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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
 
 
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