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Neuropeptide F receptor (DmNPFR1)

 NPFR_DROME              Reviewed;         485 AA.
Q9VNM1; D2CFP0; D2CFP1; D2CFP2; D2CFP3; D2CFP4; Q7KFF8; Q8SZ35;
Q967T7;
16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 3.
28-MAR-2018, entry version 124.
RecName: Full=Neuropeptide F receptor {ECO:0000303|PubMed:11897397, ECO:0000312|EMBL:AAF51909.3};
Short=DmNPFR1 {ECO:0000303|PubMed:11897397};
Name=NPFR {ECO:0000312|FlyBase:FBgn0037408}; Synonyms=NPFR1;
ORFNames=CG1147;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000305, ECO:0000312|EMBL:AAK50050.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), FUNCTION, TISSUE SPECIFICITY,
AND DISRUPTION PHENOTYPE.
TISSUE=Larva {ECO:0000269|PubMed:11897397};
PubMed=11897397; DOI=10.1016/S0196-9781(01)00647-7;
Garczynski S.F., Brown M.R., Shen P., Murray T.F., Crim J.W.;
"Characterization of a functional neuropeptide F receptor from
Drosophila melanogaster.";
Peptides 23:773-780(2002).
[2] {ECO:0000305, ECO:0000312|EMBL:ABH01175.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; A; B; C AND D).
Joergensen L.M., Grimmelikhuijzen C.J.P.;
"Molecular cloning of splice variant 1 of DmNPFR1.";
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000312|EMBL:AAF51909.3}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4] {ECO:0000305, ECO:0000312|EMBL:AAF51909.3}
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
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., 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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5] {ECO:0000305, ECO:0000312|EMBL:ABH01175.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=Berkeley {ECO:0000312|EMBL:AAL48774.1}; TISSUE=Embryo;
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.,
Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
George R., Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G.,
Miranda A., Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S.,
Patel S., Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M.,
Celniker S.;
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000305, ECO:0000312|EMBL:ABH01175.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=Berkeley {ECO:0000312|EMBL:AAL48774.1};
Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
[7] {ECO:0000305}
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=15677721; DOI=10.1073/pnas.0406814102;
Wen T., Parrish C.A., Xu D., Wu Q., Shen P.;
"Drosophila neuropeptide F and its receptor, NPFR1, define a signaling
pathway that acutely modulates alcohol sensitivity.";
Proc. Natl. Acad. Sci. U.S.A. 102:2141-2146(2005).
[8] {ECO:0000305}
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=19837040; DOI=10.1016/j.cell.2009.08.035;
Krashes M.J., DasGupta S., Vreede A., White B., Armstrong J.D.,
Waddell S.;
"A neural circuit mechanism integrating motivational state with memory
expression in Drosophila.";
Cell 139:416-427(2009).
[9] {ECO:0000305}
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=20164335; DOI=10.1523/JNEUROSCI.3262-09.2010;
Xu J., Li M., Shen P.;
"A G-protein-coupled neuropeptide Y-like receptor suppresses
behavioral and sensory response to multiple stressful stimuli in
Drosophila.";
J. Neurosci. 30:2504-2512(2010).
[10] {ECO:0000305}
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=22422983; DOI=10.1126/science.1215932;
Shohat-Ophir G., Kaun K.R., Azanchi R., Heberlein U.;
"Sexual deprivation increases ethanol intake in Drosophila.";
Science 335:1351-1355(2012).
