FLP13_CAEEL
ID FLP13_CAEEL Reviewed; 160 AA.
AC O44185;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=FMRFamide-like neuropeptides 13;
DE Contains:
DE RecName: Full=SDRPTRAMDSPLIRF-amide;
DE Contains:
DE RecName: Full=AMDSPLIRF-amide;
DE Contains:
DE RecName: Full=AADGAPLIRF-amide 1;
DE Contains:
DE RecName: Full=APEASPFIRF-amide 1;
DE Contains:
DE RecName: Full=AADGAPLIRF-amide 2;
DE Contains:
DE RecName: Full=APEASPFIRF-amide 2;
DE Contains:
DE RecName: Full=ASPSAPLIRF-amide;
DE Contains:
DE RecName: Full=SPSAVPLIRF-amide;
DE Contains:
DE RecName: Full=SAAAPLIRF-amide;
DE Contains:
DE RecName: Full=ASSAPLIRF-amide;
DE Flags: Precursor;
GN Name=flp-13 {ECO:0000312|WormBase:F33D4.3};
GN ORFNames=F33D4.3 {ECO:0000312|WormBase:F33D4.3};
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}
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND AMIDATION AT PHE-157.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:9685599};
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:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:9851916};
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 52-60; 64-73; 76-85; 89-98; 101-110; 114-123; 126-135
RP AND 138-146, AND AMIDATION AT PHE-60; PHE-73; PHE-85; PHE-98; PHE-110;
RP PHE-123; PHE-135 AND PHE-146.
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 PROTEIN SEQUENCE OF 64-73 AND 89-98, FUNCTION, MASS SPECTROMETRY, AND
RP AMIDATION AT PHE-73 AND PHE-98.
RX PubMed=11527423; DOI=10.1006/bbrc.2001.5524;
RA Marks N.J., Shaw C., Halton D.W., Thompson D.P., Geary T.G., Li C.,
RA Maule A.G.;
RT "Isolation and preliminary biological assessment of AADGAPLIRFamide and
RT SVPGVLRFamide from Caenorhabditis elegans.";
RL Biochem. Biophys. Res. Commun. 286:1170-1176(2001).
RN [5] {ECO:0000305}
RP PROTEIN SEQUENCE OF 76-85 AND 101-110, FUNCTION, MASS SPECTROMETRY, AND
RP AMIDATION AT PHE-85 AND PHE-110.
RX PubMed=9070852; DOI=10.1006/bbrc.1997.6155;
RA Marks N.J., Maule A.G., Geary T.G., Thompson D.P., Davis J.P., Halton D.W.,
RA Verhaert P., Shaw C.;
RT "APEASPFIRFamide, a novel FMRFamide-related decapeptide from Caenorhabditis
RT elegans: structure and myoactivity.";
RL Biochem. Biophys. Res. Commun. 231:591-595(1997).
RN [6] {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 [7] {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 [8]
RP FUNCTION (AADGAPLIRF-AMIDE; ASPSAPLIRF-AMIDE; SPSAVPLIRF-AMIDE;
RP SAAAPLIRF-AMIDE AND ASSAPLIRF-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] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=27546573; DOI=10.1016/j.cub.2016.07.048;
RA Nath R.D., Chow E.S., Wang H., Schwarz E.M., Sternberg P.W.;
RT "C. elegans Stress-Induced Sleep Emerges from the Collective Action of
RT Multiple Neuropeptides.";
RL Curr. Biol. 26:2446-2455(2016).
RN [10]
RP FUNCTION (AADGAPLIRF-AMIDE; APEASPFIRF-AMIDE; ASPSAPLIRF-AMIDE;
RP SPSAVPLIRF-AMIDE; SAAAPLIRF-AMIDE; ASSAPLIRF-AMIDE AND AMDSPLIRF-AMIDE).
RX PubMed=28094002; DOI=10.7554/elife.19837;
RA Iannacone M.J., Beets I., Lopes L.E., Churgin M.A., Fang-Yen C.,
RA Nelson M.D., Schoofs L., Raizen D.M.;
RT "The RFamide receptor DMSR-1 regulates stress-induced sleep in C.
RT elegans.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: Probable FMRFamide-like neuropeptides (PubMed:28094002,
CC PubMed:16377032). Binds to neuronal receptors such as dmsr-1 to promote
CC sleep in response to cellular stress also known as stress-induced sleep
CC (SIS) (PubMed:28094002). Plays a role in behaviors associated with SIS,
CC acting in concert with the FMRFamide related peptide, flp-24 and
CC neuropeptide-like protein nlp-8 (PubMed:27546573).
