ID   NPF_LOCMI               Reviewed;          92 AA.
AC   P86442;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Neuropeptide F {ECO:0000303|PubMed:16899111, ECO:0000303|PubMed:19456328, ECO:0000303|PubMed:19524670};
DE            Short=Lom-NPF {ECO:0000303|PubMed:19456328, ECO:0000303|PubMed:19524670};
DE            Short=NPF {ECO:0000303|PubMed:19456328};
DE            Short=longNPF {ECO:0000303|PubMed:16899111};
DE   Flags: Precursor;
OS   Locusta migratoria (Migratory locust).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Orthoptera; Caelifera; Acrididea; Acridomorpha;
OC   Acridoidea; Acrididae; Oedipodinae; Locusta.
OX   NCBI_TaxID=7004;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Head;
RX   PubMed=15591108; DOI=10.1073/pnas.0407753101;
RA   Kang L., Chen X., Zhou Y., Liu B., Zheng W., Li R., Wang J., Yu J.;
RT   "The analysis of large-scale gene expression correlated to the phase
RT   changes of the migratory locust.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:17611-17615(2004).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 52-60, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND
RP   AMIDATION AT PHE-60.
RX   PubMed=19456328; DOI=10.1111/j.1749-6632.2008.03624.x;
RA   Clynen E., Husson S.J., Schoofs L.;
RT   "Identification of new members of the (short) neuropeptide F family in
RT   locusts and Caenorhabditis elegans.";
RL   Ann. N. Y. Acad. Sci. 1163:60-74(2009).
RN   [3] {ECO:0000305}
RP   IDENTIFICATION.
RX   PubMed=16899111; DOI=10.1186/1471-2164-7-201;
RA   Clynen E., Huybrechts J., Verleyen P., De Loof A., Schoofs L.;
RT   "Annotation of novel neuropeptide precursors in the migratory locust based
RT   on transcript screening of a public EST database and mass spectrometry.";
RL   BMC Genomics 7:201-201(2006).
RN   [4] {ECO:0000305}
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX   PubMed=19524670; DOI=10.1016/j.ibmb.2009.06.001;
RA   Clynen E., Schoofs L.;
RT   "Peptidomic survey of the locust neuroendocrine system.";
RL   Insect Biochem. Mol. Biol. 39:491-507(2009).
CC   -!- FUNCTION: Accelerates ovarian maturation in females.
CC       {ECO:0000250|UniProtKB:P86443}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Widely expressed in the nervous system. Expressed
CC       in corpora cardiaca, hypocerebral ganglion, frontal ganglion,
CC       protocerebrum, antennal lobe, tritocerebrum and thoracic ganglia. Not
CC       detected in corpora allata, pars intercerebralis, circumesophageal
CC       connectives, subesophageal ganglion, abdominal ganglion and abdominal
CC       perisympathetic organs. {ECO:0000269|PubMed:19456328,
CC       ECO:0000269|PubMed:19524670}.
CC   -!- MASS SPECTROMETRY: Mass=1121.6; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19456328};
CC   -!- MISCELLANEOUS: The nonapeptide is a truncated form of the predicted
CC       neuropeptide F sequence. The predicted form, which extends from 28-60,
CC       is probably processed to a nonapeptide via cleavage at a K-X(6)-R-Y
CC       motif. Initial cleavage by a prohormone convertase presumably occurs C-
CC       terminally of Arg-50, with the remaining Tyr-51 removed by an
CC       aminopeptidase afterwards. The predicted form might be expressed in
CC       ovary or midgut. {ECO:0000269|PubMed:16899111,
CC       ECO:0000269|PubMed:19456328}.
CC   -!- SIMILARITY: Belongs to the NPY family. {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CO854418; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P86442; -.
DR   SMR; P86442; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR001955; Pancreatic_hormone-like.
DR   InterPro; IPR020392; Pancreatic_hormone-like_CS.
DR   Pfam; PF00159; Hormone_3; 1.
DR   PROSITE; PS00265; PANCREATIC_HORMONE_1; 1.
PE   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Neuropeptide; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   PROPEP          28..51
FT                   /evidence="ECO:0000269|PubMed:19456328"
FT                   /id="PRO_0000392443"
FT   PEPTIDE         52..60
FT                   /note="Neuropeptide F"
FT                   /evidence="ECO:0000269|PubMed:19456328"
FT                   /id="PRO_0000392444"
FT   PROPEP          64..92
FT                   /evidence="ECO:0000269|PubMed:19456328"
FT                   /id="PRO_0000392445"
FT   MOD_RES         60
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:19456328"
SQ   SEQUENCE   92 AA;  10330 MW;  00A0DD14AAB2A6C7 CRC64;
     MSQSRPLALL VVAALVAAAV LVAAAEAQQA DGNKLEGLAD ALKYLQELDR YYSQVARPRF
     GKRAELRPDV VDDVIPEEMS ADKFWRRFAR RR