SNPF_DROME
ID SNPF_DROME Reviewed; 281 AA.
AC Q9VIQ0; Q5Y9D1; Q6YLS6;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 4.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Short neuropeptide F;
DE Contains:
DE RecName: Full=sNPF-associated peptide;
DE Short=sNPF-AP;
DE Contains:
DE RecName: Full=sNPF peptide 2;
DE Short=sNPF-2;
DE Contains:
DE RecName: Full=sNPF peptide 3 {ECO:0000303|PubMed:21214272};
DE Short=sNPF-3 {ECO:0000303|PubMed:21214272};
DE Contains:
DE RecName: Full=sNPF peptide 4 {ECO:0000303|PubMed:21214272};
DE Short=sNPF-4 {ECO:0000303|PubMed:21214272};
DE Contains:
DE RecName: Full=RLRF peptide 1;
DE Contains:
DE RecName: Full=RLRF peptide 2;
DE Flags: Precursor;
GN Name=sNPF; ORFNames=CG13968;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=15385546; DOI=10.1074/jbc.m407842200;
RA Lee K.-S., You K.-H., Choo J.-K., Han Y.-M., Yu K.;
RT "Drosophila short neuropeptide F regulates food intake and body size.";
RL J. Biol. Chem. 279:50781-50789(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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]
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-189.
RA Garczynski S.F., Brown M.R., Crim J.W.;
RT "Identification of two LRLRFa peptides and their receptor from Drosophila
RT melanogaster.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 80-90 AND 93-102.
RC TISSUE=Larva;
RX PubMed=12171930; DOI=10.1074/jbc.m206257200;
RA Baggerman G., Cerstiaens A., De Loof A., Schoofs L.;
RT "Peptidomics of the larval Drosophila melanogaster central nervous
RT system.";
RL J. Biol. Chem. 277:40368-40374(2002).
RN [7]
RP PROTEIN SEQUENCE OF 93-102; 104-111; 167-173 AND 248-254, IDENTIFICATION BY
RP MASS SPECTROMETRY, MASS SPECTROMETRY, AND AMIDATION AT PHE-111; TRP-173 AND
RP TRP-254.
RC TISSUE=Midgut {ECO:0000303|PubMed:21214272};
RX PubMed=21214272; DOI=10.1021/pr101116g;
RA Reiher W., Shirras C., Kahnt J., Baumeister S., Isaac R.E., Wegener C.;
RT "Peptidomics and peptide hormone processing in the Drosophila midgut.";
RL J. Proteome Res. 10:1881-1892(2011).
CC -!- FUNCTION: Plays a role in controlling food intake and regulating body
CC size. {ECO:0000269|PubMed:15385546}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Stage 17 embryos show expression in the two brain
CC hemispheres (neural cells located in the dorsal posterior region), the
CC connected ventral ganglion (pairs of neural cells along the ventral
CC midline) and the peripheral nervous system (expressed in the antennal-
CC maxillary sensory cells). In the brain hemispheres of the feeding third
CC instar larva, expression in neural cells is located in the dorsal-
CC anterior region of the protocerebrum. In the larval ventral ganglion,
CC expression is seen in the neural cells located in the subesophagial
CC region, along the ventral midline and in thoracic and abdominal
CC segments. In the adult brain, expression is seen in the medulla and the
CC mushroom body calyx (at protein level). {ECO:0000269|PubMed:15385546}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development from embryo to
CC adult. {ECO:0000269|PubMed:15385546}.
CC -!- MASS SPECTROMETRY: [sNPF peptide 2]: Mass=1203.62; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21214272};
CC -!- MASS SPECTROMETRY: [RLRF peptide 2]: Mass=974.59; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21214272};
CC -!- MASS SPECTROMETRY: [sNPF peptide 3]: Mass=982.61; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21214272};
CC -!- MASS SPECTROMETRY: [sNPF peptide 4]: Mass=985.59; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21214272};
CC -!- MISCELLANEOUS: Flies overexpressing sNPF are heavier and bigger than
CC wild-type. But loss-of-function flies are not smaller than wild-type.
CC -!- SIMILARITY: Belongs to the NPY family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAR12637.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AY626808; AAU87571.1; -; mRNA.
DR EMBL; AE014134; AAN11060.1; -; Genomic_DNA.
DR EMBL; BT001780; AAN71535.1; -; mRNA.
DR EMBL; AY117427; AAR12637.1; ALT_SEQ; mRNA.
DR RefSeq; NP_724239.1; NM_165316.2.
DR AlphaFoldDB; Q9VIQ0; -.
DR STRING; 7227.FBpp0080859; -.
DR PaxDb; Q9VIQ0; -.
DR DNASU; 35286; -.
DR EnsemblMetazoa; FBtr0081327; FBpp0080859; FBgn0032840.
DR GeneID; 35286; -.
DR KEGG; dme:Dmel_CG13968; -.
