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FMRFamide-like neuropeptides 1 [Cleaved into: PNFMRY-amide; AGSDPNFLRF-amide; SQPNFLRF-amide; ASGDPNFLRF-amide; SDPNFLRF-amide (PF1); AAADPNFLRF-amide; SADPNFLRF-amide (PF2); PNFLRF-amide]

 FLP01_CAEEL             Reviewed;         175 AA.
P41855; Q7JKL0; Q8I122;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
12-SEP-2018, entry version 116.
RecName: Full=FMRFamide-like neuropeptides 1;
Contains:
RecName: Full=PNFMRY-amide;
Contains:
RecName: Full=AGSDPNFLRF-amide;
Contains:
RecName: Full=SQPNFLRF-amide;
Contains:
RecName: Full=ASGDPNFLRF-amide;
Contains:
RecName: Full=SDPNFLRF-amide;
AltName: Full=PF1;
Contains:
RecName: Full=AAADPNFLRF-amide;
Contains:
RecName: Full=SADPNFLRF-amide;
AltName: Full=PF2;
Contains:
RecName: Full=PNFLRF-amide;
Flags: Precursor;
Name=flp-1; ORFNames=F23B2.5;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS
A AND B).
STRAIN=Bristol N2;
PubMed=1607945;
Rosoff M.L., Buerglin T.R., Li C.;
"Alternatively spliced transcripts of the flp-1 gene encode distinct
FMRFamide-like peptides in Caenorhabditis elegans.";
J. Neurosci. 12:2356-2361(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3]
PROTEIN SEQUENCE OF 71-76; 89-98; 101-108; 111-120; 123-130; 133-142;
146-154 AND 168-173, MASS SPECTROMETRY, AND AMIDATION AT TYR-76;
PHE-98; PHE-108; PHE-120; PHE-130; PHE-142; PHE-154 AND PHE-173.
PubMed=8483810; DOI=10.1016/0196-9781(93)90049-M;
Rosoff M.L., Doble K.E., Price D.A., Li C.;
"The flp-1 propeptide is processed into multiple, highly similar
FMRFamide-like peptides in Caenorhabditis elegans.";
Peptides 14:331-338(1993).
[4]
PROTEIN SEQUENCE OF 133-142 AND 146-154, AND AMIDATION AT PHE-142 AND
PHE-154.
STRAIN=Bristol N2;
PubMed=16061202; DOI=10.1016/j.bbrc.2005.07.044;
Husson S.J., Clynen E., Baggerman G., De Loof A., Schoofs L.;
"Discovering neuropeptides in Caenorhabditis elegans by two
dimensional liquid chromatography and mass spectrometry.";
Biochem. Biophys. Res. Commun. 335:76-86(2005).
[5]
PROTEIN SEQUENCE OF 168-173, AMIDATION AT PHE-173, AND MASS
SPECTROMETRY.
PubMed=28847365; DOI=10.7554/eLife.28877;
Ohno H., Yoshida M., Sato T., Kato J., Miyazato M., Kojima M., Ida T.,
Iino Y.;
"Luqin-like RYamide peptides regulate food-evoked responses in C.
elegans.";
Elife 6:0-0(2017).
[6]
TISSUE SPECIFICITY.
PubMed=15236235; DOI=10.1002/cne.20189;
Kim K., Li C.;
"Expression and regulation of an FMRFamide-related neuropeptide gene
family in Caenorhabditis elegans.";
J. Comp. Neurol. 475:540-550(2004).
[7]
FUNCTION.
PubMed=16187307; DOI=10.1002/neu.20201;
Papaioannou S., Marsden D., Franks C.J., Walker R.J., Holden-Dye L.;
"Role of a FMRFamide-like family of neuropeptides in the pharyngeal
nervous system of Caenorhabditis elegans.";
J. Neurobiol. 65:304-319(2005).
[8]
FUNCTION (PNFMRY-AMIDE).
PubMed=16377032; DOI=10.1016/j.peptides.2005.11.017;
Mertens I., Clinckspoor I., Janssen T., Nachman R., Schoofs L.;
"FMRFamide related peptide ligands activate the Caenorhabditis elegans
orphan GPCR Y59H11AL.1.";
Peptides 27:1291-1296(2006).
