NPF_ANOGA
ID NPF_ANOGA Reviewed; 89 AA.
AC Q7Q7R8; Q5QGM6;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Neuropeptide F;
DE Short=Ang-NPF;
DE Flags: Precursor;
GN Name=npf {ECO:0000312|EMBL:EAA10607.3}; ORFNames=AGAP004642;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAT81601.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=G3; TISSUE=Head {ECO:0000312|EMBL:AAT81601.1};
RX PubMed=15626509; DOI=10.1016/j.peptides.2004.07.014;
RA Garczynski S.F., Crim J.W., Brown M.R.;
RT "Characterization of neuropeptide F and its receptor from the African
RT malaria mosquito, Anopheles gambiae.";
RL Peptides 26:99-107(2005).
RN [2] {ECO:0000312|EMBL:EAA10607.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST {ECO:0000312|EMBL:EAA10607.3};
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 30-61, AND AMIDATION AT PHE-61.
RX PubMed=12364794; DOI=10.1126/science.1076827;
RA Riehle M.A., Garczynski S.F., Crim J.W., Hill C.A., Brown M.R.;
RT "Neuropeptides and peptide hormones in Anopheles gambiae.";
RL Science 298:172-175(2002).
CC -!- FUNCTION: An 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. May have a hormonal role in females (By
CC similarity). {ECO:0000250|UniProtKB:Q8MP00,
CC ECO:0000250|UniProtKB:Q9VET0}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically in
CC larvae, pupae, and the heads of adults. {ECO:0000269|PubMed:15626509}.
CC -!- SIMILARITY: Belongs to the NPY family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT81601.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AY579077; AAT81601.1; ALT_SEQ; mRNA.
DR EMBL; AAAB01008952; EAA10607.3; -; Genomic_DNA.
DR RefSeq; XP_315165.3; XM_315165.4.
DR AlphaFoldDB; Q7Q7R8; -.
DR SMR; Q7Q7R8; -.
DR STRING; 7165.AGAP004642-PA; -.
DR PaxDb; Q7Q7R8; -.
DR GeneID; 1275883; -.
DR KEGG; aga:AgaP_AGAP004642; -.
DR CTD; 1275883; -.
DR VEuPathDB; VectorBase:AGAP004642; -.
DR eggNOG; ENOG502TC38; Eukaryota.
DR HOGENOM; CLU_2456617_0_0_1; -.
DR InParanoid; Q7Q7R8; -.
DR OMA; TKHAQHA; -.
DR OrthoDB; 1620251at2759; -.
DR PhylomeDB; Q7Q7R8; -.
DR Proteomes; UP000007062; Chromosome 2R.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005184; F:neuropeptide hormone activity; ISS:UniProtKB.
DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR GO; GO:0035177; P:larval foraging behavior; ISS:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0032095; P:regulation of response to food; ISS:UniProtKB.
DR GO; GO:0035176; P:social behavior; ISS:UniProtKB.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Digestion;
KW Direct protein sequencing; Hormone; Neuropeptide; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:12364794"
FT CHAIN 30..61
FT /note="Neuropeptide F"
FT /evidence="ECO:0000269|PubMed:12364794"
FT /id="PRO_0000283077"
FT PROPEP 65..89
FT /evidence="ECO:0000269|PubMed:12364794"
FT /id="PRO_0000283078"
FT MOD_RES 61
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:12364794"
SQ SEQUENCE 89 AA; 9838 MW; A893F9996208BEA1 CRC64;
MASGTFTQRL LVALMIFALI ADLSTLVAAR PQDSDAASVA AAIRYLQELE TKHAQHARPR
FGKRGGYLNP AIFGQDEQEV DWQDSTFSR