DR CTD; 35286; -.
DR FlyBase; FBgn0032840; sNPF.
DR VEuPathDB; VectorBase:FBgn0032840; -.
DR eggNOG; ENOG502SEMZ; Eukaryota.
DR HOGENOM; CLU_953988_0_0_1; -.
DR InParanoid; Q9VIQ0; -.
DR OMA; EARKPMR; -.
DR OrthoDB; 1229133at2759; -.
DR PhylomeDB; Q9VIQ0; -.
DR BioGRID-ORCS; 35286; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35286; -.
DR PRO; PR:Q9VIQ0; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0032840; Expressed in brain and 26 other tissues.
DR ExpressionAtlas; Q9VIQ0; baseline and differential.
DR Genevisible; Q9VIQ0; DM.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR GO; GO:0005184; F:neuropeptide hormone activity; IDA:UniProtKB.
DR GO; GO:0071855; F:neuropeptide receptor binding; IPI:FlyBase.
DR GO; GO:0048018; F:receptor ligand activity; IPI:FlyBase.
DR GO; GO:0008343; P:adult feeding behavior; IMP:FlyBase.
DR GO; GO:0007623; P:circadian rhythm; IEP:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0030536; P:larval feeding behavior; IMP:FlyBase.
DR GO; GO:0035264; P:multicellular organism growth; IMP:FlyBase.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:UniProtKB.
DR GO; GO:0045793; P:positive regulation of cell size; IMP:FlyBase.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:FlyBase.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:FlyBase.
DR GO; GO:0010906; P:regulation of glucose metabolic process; IMP:FlyBase.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:UniProtKB.
DR GO; GO:0032095; P:regulation of response to food; IMP:UniProtKB.
DR GO; GO:0090062; P:regulation of trehalose metabolic process; IMP:FlyBase.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Neuropeptide; Reference proteome; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT PROPEP 31..64
FT /id="PRO_0000022379"
FT PEPTIDE 67..77
FT /note="RLRF peptide 1"
FT /id="PRO_0000284135"
FT PEPTIDE 80..90
FT /note="sNPF-associated peptide"
FT /id="PRO_0000022380"
FT PEPTIDE 93..102
FT /note="sNPF peptide 2"
FT /evidence="ECO:0000269|PubMed:21214272"
FT /id="PRO_0000022381"
FT PEPTIDE 104..111
FT /note="RLRF peptide 2"
FT /evidence="ECO:0000269|PubMed:21214272"
FT /id="PRO_0000284136"
FT PROPEP 115..165
FT /evidence="ECO:0000305"
FT /id="PRO_0000435014"
FT PEPTIDE 167..173
FT /note="sNPF peptide 3"
FT /evidence="ECO:0000269|PubMed:21214272"
FT /id="PRO_0000435015"
FT PROPEP 176..246
FT /evidence="ECO:0000305"
FT /id="PRO_0000435016"
FT PEPTIDE 248..254
FT /note="sNPF peptide 4"
FT /evidence="ECO:0000269|PubMed:21214272"
FT /id="PRO_0000435017"
FT PROPEP 257..281
FT /evidence="ECO:0000305"
FT /id="PRO_0000022382"
FT REGION 137..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250"
FT MOD_RES 111
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:21214272"
FT MOD_RES 173
FT /note="Tryptophan amide"
FT /evidence="ECO:0000269|PubMed:21214272"
FT MOD_RES 254
FT /note="Tryptophan amide"
FT /evidence="ECO:0000269|PubMed:21214272"
FT CONFLICT 8
FT /note="L -> Q (in Ref. 4; AAN71535)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="K -> R (in Ref. 4; AAN71535)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="L -> P (in Ref. 1; AAU87571)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="Missing (in Ref. 1; AAU87571)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="T -> S (in Ref. 1; AAU87571)"
FT /evidence="ECO:0000305"
FT CONFLICT 150..151
FT /note="DS -> NF (in Ref. 1; AAU87571)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="A -> S (in Ref. 1; AAU87571)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="T -> A (in Ref. 1; AAU87571)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="R -> G (in Ref. 4; AAN71535)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 281 AA; 32545 MW; 030B73E32F3875D5 CRC64;
MFHLKRELSQ GCALALICLV SLQMQQPAQA EVSSAQGTPL SNLYDNLLQR EYAGPVVFPN
HQVERKAQRS PSLRLRFGRS DPDMLNSIVE KRWFGDVNQK PIRSPSLRLR FGRRDPSLPQ
MRRTAYDDLL ERELTLNSQQ QQQQLGTEPD SDLGADYDGL YERVVRKPQR LRWGRSVPQF
EANNADNEQI ERSQWYNSLL NSDKMRRMLV ALQQQYEIPE NVASYANDED TDTDLNNDTS
EFQREVRKPM RLRWGRSTGK APSEQKHTPE ETSSIPPKTQ N