-!- FUNCTION: Receptor for NPF. 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. {ECO:0000269|PubMed:11897397,
ECO:0000269|PubMed:15677721, ECO:0000269|PubMed:19837040,
ECO:0000269|PubMed:20164335, ECO:0000269|PubMed:22422983}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
protein {ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=A {ECO:0000269|PubMed:10731132}; Synonyms=variant 1
{ECO:0000269|Ref.2};
IsoId=Q9VNM1-1; Sequence=Displayed;
Name=2 {ECO:0000269|Ref.2};
IsoId=Q9VNM1-2; Sequence=VSP_043735, VSP_043736;
Name=B {ECO:0000269|PubMed:10731132}; Synonyms=variant 3
{ECO:0000269|Ref.2};
IsoId=Q9VNM1-3; Sequence=VSP_043736, VSP_043737;
Name=D {ECO:0000269|PubMed:10731132}; Synonyms=variant 4
{ECO:0000269|Ref.2};
IsoId=Q9VNM1-4; Sequence=VSP_043737;
Name=C {ECO:0000269|PubMed:10731132}; Synonyms=variant 5
{ECO:0000269|Ref.2};
IsoId=Q9VNM1-5; Sequence=VSP_043736;
Name=6 {ECO:0000269|PubMed:10731132, ECO:0000269|PubMed:11897397};
IsoId=Q9VNM1-6; Sequence=VSP_043735;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in midgut, brain lobes and ventral
nerve cord of larvae. In adults, expressed in a pair of
dorsolateral neurons in the protocerebrum, and the central complex
and a small number of neurons in the subesophageal ganglion (at
protein level). Expressed in a subset of sugar-responsive PAIN
neurons in the thoracic body but is absent from other peripheral
PAIN neurons. {ECO:0000269|PubMed:11897397,
ECO:0000269|PubMed:15677721, ECO:0000269|PubMed:19837040,
ECO:0000269|PubMed:20164335, ECO:0000269|PubMed:22422983}.
-!- 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.
{ECO:0000269|PubMed:11897397, ECO:0000269|PubMed:15677721,
ECO:0000269|PubMed:20164335, ECO:0000269|PubMed:22422983}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-----------------------------------------------------------------------
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EMBL; AF364400; AAK50050.1; -; mRNA.
EMBL; DQ666847; ABH01175.1; -; mRNA.
EMBL; DQ666848; ABH01176.1; -; mRNA.
EMBL; DQ666849; ABH01177.1; -; mRNA.
EMBL; DQ666850; ABH01178.1; -; mRNA.
EMBL; DQ666851; ABH01179.1; -; mRNA.
EMBL; AE014297; AAF51909.3; -; Genomic_DNA.
EMBL; AY071152; AAL48774.1; -; mRNA.
EMBL; BT044552; ACI12877.1; -; mRNA.
RefSeq; NP_001246946.1; NM_001260017.2. [Q9VNM1-5]
RefSeq; NP_524245.3; NM_079521.4. [Q9VNM1-1]
UniGene; Dm.2483; -.
ProteinModelPortal; Q9VNM1; -.
IntAct; Q9VNM1; 1.
STRING; 7227.FBpp0300637; -.
PaxDb; Q9VNM1; -.
PRIDE; Q9VNM1; -.
EnsemblMetazoa; FBtr0078590; FBpp0078239; FBgn0037408. [Q9VNM1-1]
EnsemblMetazoa; FBtr0308316; FBpp0300635; FBgn0037408. [Q9VNM1-3]
EnsemblMetazoa; FBtr0308317; FBpp0300636; FBgn0037408. [Q9VNM1-5]
EnsemblMetazoa; FBtr0308318; FBpp0300637; FBgn0037408. [Q9VNM1-4]
GeneID; 40754; -.
KEGG; dme:Dmel_CG1147; -.
UCSC; CG1147-RA; d. melanogaster. [Q9VNM1-1]
CTD; 40754; -.
FlyBase; FBgn0037408; NPFR.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00900000140797; -.
HOGENOM; HOG000115783; -.
InParanoid; Q9VNM1; -.
KO; K04209; -.
OMA; VRKPIMR; -.
OrthoDB; EOG091G0COX; -.
PhylomeDB; Q9VNM1; -.
GenomeRNAi; 40754; -.
PRO; PR:Q9VNM1; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0037408; -.
ExpressionAtlas; Q9VNM1; differential.
Genevisible; Q9VNM1; DM.
GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
GO; GO:0042263; F:neuropeptide F receptor activity; IPI:FlyBase.
GO; GO:0008188; F:neuropeptide receptor activity; ISM:FlyBase.
GO; GO:0004983; F:neuropeptide Y receptor activity; IEA:InterPro.
GO; GO:0004995; F:tachykinin receptor activity; ISS:FlyBase.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:FlyBase.
GO; GO:0030536; P:larval feeding behavior; IMP:FlyBase.
GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IDA:FlyBase.
GO; GO:0007218; P:neuropeptide signaling pathway; IDA:FlyBase.
