FLP14_CAEEL
ID FLP14_CAEEL Reviewed; 143 AA.
AC Q9XWV7;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=FMRFamide-like neuropeptides 14;
DE Contains:
DE RecName: Full=KHEYLRF-amide 1;
DE AltName: Full=AF2 1;
DE Contains:
DE RecName: Full=KHEYLRF-amide 2;
DE AltName: Full=AF2 2;
DE Contains:
DE RecName: Full=KHEYLRF-amide 3;
DE AltName: Full=AF2 3;
DE Contains:
DE RecName: Full=KHEYLRF-amide 4;
DE AltName: Full=AF2 4;
DE Flags: Precursor;
GN Name=flp-14 {ECO:0000312|WormBase:Y37D8A.15};
GN ORFNames=Y37D8A.15 {ECO:0000312|WormBase:Y37D8A.15};
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:0000312|EMBL:CAA21533.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA21533.2};
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 [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 104-110; 114-120; 124-130 AND 134-140, MASS
RP SPECTROMETRY, AND AMIDATION AT PHE-110; PHE-120; PHE-130 AND PHE-140.
RX PubMed=8554607; DOI=10.1006/bbrc.1995.2849;
RA Marks N.J., Shaw C., Maule A.G., Davis J.P., Halton D.W., Verhaert P.,
RA Geary T.G., Thompson D.P.;
RT "Isolation of AF2 (KHEYLRFamide) from Caenorhabditis elegans: evidence for
RT the presence of more than one FMRFamide-related peptide-encoding gene.";
RL Biochem. Biophys. Res. Commun. 217:845-851(1995).
RN [3] {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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27855782; DOI=10.7554/elife.19887;
RA Lim M.A., Chitturi J., Laskova V., Meng J., Findeis D., Wiekenberg A.,
RA Mulcahy B., Luo L., Li Y., Lu Y., Hung W., Qu Y., Ho C.Y., Holmyard D.,
RA Ji N., McWhirter R., Samuel A.D., Miller D.M., Schnabel R., Calarco J.A.,
RA Zhen M.;
RT "Neuroendocrine modulation sustains the C. elegans forward motor state.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: FMRFamides and FMRFamide-like peptides are neuropeptides
CC (PubMed:16187307). KHEYLRF-amide has an excitatory effect on dissected
CC pharyngeal myogenic muscle system (PubMed:16187307). Functions in RID
CC peptidergic neurons to promote forward locomotory behavior
CC (PubMed:27855782). {ECO:0000269|PubMed:16187307,
CC ECO:0000269|PubMed:27855782}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Perikaryon
CC {ECO:0000269|PubMed:27855782}. Cell projection, axon
CC {ECO:0000269|PubMed:27855782}.
CC -!- TISSUE SPECIFICITY: Expressed in RID peptidergic neurons, and the
CC sensory neurons ALA, PDE and PLN. {ECO:0000269|PubMed:27855782}.
CC -!- MASS SPECTROMETRY: [KHEYLRF-amide 1]: Mass=920; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:8554607};
CC -!- DISRUPTION PHENOTYPE: Defective forwards locomotion whereby sustained
CC long foraging forwards movements are replaced with shortened forwards
CC runs, more frequent pauses and reversals.
CC {ECO:0000269|PubMed:27855782}.
CC -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.
CC {ECO:0000255}.
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DR EMBL; BX284603; CAA21533.2; -; Genomic_DNA.
DR PIR; T26632; T26632.
DR RefSeq; NP_499682.2; NM_067281.6.
DR AlphaFoldDB; Q9XWV7; -.
DR BioGRID; 41881; 4.
DR STRING; 6239.Y37D8A.15; -.
DR PaxDb; Q9XWV7; -.
DR PeptideAtlas; Q9XWV7; -.
DR EnsemblMetazoa; Y37D8A.15.1; Y37D8A.15.1; WBGene00001457.
DR GeneID; 176708; -.
DR KEGG; cel:CELE_Y37D8A.15; -.
DR UCSC; Y37D8A.15; c. elegans.
DR CTD; 176708; -.
DR WormBase; Y37D8A.15; CE39649; WBGene00001457; flp-14.
DR eggNOG; ENOG502S9P2; Eukaryota.
DR GeneTree; ENSGT00970000196033; -.
DR HOGENOM; CLU_1836862_0_0_1; -.
DR InParanoid; Q9XWV7; -.
DR OMA; CQLYESS; -.
DR OrthoDB; 1542953at2759; -.
DR PRO; PR:Q9XWV7; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001457; Expressed in larva and 3 other tissues.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR002544; FMRFamid-related_peptide-like.
DR Pfam; PF01581; FARP; 4.
PE 1: Evidence at protein level;
KW Amidation; Cell projection; Cleavage on pair of basic residues;
KW Direct protein sequencing; Neuropeptide; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..101
FT /evidence="ECO:0000255"
FT /id="PRO_0000312070"
FT PEPTIDE 104..110
FT /note="KHEYLRF-amide 1"
FT /evidence="ECO:0000269|PubMed:8554607"
FT /id="PRO_0000312071"
FT PEPTIDE 114..120
FT /note="KHEYLRF-amide 2"
FT /evidence="ECO:0000269|PubMed:8554607"
FT /id="PRO_0000312072"
FT PEPTIDE 124..130
FT /note="KHEYLRF-amide 3"
FT /evidence="ECO:0000269|PubMed:8554607"
FT /id="PRO_0000312073"
FT PEPTIDE 134..140
FT /note="KHEYLRF-amide 4"
FT /evidence="ECO:0000269|PubMed:8554607"
FT /id="PRO_0000312074"
FT MOD_RES 110
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:8554607"
FT MOD_RES 120
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:8554607"
FT MOD_RES 130
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:8554607"
FT MOD_RES 140
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:8554607"
SQ SEQUENCE 143 AA; 15894 MW; 08853E29C7784312 CRC64;
MMICLPTALL LSAFVVAASG QEAPAGAGAS GAAQAPHNPK DCQAILANNG DQQEALLCQL
SESSMLLAQL GALVSEGVER LVQTHGLALE EETNEGDNDM EKRKHEYLRF GKRKHEYLRF
GKRKHEYLRF GKRKHEYLRF GRK