CC {ECO:0000269|PubMed:16377032, ECO:0000269|PubMed:27546573,
CC ECO:0000269|PubMed:28094002, ECO:0000305}.
CC -!- FUNCTION: AADGAPLIRF-amide: Inhibits muscle tension in somatic muscle
CC (PubMed:11527423). Acts as a ligand for the npr-22 receptor in vitro
CC (PubMed:16377032). Acts as a ligand for isoform a of the dmsr-1 G-
CC protein coupled receptor in vitro (PubMed:28094002).
CC {ECO:0000269|PubMed:11527423, ECO:0000269|PubMed:16377032,
CC ECO:0000269|PubMed:28094002}.
CC -!- FUNCTION: APEASPFIRF-amide: Inhibits muscle tension in somatic muscle
CC (PubMed:9070852). Potent inhibitor of the activity of the dissected
CC pharyngeal myogenic muscle system (PubMed:16187307). Acts as a ligand
CC for isoform a of the dmsr-1 G-protein coupled receptor in vitro
CC (PubMed:28094002). {ECO:0000269|PubMed:16187307,
CC ECO:0000269|PubMed:28094002, ECO:0000269|PubMed:9070852}.
CC -!- FUNCTION: [ASPSAPLIRF-amide]: Acts as a ligand for the npr-22 receptor
CC in vitro. Acts as a ligand for isoform a of the dmsr-1 G-protein
CC coupled receptor in vitro (PubMed:28094002).
CC {ECO:0000269|PubMed:16377032, ECO:0000269|PubMed:28094002}.
CC -!- FUNCTION: [SPSAVPLIRF-amide]: Acts as a ligand for the npr-22 receptor
CC in vitro. Acts as a ligand for isoform a of the dmsr-1 G-protein
CC coupled receptor in vitro (PubMed:28094002).
CC {ECO:0000269|PubMed:16377032, ECO:0000269|PubMed:28094002}.
CC -!- FUNCTION: [SAAAPLIRF-amide]: Acts as a ligand for the npr-22 receptor
CC in vitro. Acts as a ligand for isoform a of the dmsr-1 G-protein
CC coupled receptor in vitro (PubMed:28094002).
CC {ECO:0000269|PubMed:16377032, ECO:0000269|PubMed:28094002}.
CC -!- FUNCTION: [ASSAPLIRF-amide]: Acts as a ligand for the npr-22 receptor
CC in vitro. Acts as a ligand for isoform a of the dmsr-1 G-protein
CC coupled receptor in vitro (PubMed:28094002).
CC {ECO:0000269|PubMed:16377032, ECO:0000269|PubMed:28094002}.
CC -!- FUNCTION: [AMDSPLIRF-amide]: Acts as a ligand for isoform a of the
CC dmsr-1 G-protein coupled receptor in vitro.
CC {ECO:0000269|PubMed:28094002}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the ASE sensory neurons, the DD motor
CC neurons, the 15, M3 and M5 cholinergic pharyngeal motoneurons, and the
CC ASG, ASK and BAG neurons. {ECO:0000269|PubMed:15236235}.
CC -!- DEVELOPMENTAL STAGE: Expressed from the comma stage of embryogenesis,
CC during all larval stages, and in low levels in adults (PubMed:9685599,
CC PubMed:15236235). Expressed in the ALA neuron in L4 stage larvae
CC (PubMed:27546573). {ECO:0000269|PubMed:15236235,
CC ECO:0000269|PubMed:27546573, ECO:0000269|PubMed:9685599}.
CC -!- MASS SPECTROMETRY: [AADGAPLIRF-amide 1]: Mass=1032; Method=MALDI;
CC Note=The measured mass is that of either AADGAPLIRF-amide 1 or
CC AADGAPLIRF-amide 2.; Evidence={ECO:0000269|PubMed:11527423};
CC -!- MASS SPECTROMETRY: [APEASPFIRF-amide 1]: Mass=1133.7; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9070852};
CC -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.
CC {ECO:0000255}.
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DR EMBL; AF042400; AAC08951.1; -; mRNA.
DR EMBL; BX284604; CCD63768.1; -; Genomic_DNA.
DR PIR; T32553; T32553.
DR RefSeq; NP_501255.1; NM_068854.1.
DR AlphaFoldDB; O44185; -.
