FLP03_CAEEL
ID FLP03_CAEEL Reviewed; 184 AA.
AC Q23212;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=FMRFamide-like neuropeptides 3;
DE Contains:
DE RecName: Full=SPLGTMRF-amide;
DE Contains:
DE RecName: Full=TPLGTMRF-amide;
DE Contains:
DE RecName: Full=SAEPFGTMRF-amide;
DE Contains:
DE RecName: Full=NPENDTPFGTMRF-amide;
DE Contains:
DE RecName: Full=ASEDALFGTMRF-amide;
DE Contains:
DE RecName: Full=EAEEPLGTMRF-amide;
DE Contains:
DE RecName: Full=SADDSAPFGTMRF-amide;
DE Contains:
DE RecName: Full=NPLGTMRF-amide;
DE Flags: Precursor;
GN Name=flp-3 {ECO:0000312|EMBL:CAA90030.1, ECO:0000312|WormBase:W07E11.2};
GN ORFNames=W07E11.2;
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:AAC08940.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAC08940.1};
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:CAA90030.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA90030.1};
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 75-82; 86-95; 99-111; 115-126; 145-155 AND 159-171, AND
RP AMIDATION AT PHE-82; PHE-95; PHE-111; PHE-126; PHE-155 AND PHE-171.
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 [4] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15236235; DOI=10.1002/cne.20189;
RA Kim K., Li C.;
RT "Expression and regulation of an FMRFamide-related neuropeptide gene family
RT in Caenorhabditis elegans.";
RL J. Comp. Neurol. 475:540-550(2004).
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).
CC -!- FUNCTION: FMRFamides and FMRFamide-like peptides are neuropeptides.
CC SAEPFGTMRF-amide inhibits the activity of dissected pharyngeal myogenic
CC muscle system. {ECO:0000269|PubMed:16187307}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Each flp gene is expressed in a distinct set of
CC neurons. Flp-3 is expressed in the IL1 and PQR neurons.
CC {ECO:0000269|PubMed:15236235}.
CC -!- DEVELOPMENTAL STAGE: Expressed from the comma stage of embryogenesis,
CC during all larval stages, and in adults. {ECO:0000269|PubMed:15236235,
CC ECO:0000269|PubMed:9685599}.
CC -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.
CC {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; AF042389; AAC08940.1; -; mRNA.
DR EMBL; Z49868; CAA90030.1; -; Genomic_DNA.
DR PIR; T26262; T26262.
DR RefSeq; NP_509694.1; NM_077293.6.
DR AlphaFoldDB; Q23212; -.
DR BioGRID; 46135; 3.
DR STRING; 6239.W07E11.2; -.
DR EPD; Q23212; -.
DR PaxDb; Q23212; -.
DR EnsemblMetazoa; W07E11.2.1; W07E11.2.1; WBGene00001446.
DR GeneID; 181221; -.
DR KEGG; cel:CELE_W07E11.2; -.
DR UCSC; W07E11.2; c. elegans.
DR CTD; 181221; -.
DR WormBase; W07E11.2; CE02373; WBGene00001446; flp-3.
DR eggNOG; ENOG502T0VU; Eukaryota.
DR GeneTree; ENSGT00970000196033; -.
DR HOGENOM; CLU_1311141_0_0_1; -.
DR InParanoid; Q23212; -.
DR OMA; APFGTMR; -.
DR OrthoDB; 1409884at2759; -.
DR PhylomeDB; Q23212; -.
DR PRO; PR:Q23212; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001446; Expressed in larva and 3 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0045759; P:negative regulation of action potential; IDA:WormBase.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:WormBase.
DR GO; GO:0043051; P:regulation of pharyngeal pumping; IDA:WormBase.
DR InterPro; IPR002544; FMRFamid-related_peptide-like.
DR Pfam; PF01581; FARP; 9.
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..23
FT /evidence="ECO:0000255"
FT PROPEP 24..25
FT /evidence="ECO:0000255"
FT /id="PRO_0000312032"
FT PEPTIDE 28..35
FT /note="SPLGTMRF-amide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000312033"
FT PROPEP 39..73
FT /evidence="ECO:0000255"
FT /id="PRO_0000312034"
FT PEPTIDE 75..82
FT /note="TPLGTMRF-amide"
FT /evidence="ECO:0000269|PubMed:16061202"
FT /id="PRO_0000312035"
FT PEPTIDE 86..95
FT /note="SAEPFGTMRF-amide"
FT /evidence="ECO:0000269|PubMed:16061202"
FT /id="PRO_0000312036"
FT PEPTIDE 99..111
FT /note="NPENDTPFGTMRF-amide"
FT /evidence="ECO:0000269|PubMed:16061202"
FT /id="PRO_0000312037"
FT PEPTIDE 115..126
FT /note="ASEDALFGTMRF-amide"
FT /evidence="ECO:0000269|PubMed:16061202"
FT /id="PRO_0000312038"
FT PROPEP 130..142
FT /evidence="ECO:0000255"
FT /id="PRO_0000312039"
FT PEPTIDE 145..155
FT /note="EAEEPLGTMRF-amide"
FT /evidence="ECO:0000269|PubMed:16061202"
FT /id="PRO_0000312040"
FT PEPTIDE 159..171
FT /note="SADDSAPFGTMRF-amide"
FT /evidence="ECO:0000269|PubMed:16061202"
FT /id="PRO_0000312041"
FT PEPTIDE 175..182
FT /note="NPLGTMRF-amide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000312042"
FT REGION 90..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 35
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000255"
FT MOD_RES 82
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:16061202"
FT MOD_RES 95
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:16061202"
FT MOD_RES 111
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:16061202"
FT MOD_RES 126
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:16061202"
FT MOD_RES 155
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:16061202"
FT MOD_RES 171
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:16061202"
FT MOD_RES 182
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000255"
SQ SEQUENCE 184 AA; 20707 MW; 9B5B4BE6B2B72EB5 CRC64;
MISPNHLILL FCVNCAFLVA SDATPKRSPL GTMRFGKRAI ADEMTFEEDG YYPSNVMWKR
STVDSSEPVI RDQRTPLGTM RFGKRSAEPF GTMRFGKRNP ENDTPFGTMR FGKRASEDAL
FGTMRFGKRE DGNAPFGTMK FGKREAEEPL GTMRFGKRSA DDSAPFGTMR FGKRNPLGTM
RFGK