FLP09_CAEEL
ID FLP09_CAEEL Reviewed; 102 AA.
AC Q18502; Q7KPT0;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=FMRFamide-like neuropeptides 9;
DE Contains:
DE RecName: Full=KPSFVRF-amide 1;
DE Contains:
DE RecName: Full=KPSFVRF-amide 2;
DE Flags: Precursor;
GN Name=flp-9 {ECO:0000312|WormBase:C36H8.3}; ORFNames=C36H8.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC08946.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAC08946.1};
RX PubMed=9685599; DOI=10.1016/s0169-328x(98)00106-5;
RA Nelson L.S., Kim K., Memmott J.E., Li C.;
RT "FMRFamide-related gene family in the nematode, Caenorhabditis elegans.";
RL Brain Res. Mol. Brain Res. 58:103-111(1998).
RN [2] {ECO:0000312|EMBL:CAA93480.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 66-72 AND 93-99, FUNCTION, DEVELOPMENTAL STAGE, MASS
RP SPECTROMETRY, AND AMIDATION AT PHE-72 AND PHE-99.
RX PubMed=9920762; DOI=10.1006/bbrc.1998.9920;
RA Marks N.J., Maule A.G., Li C., Nelson L.S., Thompson D.P.,
RA Alexander-Bowman S., Geary T.G., Halton D.W., Verhaert P., Shaw C.;
RT "Isolation, pharmacology and gene organization of KPSFVRFamide: a
RT neuropeptide from Caenorhabditis elegans.";
RL Biochem. Biophys. Res. Commun. 254:222-230(1999).
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 66-72 AND 93-99, AND AMIDATION AT PHE-72 AND PHE-99.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:16061202};
RX PubMed=16061202; DOI=10.1016/j.bbrc.2005.07.044;
RA Husson S.J., Clynen E., Baggerman G., De Loof A., Schoofs L.;
RT "Discovering neuropeptides in Caenorhabditis elegans by two dimensional
RT liquid chromatography and mass spectrometry.";
RL Biochem. Biophys. Res. Commun. 335:76-86(2005).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=16187307; DOI=10.1002/neu.20201;
RA Papaioannou S., Marsden D., Franks C.J., Walker R.J., Holden-Dye L.;
RT "Role of a FMRFamide-like family of neuropeptides in the pharyngeal nervous
RT system of Caenorhabditis elegans.";
RL J. Neurobiol. 65:304-319(2005).
RN [6]
RP FUNCTION (KPSFVRF-AMIDE).
RX PubMed=16377032; DOI=10.1016/j.peptides.2005.11.017;
RA Mertens I., Clinckspoor I., Janssen T., Nachman R., Schoofs L.;
RT "FMRFamide related peptide ligands activate the Caenorhabditis elegans
RT orphan GPCR Y59H11AL.1.";
RL Peptides 27:1291-1296(2006).
CC -!- FUNCTION: FMRFamides and FMRFamide-like peptides are neuropeptides.
CC {ECO:0000305}.
CC -!- FUNCTION: KPSFVRF-amide: Has no effect on somatic body wall muscle,
CC inhibits contraction of vaginal vera muscle, and inhibits the activity
CC of the dissected pharyngeal myogenic muscle system (PubMed:9920762,
CC PubMed:16187307). Acts as a ligand for the npr-22 receptor in vitro
CC (PubMed:16377032). {ECO:0000269|PubMed:16187307,
CC ECO:0000269|PubMed:16377032, ECO:0000269|PubMed:9920762}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Each flp gene is expressed in a distinct set of
CC neurons. {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed in eggs and larvae, but not in adults.
CC {ECO:0000269|PubMed:9920762}.
CC -!- MASS SPECTROMETRY: [KPSFVRF-amide 1]: Mass=879.50; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9920762};
CC -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC08946.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF042395; AAC08946.1; ALT_INIT; mRNA.
DR EMBL; Z69658; CAA93480.2; -; Genomic_DNA.
DR PIR; T19799; T19799.
DR RefSeq; NP_502436.2; NM_070035.6.
DR AlphaFoldDB; Q18502; -.
DR BioGRID; 43324; 2.
DR DIP; DIP-24577N; -.
DR STRING; 6239.C36H8.3; -.
DR EPD; Q18502; -.
DR PaxDb; Q18502; -.
DR PeptideAtlas; Q18502; -.
DR EnsemblMetazoa; C36H8.3.1; C36H8.3.1; WBGene00001452.
DR GeneID; 178232; -.
DR KEGG; cel:CELE_C36H8.3; -.
DR UCSC; C36H8.3.1; c. elegans.
DR CTD; 178232; -.
DR WormBase; C36H8.3; CE39568; WBGene00001452; flp-9.
DR eggNOG; ENOG502TI82; Eukaryota.
DR HOGENOM; CLU_2279980_0_0_1; -.
DR InParanoid; Q18502; -.
DR OMA; PQNREVC; -.
DR OrthoDB; 1579639at2759; -.
DR PRO; PR:Q18502; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001452; Expressed in larva and 3 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0071855; F:neuropeptide receptor binding; IDA:WormBase.
DR GO; GO:0042165; F:neurotransmitter binding; ISS:WormBase.
DR GO; GO:0001508; P:action potential; IDA:WormBase.
DR GO; GO:0007626; P:locomotory behavior; IMP:WormBase.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:WormBase.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Neuropeptide; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..63
FT /evidence="ECO:0000255"
FT /id="PRO_0000312060"
FT PEPTIDE 66..72
FT /note="KPSFVRF-amide 1"
FT /evidence="ECO:0000269|PubMed:16061202,
FT ECO:0000269|PubMed:9920762"
FT /id="PRO_0000312061"
FT PROPEP 75..90
FT /evidence="ECO:0000255"
FT /id="PRO_0000312062"
FT PEPTIDE 93..99
FT /note="KPSFVRF-amide 2"
FT /evidence="ECO:0000269|PubMed:16061202,
FT ECO:0000269|PubMed:9920762"
FT /id="PRO_0000312063"
FT MOD_RES 72
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:16061202,
FT ECO:0000269|PubMed:9920762"
FT MOD_RES 99
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:16061202,
FT ECO:0000269|PubMed:9920762"
SQ SEQUENCE 102 AA; 11829 MW; 4584913CCA9C95D3 CRC64;
MNQFYALFLV ACIAAMANAY EEPDLDALAE FCGKESNRKY CDQIAQLATQ HAIGINQEQV
RMEKRKPSFV RFGKRSGYPL VIDDEEMRMD KRKPSFVRFG RK