[9]
FUNCTION, AND PROTEOLYTIC CLEAVAGE.
PubMed=23658528; DOI=10.1371/journal.pgen.1003472;
Stawicki T.M., Takayanagi-Kiya S., Zhou K., Jin Y.;
"Neuropeptides function in a homeostatic manner to modulate
excitation-inhibition imbalance in C. elegans.";
PLoS Genet. 9:E1003472-E1003472(2013).
-!- FUNCTION: Together with flp-18, plays a homeostatic role by acting
on the GABAergic neural transmission at neuromuscular junctions to
prevent overexcitation of the locomotor circuit.
{ECO:0000269|PubMed:23658528}.
-!- FUNCTION: SADPNFLRF-amide: Inhibits the activity of dissected
pharyngeal myogenic muscle system. {ECO:0000269|PubMed:16187307}.
-!- FUNCTION: DPNFLRF-amide: Inhibits the activity of dissected
pharyngeal myogenic muscle system. {ECO:0000269|PubMed:16187307}.
-!- FUNCTION: PNFMRY-amide: Acts as a ligand for the npr-22 receptor
in vitro. {ECO:0000269|PubMed:16377032}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=a;
IsoId=P41855-1; Sequence=Displayed;
Name=b;
IsoId=P41855-2; Sequence=VSP_001563;
Note=Expressed at about a twofold higher level than isoform
Long.;
Name=c;
IsoId=P41855-3; Sequence=VSP_020150;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Each flp gene is expressed in a distinct set
of neurons. Flp-1 is expressed in the AVA interneurons, the M5
cholinergic pharyngeal motoneurons, and the AIA, AIY, AVE, AVK,
RIG and RMG neurons. {ECO:0000269|PubMed:15236235}.
-!- PTM: May be processed by convertase egl-3.
{ECO:0000305|PubMed:23658528}.
-!- MASS SPECTROMETRY: Mass=1065.0; Method=Electrospray; Range=146-
154; Evidence={ECO:0000269|PubMed:8483810};
-!- MASS SPECTROMETRY: Mass=1007.0; Method=Electrospray; Range=101-
108; Evidence={ECO:0000269|PubMed:8483810};
-!- MASS SPECTROMETRY: Mass=1123.0; Method=Electrospray; Range=111-
120; Evidence={ECO:0000269|PubMed:8483810};
-!- MASS SPECTROMETRY: Mass=994.0; Method=Electrospray; Range=123-130;
Evidence={ECO:0000269|PubMed:8483810};
-!- MASS SPECTROMETRY: Mass=1122.0; Method=Electrospray; Range=133-
142; Evidence={ECO:0000269|PubMed:8483810};
-!- MASS SPECTROMETRY: Mass=791.8; Method=Electrospray; Range=168-173;
Evidence={ECO:0000269|PubMed:8483810};
-!- MASS SPECTROMETRY: Mass=792.29; Method=MALDI; Range=168-173;
Evidence={ECO:0000269|PubMed:28847365};
-!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide)
family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; S38096; AAB22368.1; -; Genomic_DNA.
EMBL; U00670; AAC46464.1; -; Genomic_DNA.
EMBL; Z82266; CAB05179.1; -; Genomic_DNA.
EMBL; Z82266; CAD56243.1; -; Genomic_DNA.
EMBL; Z82266; CAD56244.1; -; Genomic_DNA.
PIR; B44827; B44827.
PIR; T21297; T21297.
RefSeq; NP_501592.1; NM_069191.6. [P41855-1]
RefSeq; NP_872077.1; NM_182277.5. [P41855-2]
RefSeq; NP_872078.1; NM_182278.4. [P41855-3]
UniGene; Cel.8838; -.
ProteinModelPortal; P41855; -.
SMR; P41855; -.
STRING; 6239.F23B2.5a; -.
PaxDb; P41855; -.
PRIDE; P41855; -.
EnsemblMetazoa; F23B2.5a; F23B2.5a; WBGene00001444. [P41855-1]
GeneID; 177737; -.
