FLP01_CAEEL
ID FLP01_CAEEL Reviewed; 175 AA.
AC P41855; Q7JKL0; Q8I122;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=FMRFamide-like neuropeptides 1;
DE Contains:
DE RecName: Full=PNFMRY-amide;
DE Contains:
DE RecName: Full=AGSDPNFLRF-amide;
DE Contains:
DE RecName: Full=SQPNFLRF-amide;
DE Contains:
DE RecName: Full=ASGDPNFLRF-amide;
DE Contains:
DE RecName: Full=SDPNFLRF-amide;
DE AltName: Full=PF1;
DE Contains:
DE RecName: Full=AAADPNFLRF-amide;
DE Contains:
DE RecName: Full=SADPNFLRF-amide;
DE AltName: Full=PF2;
DE Contains:
DE RecName: Full=PNFLRF-amide;
DE Flags: Precursor;
GN Name=flp-1; ORFNames=F23B2.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS A AND
RP B).
RC STRAIN=Bristol N2;
RX PubMed=1607945; DOI=10.1523/jneurosci.12-06-02356.1992;
RA Rosoff M.L., Buerglin T.R., Li C.;
RT "Alternatively spliced transcripts of the flp-1 gene encode distinct
RT FMRFamide-like peptides in Caenorhabditis elegans.";
RL J. Neurosci. 12:2356-2361(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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]
RP PROTEIN SEQUENCE OF 71-76; 89-98; 101-108; 111-120; 123-130; 133-142;
RP 146-154 AND 168-173, MASS SPECTROMETRY, AND AMIDATION AT TYR-76; PHE-98;
RP PHE-108; PHE-120; PHE-130; PHE-142; PHE-154 AND PHE-173.
RX PubMed=8483810; DOI=10.1016/0196-9781(93)90049-m;
RA Rosoff M.L., Doble K.E., Price D.A., Li C.;
RT "The flp-1 propeptide is processed into multiple, highly similar FMRFamide-
RT like peptides in Caenorhabditis elegans.";
RL Peptides 14:331-338(1993).
RN [4]
RP PROTEIN SEQUENCE OF 133-142 AND 146-154, AND AMIDATION AT PHE-142 AND
RP PHE-154.
RC STRAIN=Bristol N2;
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]
RP PROTEIN SEQUENCE OF 168-173, AMIDATION AT PHE-173, AND MASS SPECTROMETRY.
RX PubMed=28847365; DOI=10.7554/elife.28877;
RA Ohno H., Yoshida M., Sato T., Kato J., Miyazato M., Kojima M., Ida T.,
RA Iino Y.;
RT "Luqin-like RYamide peptides regulate food-evoked responses in C.
RT elegans.";
RL Elife 6:0-0(2017).
RN [6]
RP TISSUE SPECIFICITY.
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 [7]
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 [8]
RP FUNCTION (PNFMRY-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).
RN [9]
RP FUNCTION, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=23658528; DOI=10.1371/journal.pgen.1003472;
RA Stawicki T.M., Takayanagi-Kiya S., Zhou K., Jin Y.;
RT "Neuropeptides function in a homeostatic manner to modulate excitation-
RT inhibition imbalance in C. elegans.";
RL PLoS Genet. 9:E1003472-E1003472(2013).
CC -!- FUNCTION: Together with flp-18, plays a homeostatic role by acting on
CC the GABAergic neural transmission at neuromuscular junctions to prevent
CC overexcitation of the locomotor circuit. {ECO:0000269|PubMed:23658528}.
CC -!- FUNCTION: [SADPNFLRF-amide]: Inhibits the activity of dissected
CC pharyngeal myogenic muscle system. {ECO:0000269|PubMed:16187307}.
CC -!- FUNCTION: DPNFLRF-amide: Inhibits the activity of dissected pharyngeal
CC myogenic muscle system. {ECO:0000269|PubMed:16187307}.
CC -!- FUNCTION: [PNFMRY-amide]: Acts as a ligand for the npr-22 receptor in
CC vitro. {ECO:0000269|PubMed:16377032}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a;
CC IsoId=P41855-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P41855-2; Sequence=VSP_001563;
CC Name=c;
CC IsoId=P41855-3; Sequence=VSP_020150;
CC -!- TISSUE SPECIFICITY: Each flp gene is expressed in a distinct set of
CC neurons. Flp-1 is expressed in the AVA interneurons, the M5 cholinergic
CC pharyngeal motoneurons, and the AIA, AIY, AVE, AVK, RIG and RMG
CC neurons. {ECO:0000269|PubMed:15236235}.
CC -!- PTM: May be processed by convertase egl-3.
CC {ECO:0000305|PubMed:23658528}.
CC -!- MASS SPECTROMETRY: [SADPNFLRF-amide]: Mass=1065.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8483810};
CC -!- MASS SPECTROMETRY: [SQPNFLRF-amide]: Mass=1007.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8483810};
CC -!- MASS SPECTROMETRY: [ASGDPNFLRF-amide]: Mass=1123.0;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:8483810};
CC -!- MASS SPECTROMETRY: [SDPNFLRF-amide]: Mass=994.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8483810};
CC -!- MASS SPECTROMETRY: [AAADPNFLRF-amide]: Mass=1122.0;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:8483810};
CC -!- MASS SPECTROMETRY: [PNFLRF-amide]: Mass=791.8; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8483810};
CC -!- MASS SPECTROMETRY: [PNFLRF-amide]: Mass=792.29; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:28847365};
CC -!- MISCELLANEOUS: [Isoform b]: Expressed at about a twofold higher level
CC than isoform Long. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.