GO; GO:0007217; P:tachykinin receptor signaling pathway; ISS:FlyBase.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
InterPro; IPR000611; NPY_rcpt.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00237; GPCRRHODOPSN.
PRINTS; PR01012; NRPEPTIDEYR.
SMART; SM01381; 7TM_GPCR_Srsx; 1.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
Alternative splicing; Behavior; Complete proteome; Disulfide bond;
G-protein coupled receptor; Membrane; Neuropeptide; Receptor;
Reference proteome; Stress response; Transducer; Transmembrane;
Transmembrane helix.
CHAIN 1 485 Neuropeptide F receptor.
/FTId=PRO_0000417447.
TOPO_DOM 1 91 Extracellular. {ECO:0000255}.
TRANSMEM 92 112 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 113 122 Cytoplasmic. {ECO:0000255}.
TRANSMEM 123 143 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 144 163 Extracellular. {ECO:0000255}.
TRANSMEM 164 184 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 185 202 Cytoplasmic. {ECO:0000255}.
TRANSMEM 203 223 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 224 262 Extracellular. {ECO:0000255}.
TRANSMEM 263 283 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 284 317 Cytoplasmic. {ECO:0000255}.
TRANSMEM 318 338 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 339 355 Extracellular. {ECO:0000255}.
TRANSMEM 356 376 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 377 485 Cytoplasmic. {ECO:0000255}.
COMPBIAS 412 415 Poly-Arg. {ECO:0000255}.
DISULFID 161 248 {ECO:0000255|PROSITE-ProRule:PRU00521}.
VAR_SEQ 1 4 Missing (in isoform 2 and isoform 6).
{ECO:0000303|PubMed:11897397,
ECO:0000303|Ref.2}.
/FTId=VSP_043735.
VAR_SEQ 382 404 Missing (in isoform 2, isoform B and
isoform C). {ECO:0000303|PubMed:10731132,
ECO:0000303|Ref.2}.
/FTId=VSP_043736.
VAR_SEQ 485 485 R -> RLEQY (in isoform B and isoform D).
{ECO:0000303|PubMed:10731132,
ECO:0000303|Ref.2}.
/FTId=VSP_043737.
CONFLICT 65 65 R -> M (in Ref. 5; AAL48774).
{ECO:0000305}.
CONFLICT 162 162 K -> E (in Ref. 2; ABH01175).
{ECO:0000305}.
CONFLICT 166 166 M -> V (in Ref. 2; ABH01178).
{ECO:0000305}.
CONFLICT 304 304 R -> W (in Ref. 2; ABH01178).
{ECO:0000305}.
CONFLICT 340 340 A -> T (in Ref. 2; ABH01177).
{ECO:0000305}.
CONFLICT 347 347 V -> A (in Ref. 2; ABH01175).
{ECO:0000305}.
CONFLICT 413 413 R -> K (in Ref. 2; ABH01177).
{ECO:0000305}.
SEQUENCE 485 AA; 53537 MW; 8E92C4A83BE08DC8 CRC64;
MIISMNQTEP AQLADGEHLS GYASSSNSVR YLDDRHPLDY LDLGTVHALN TTAINTSDLN
ETGSRPLDPV LIDRFLSNRA VDSPWYHMLI SMYGVLIVFG ALGNTLVVIA VIRKPIMRTA
RNLFILNLAI SDLLLCLVTM PLTLMEILSK YWPYGSCSIL CKTIAMLQAL CIFVSTISIT
AIAFDRYQVI VYPTRDSLQF VGAVTILAGI WALALLLASP LFVYKELINT DTPALLQQIG
LQDTIPYCIE DWPSRNGRFY YSIFSLCVQY LVPILIVSVA YFGIYNKLKS RITVVAVQAS
SAQRKVERGR RMKRTNCLLI SIAIIFGVSW LPLNFFNLYA DMERSPVTQS MLVRYAICHM
IGMSSACSNP LLYGWLNDNF RKEFQELLCR CSDTNVALNG HTTGCNVQAA ARRRRKLGAE
LSKGELKLLG PGGAQSGTAG GEGGLAATDF MTGHHEGGLR SAITESVALT DHNPVPSEVT
KLMPR


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