KEGG; cel:CELE_F23B2.5; -.
UCSC; F23B2.5a; c. elegans. [P41855-1]
CTD; 177737; -.
WormBase; F23B2.5a; CE09585; WBGene00001444; flp-1. [P41855-1]
WormBase; F23B2.5b; CE32045; WBGene00001444; flp-1. [P41855-2]
WormBase; F23B2.5c; CE32046; WBGene00001444; flp-1. [P41855-3]
eggNOG; ENOG410J6AD; Eukaryota.
eggNOG; ENOG410YAZT; LUCA.
GeneTree; ENSGT00730000112821; -.
InParanoid; P41855; -.
OMA; RSADPNF; -.
OrthoDB; EOG091G17R9; -.
PhylomeDB; P41855; -.
PRO; PR:P41855; -.
Proteomes; UP000001940; Chromosome IV.
Bgee; WBGene00001444; Expressed in 4 organ(s), highest expression level in multi-cellular organism.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0071855; F:neuropeptide receptor binding; IDA:WormBase.
GO; GO:0006972; P:hyperosmotic response; IMP:WormBase.
GO; GO:0007626; P:locomotory behavior; IMP:WormBase.
GO; GO:0007638; P:mechanosensory behavior; IMP:WormBase.
GO; GO:0007218; P:neuropeptide signaling pathway; IDA:WormBase.
GO; GO:0006937; P:regulation of muscle contraction; IGI:UniProtKB.
GO; GO:0046662; P:regulation of oviposition; IMP:WormBase.
InterPro; IPR002544; FMRFamid-related_peptide-like.
Pfam; PF01581; FARP; 8.
1: Evidence at protein level;
Alternative splicing; Amidation; Cleavage on pair of basic residues;
Complete proteome; Direct protein sequencing; Neuropeptide;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 21 {ECO:0000255}.
PROPEP 22 68
/FTId=PRO_0000009545.
PEPTIDE 71 76 PNFMRY-amide.
/FTId=PRO_0000009546.
PROPEP 79 86
/FTId=PRO_0000009547.
PEPTIDE 89 98 AGSDPNFLRF-amide.
/FTId=PRO_0000009548.
PEPTIDE 101 108 SQPNFLRF-amide.
/FTId=PRO_0000009549.
PEPTIDE 111 120 ASGDPNFLRF-amide.
/FTId=PRO_0000009550.
PEPTIDE 123 130 SDPNFLRF-amide.
/FTId=PRO_0000009551.
PEPTIDE 133 142 AAADPNFLRF-amide.
/FTId=PRO_0000009552.
PEPTIDE 146 154 SADPNFLRF-amide.
/FTId=PRO_0000009553.
PROPEP 157 165
/FTId=PRO_0000009554.
PEPTIDE 168 173 PNFLRF-amide.
{ECO:0000269|PubMed:28847365}.
/FTId=PRO_0000009555.
MOD_RES 76 76 Tyrosine amide.
{ECO:0000269|PubMed:8483810}.
MOD_RES 98 98 Phenylalanine amide.
{ECO:0000269|PubMed:8483810}.
MOD_RES 108 108 Phenylalanine amide.
{ECO:0000269|PubMed:8483810}.
MOD_RES 120 120 Phenylalanine amide.
{ECO:0000269|PubMed:8483810}.
MOD_RES 130 130 Phenylalanine amide.
{ECO:0000269|PubMed:8483810}.
MOD_RES 142 142 Phenylalanine amide.
{ECO:0000269|PubMed:16061202,
ECO:0000269|PubMed:8483810}.
MOD_RES 154 154 Phenylalanine amide.
{ECO:0000269|PubMed:16061202,
ECO:0000269|PubMed:8483810}.
MOD_RES 173 173 Phenylalanine amide.
{ECO:0000269|PubMed:28847365,
ECO:0000269|PubMed:8483810}.
VAR_SEQ 81 113 Missing (in isoform c). {ECO:0000305}.
/FTId=VSP_020150.
VAR_SEQ 81 91 Missing (in isoform b). {ECO:0000305}.
/FTId=VSP_001563.
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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