1, define a signaling
RT pathway that acutely modulates alcohol sensitivity.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:2141-2146(2005).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19837040; DOI=10.1016/j.cell.2009.08.035;
RA Krashes M.J., DasGupta S., Vreede A., White B., Armstrong J.D., Waddell S.;
RT "A neural circuit mechanism integrating motivational state with memory
RT expression in Drosophila.";
RL Cell 139:416-427(2009).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20164335; DOI=10.1523/jneurosci.3262-09.2010;
RA Xu J., Li M., Shen P.;
RT "A G-protein-coupled neuropeptide Y-like receptor suppresses behavioral and
RT sensory response to multiple stressful stimuli in Drosophila.";
RL J. Neurosci. 30:2504-2512(2010).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22422983; DOI=10.1126/science.1215932;
RA Shohat-Ophir G., Kaun K.R., Azanchi R., Heberlein U.;
RT "Sexual deprivation increases ethanol intake in Drosophila.";
RL Science 335:1351-1355(2012).
CC -!- FUNCTION: Integral part of the sensory system that mediates food
CC signaling, providing the neural basis for the regulation of food
CC response; coordinates larval foraging and social behavior changes
CC during development. Required in dopaminergic (DA) neurons that
CC innervate the mushroom body for satiety to suppress appetitive memory
CC performance; a key factor in the internal state of hunger in the brain.
CC NPF neurons coordinately modulate diverse sensory and motor neurons
CC important for feeding, flight, and locomotion. NPF/NPFR pathway exerts
CC its suppressive effect on larval aversion to diverse stressful stimuli
CC (chemical stress and noxious heat) through attenuation of TRP channel-
CC induced neuronal excitation. NPF neural signaling system plays a
CC physiological role in acute modulation of alcohol sensitivity in
CC adults, rather than a general response to intoxication by sedative
CC agents. Activation and inhibition of the NPF system reduces and
CC enhances ethanol preference, respectively. Sexual experience, the NPF
CC system activity and ethanol consumption are all linked; sexual
CC deprivation is a major contributor to enhanced ethanol preference.
CC {ECO:0000269|PubMed:10499420, ECO:0000269|PubMed:11257610,
CC ECO:0000269|PubMed:12848939, ECO:0000269|PubMed:15677721,
CC ECO:0000269|PubMed:19837040, ECO:0000269|PubMed:20164335,
CC ECO:0000269|PubMed:22422983}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10499420}.
CC -!- TISSUE SPECIFICITY: Expressed in midgut, brain lobes and ventral nerve
CC cord of larvae. Predominantly expressed in two pairs of protocerebral
CC neurons in the larval CNS (at protein level). Intense expression is
CC also seen in the fan-shaped body of the central complex and two lateral
CC areas of the lower part of the central brain that appear to harbor the
CC giant commissural interneurons of the giant fiber pathway (at protein
CC level). Upon glucose feeding, two additional dNPFergic neurons are
CC consistently detected on the ventromedial surface of the subesophageal
CC ganglion (SEG) of third instars larvae. Expressed in a subset of sugar-
CC responsive PAIN neurons in the thoracic body but is absent from other
CC peripheral PAIN neurons. {ECO:0000269|PubMed:10499420,
CC ECO:0000269|PubMed:11257610, ECO:0000269|PubMed:15677721,
CC ECO:0000269|PubMed:19837040, ECO:0000269|PubMed:20164335,
CC ECO:0000269|PubMed:22422983}.
CC -!- DEVELOPMENTAL STAGE: Expression is high in larvae seeking food and is
CC down-regulated in late embryos coinciding with the onset of the
CC behavior of older larvae, including food aversion, hypermobility, and
CC cooperative burrowing. In males, expression is increased by mating and
CC reduced by sexual deprivation. {ECO:0000269|PubMed:12848939}.
CC -!- DISRUPTION PHENOTYPE: Increased NPF or NPFR activity dominantly
CC suppresses PAIN-mediated food aversion in postfeeding larvae.
CC Deficiency in NPF/NPFR signaling causes decreased alcohol sensitivity
CC and overexpression causes a hypersensitive response to alcohol
CC sedation. Controlled functional disruption of NPF or NPFR neurons
CC rapidly triggers acute resistance to ethanol sedation.