CC {ECO:0000305}.
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DR EMBL; S38096; AAB22368.1; -; Genomic_DNA.
DR EMBL; U00670; AAC46464.1; -; Genomic_DNA.
DR EMBL; Z82266; CAB05179.1; -; Genomic_DNA.
DR EMBL; Z82266; CAD56243.1; -; Genomic_DNA.
DR EMBL; Z82266; CAD56244.1; -; Genomic_DNA.
DR PIR; B44827; B44827.
DR PIR; T21297; T21297.
DR RefSeq; NP_501592.1; NM_069191.6. [P41855-1]
DR RefSeq; NP_872077.1; NM_182277.5. [P41855-2]
DR RefSeq; NP_872078.1; NM_182278.4. [P41855-3]
DR AlphaFoldDB; P41855; -.
DR BioGRID; 42843; 4.
DR STRING; 6239.F23B2.5a; -.
DR PaxDb; P41855; -.
DR EnsemblMetazoa; F23B2.5a.1; F23B2.5a.1; WBGene00001444. [P41855-1]
DR EnsemblMetazoa; F23B2.5b.1; F23B2.5b.1; WBGene00001444. [P41855-2]
DR EnsemblMetazoa; F23B2.5c.1; F23B2.5c.1; WBGene00001444. [P41855-3]
DR GeneID; 177737; -.
DR KEGG; cel:CELE_F23B2.5; -.
DR UCSC; F23B2.5a; c. elegans. [P41855-1]
DR CTD; 177737; -.
DR WormBase; F23B2.5a; CE09585; WBGene00001444; flp-1. [P41855-1]
DR WormBase; F23B2.5b; CE32045; WBGene00001444; flp-1. [P41855-2]
DR WormBase; F23B2.5c; CE32046; WBGene00001444; flp-1. [P41855-3]
DR eggNOG; ENOG502SDD0; Eukaryota.
DR GeneTree; ENSGT00970000196033; -.
DR InParanoid; P41855; -.
DR OMA; FGRNQPN; -.
DR OrthoDB; 1313570at2759; -.
DR PhylomeDB; P41855; -.
DR PRO; PR:P41855; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001444; 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:0006972; P:hyperosmotic response; IMP:WormBase.
DR GO; GO:0007626; P:locomotory behavior; IMP:WormBase.
DR GO; GO:0007638; P:mechanosensory behavior; IMP:WormBase.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:WormBase.
DR GO; GO:0006937; P:regulation of muscle contraction; IGI:UniProtKB.
DR GO; GO:0046662; P:regulation of oviposition; IMP:WormBase.
DR InterPro; IPR002544; FMRFamid-related_peptide-like.
DR Pfam; PF01581; FARP; 8.
PE 1: Evidence at protein level;
KW Alternative splicing; Amidation; Cleavage on pair of basic residues;
KW Direct protein sequencing; Neuropeptide; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..68
FT /id="PRO_0000009545"
FT PEPTIDE 71..76
FT /note="PNFMRY-amide"
FT /id="PRO_0000009546"
FT PROPEP 79..86
FT /id="PRO_0000009547"
FT PEPTIDE 89..98
FT /note="AGSDPNFLRF-amide"
FT /id="PRO_0000009548"
FT PEPTIDE 101..108
FT /note="SQPNFLRF-amide"
FT /id="PRO_0000009549"
FT PEPTIDE 111..120
FT /note="ASGDPNFLRF-amide"
FT /id="PRO_0000009550"
FT PEPTIDE 123..130
FT /note="SDPNFLRF-amide"
FT /id="PRO_0000009551"
FT PEPTIDE 133..142
FT /note="AAADPNFLRF-amide"
FT /id="PRO_0000009552"
FT PEPTIDE 146..154
FT /note="SADPNFLRF-amide"
FT /id="PRO_0000009553"
FT PROPEP 157..165
FT /id="PRO_0000009554"
FT PEPTIDE 168..173
FT /note="PNFLRF-amide"
FT /evidence="ECO:0000269|PubMed:28847365"
FT /id="PRO_0000009555"
FT MOD_RES 76
FT /note="Tyrosine amide"
FT /evidence="ECO:0000269|PubMed:8483810"
FT MOD_RES 98
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:8483810"
FT MOD_RES 108
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:8483810"
FT MOD_RES 120
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:8483810"
FT MOD_RES 130
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:8483810"
FT MOD_RES 142
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:16061202,
FT ECO:0000269|PubMed:8483810"
FT MOD_RES 154
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:16061202,
FT ECO:0000269|PubMed:8483810"
FT MOD_RES 173
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:28847365,
FT ECO:0000269|PubMed:8483810"
FT VAR_SEQ 81..113
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_020150"
FT VAR_SEQ 81..91
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_001563"
SQ SEQUENCE 175 AA; 19706 MW; 8E88DF266BE59E7F CRC64;
MTLLYQVGLL LLVAATYKVS AECCTPGATS DFCTVFSMLS TMEQNEVMNF IGENCDGDAE
VALQKMEKRK PNFMRYGRSA AVKSLGKKAG SDPNFLRFGR SQPNFLRFGK ASGDPNFLRF
GRSDPNFLRF GKAAADPNFL RFGKRSADPN FLRFGRSFDN FDRESRKPNF LRFGK