DR BioGRID; 42665; 1.
DR STRING; 6239.F33D4.3; -.
DR EPD; O44185; -.
DR PaxDb; O44185; -.
DR EnsemblMetazoa; F33D4.3.1; F33D4.3.1; WBGene00001456.
DR GeneID; 177547; -.
DR KEGG; cel:CELE_F33D4.3; -.
DR UCSC; F33D4.3; c. elegans.
DR CTD; 177547; -.
DR WormBase; F33D4.3; CE17033; WBGene00001456; flp-13.
DR eggNOG; ENOG502SDD0; Eukaryota.
DR HOGENOM; CLU_1723987_0_0_1; -.
DR InParanoid; O44185; -.
DR OMA; FFQFLEN; -.
DR OrthoDB; 1384980at2759; -.
DR PhylomeDB; O44185; -.
DR PRO; PR:O44185; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001456; Expressed in larva and 3 other tissues.
DR GO; GO:0005576; C:extracellular region; IC:UniProtKB.
DR GO; GO:0071855; F:neuropeptide receptor binding; IDA:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:UniProtKB.
DR GO; GO:1900034; P:regulation of cellular response to heat; IGI:UniProtKB.
DR GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; IMP:UniProtKB.
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; Repeat; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..43
FT /evidence="ECO:0000305"
FT /id="PRO_0000009556"
FT PEPTIDE 46..60
FT /note="SDRPTRAMDSPLIRF-amide"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:9685599"
FT /id="PRO_0000248047"
FT PEPTIDE 52..60
FT /note="AMDSPLIRF-amide"
FT /evidence="ECO:0000269|PubMed:16061202"
FT /id="PRO_0000311849"
FT PEPTIDE 64..73
FT /note="AADGAPLIRF-amide 1"
FT /evidence="ECO:0000269|PubMed:11527423,
FT ECO:0000269|PubMed:16061202"
FT /id="PRO_0000009557"
FT PEPTIDE 76..85
FT /note="APEASPFIRF-amide 1"
FT /evidence="ECO:0000269|PubMed:16061202,
FT ECO:0000269|PubMed:9070852"
FT /id="PRO_0000009558"
FT PEPTIDE 89..98
FT /note="AADGAPLIRF-amide 2"
FT /evidence="ECO:0000269|PubMed:11527423,
FT ECO:0000269|PubMed:16061202"
FT /id="PRO_0000009559"
FT PEPTIDE 101..110
FT /note="APEASPFIRF-amide 2"
FT /evidence="ECO:0000269|PubMed:16061202,
FT ECO:0000269|PubMed:9070852"
FT /id="PRO_0000248048"
FT PEPTIDE 114..123
FT /note="ASPSAPLIRF-amide"
FT /evidence="ECO:0000269|PubMed:16061202"
FT /id="PRO_0000248049"
FT PEPTIDE 126..135
FT /note="SPSAVPLIRF-amide"
FT /evidence="ECO:0000269|PubMed:16061202"
FT /id="PRO_0000248050"
FT PEPTIDE 138..146
FT /note="SAAAPLIRF-amide"
FT /evidence="ECO:0000269|PubMed:16061202"
FT /id="PRO_0000248051"
FT PEPTIDE 149..157
FT /note="ASSAPLIRF-amide"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:9685599"
FT /id="PRO_0000248052"
FT MOD_RES 60
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:16061202"
FT MOD_RES 73
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:11527423,
FT ECO:0000269|PubMed:16061202"
FT MOD_RES 85
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:16061202,
FT ECO:0000269|PubMed:9070852"
FT MOD_RES 98
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:11527423,
FT ECO:0000269|PubMed:16061202"
FT MOD_RES 110
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:16061202,
FT ECO:0000269|PubMed:9070852"
FT MOD_RES 123
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:16061202"
FT MOD_RES 135
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:16061202"
FT MOD_RES 146
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:16061202"
FT MOD_RES 157
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:9685599"
SQ SEQUENCE 160 AA; 17736 MW; BE4C24E9B85FCD11 CRC64;
MMTSLLTISM FVVAIQAFDS SEIRMLDEQY DTKNPFFQFL ENSKRSDRPT RAMDSPLIRF
GKRAADGAPL IRFGRAPEAS PFIRFGKRAA DGAPLIRFGR APEASPFIRF GKRASPSAPL
IRFGRSPSAV PLIRFGRSAA APLIRFGRAS SAPLIRFGRK