CC {ECO:0000269|PubMed:15677721, ECO:0000269|PubMed:20164335,
CC ECO:0000269|PubMed:22422983}.
CC -!- SIMILARITY: Belongs to the NPY family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD42053.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=On sex, drugs and
CC satisfaction - Issue 138 of May 2012;
CC URL="https://web.expasy.org/spotlight/back_issues/138";
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DR EMBL; AF117896; AAD42053.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE014297; AAF55339.1; -; Genomic_DNA.
DR EMBL; BT023797; AAZ41806.1; -; mRNA.
DR RefSeq; NP_001262642.1; NM_001275713.1.
DR RefSeq; NP_001262643.1; NM_001275714.1.
DR RefSeq; NP_536741.1; NM_080493.3.
DR AlphaFoldDB; Q9VET0; -.
DR SMR; Q9VET0; -.
DR BioGRID; 67063; 1.
DR STRING; 7227.FBpp0304074; -.
DR PaxDb; Q9VET0; -.
DR DNASU; 42018; -.
DR EnsemblMetazoa; FBtr0083328; FBpp0082778; FBgn0027109.
DR EnsemblMetazoa; FBtr0331685; FBpp0304074; FBgn0027109.
DR EnsemblMetazoa; FBtr0331686; FBpp0304075; FBgn0027109.
DR GeneID; 42018; -.
DR KEGG; dme:Dmel_CG10342; -.
DR CTD; 42018; -.
DR FlyBase; FBgn0027109; NPF.
DR VEuPathDB; VectorBase:FBgn0027109; -.
DR eggNOG; ENOG502T6VN; Eukaryota.
DR HOGENOM; CLU_2294604_0_0_1; -.
DR InParanoid; Q9VET0; -.
DR OMA; PPRNNEI; -.
DR OrthoDB; 1553020at2759; -.
DR PhylomeDB; Q9VET0; -.
DR BioGRID-ORCS; 42018; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 42018; -.
DR PRO; PR:Q9VET0; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0027109; Expressed in brain and 12 other tissues.
DR ExpressionAtlas; Q9VET0; baseline and differential.
DR Genevisible; Q9VET0; DM.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IPI:FlyBase.
DR GO; GO:0071859; F:neuropeptide F receptor binding; IPI:FlyBase.
DR GO; GO:0005184; F:neuropeptide hormone activity; IMP:UniProtKB.
DR GO; GO:0048512; P:circadian behavior; IDA:FlyBase.
DR GO; GO:0007623; P:circadian rhythm; IEP:FlyBase.
DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR GO; GO:0038002; P:endocrine signaling; IMP:FlyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0030536; P:larval feeding behavior; IMP:FlyBase.
DR GO; GO:0035177; P:larval foraging behavior; IMP:UniProtKB.
DR GO; GO:0008345; P:larval locomotory behavior; TAS:FlyBase.
DR GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
DR GO; GO:0008049; P:male courtship behavior; IMP:FlyBase.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:FlyBase.
DR GO; GO:0042048; P:olfactory behavior; IMP:FlyBase.
DR GO; GO:0032095; P:regulation of response to food; IMP:UniProtKB.
DR GO; GO:1990834; P:response to odorant; IMP:FlyBase.
DR GO; GO:0035176; P:social behavior; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Amidation; Behavior; Cleavage on pair of basic residues; Digestion;
KW Direct protein sequencing; Hormone; Neuropeptide; Reference proteome;
KW Secreted; Signal; Stress response.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..32
FT /evidence="ECO:0000269|PubMed:10499420"
FT /id="PRO_0000283079"
FT PEPTIDE 35..62
FT /note="Neuropeptide F"
FT /evidence="ECO:0000269|PubMed:10499420"
FT /id="PRO_0000283080"
FT PROPEP 66..102
FT /evidence="ECO:0000269|PubMed:10499420"
FT /id="PRO_0000283081"
FT MOD_RES 62
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:10499420"
FT CONFLICT 59
FT /note="R -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="R -> V (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="D -> E (in Ref. 1; AAD42053)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 102 AA; 11465 MW; D6403F3C5DA7D79F CRC64;
MCQTMRCILV ACVALALLAA GCRVEASNSR PPRKNDVNTM ADAYKFLQDL DTYYGDRARV
RFGKRGSLMD ILRNHEMDNI NLGKNANNGG EFARGFNEEE IF
