FLP7_CAEEL
ID FLP7_CAEEL Reviewed; 177 AA.
AC G5EEC2;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=FMRFamide-like neuropeptides 7 {ECO:0000305};
DE Contains:
DE RecName: Full=TPMQRSSMVRF-amide 1 {ECO:0000305|PubMed:16377032};
DE Contains:
DE RecName: Full=SPMQRSSMVRF-amide 1 {ECO:0000305|PubMed:16377032};
DE Contains:
DE RecName: Full=SPMQRSSMVRF-amide 2 {ECO:0000305|PubMed:16377032};
DE Contains:
DE RecName: Full=SPMQRSSMVRF-amide 3 {ECO:0000305|PubMed:16377032};
DE Contains:
DE RecName: Full=SPMERSAMVRF-amide {ECO:0000305|PubMed:16377032};
DE Contains:
DE RecName: Full=SPMDRSKMVRF-amide {ECO:0000305|PubMed:16377032};
DE Contains:
DE RecName: Full=SSIDRASMVRL-amide {ECO:0000305|PubMed:16377032};
DE Contains:
DE RecName: Full=TPMQRSSMVRF-amide 2 {ECO:0000305|PubMed:16377032};
DE Flags: Precursor;
GN Name=flp-7 {ECO:0000312|WormBase:F49E10.3};
GN ORFNames=F49E10.3 {ECO:0000312|WormBase:F49E10.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:AAC08944.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAC08944.1};
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:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 FUNCTION, AND AMIDATION AT PHE-62; PHE-75; PHE-89; PHE-103; PHE-117;
RP PHE-130; LEU-143 AND PHE-157.
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 [4] {ECO:0000305}
RP 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 [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=28128367; DOI=10.1038/ncomms14237;
RA Palamiuc L., Noble T., Witham E., Ratanpal H., Vaughan M., Srinivasan S.;
RT "A tachykinin-like neuroendocrine signalling axis couples central serotonin
RT action and nutrient sensing with peripheral lipid metabolism.";
RL Nat. Commun. 8:14237-14237(2017).
RN [6]
RP FUNCTION.
RX PubMed=33078707; DOI=10.7554/elife.58815;
RA Littlejohn N.K., Seban N., Liu C.C., Srinivasan S.;
RT "A feedback loop governs the relationship between lipid metabolism and
RT longevity.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: FMRFamide-like neuropeptides (PubMed:16377032,
CC PubMed:28128367). Stimulates serotonin-induced fat loss by binding to
CC and activating the npr-22 receptor which leads to induction of the
CC atgl-1 lipase and subsequent fat loss (PubMed:33078707). Together with
CC atfs-1, negatively regulates the expression of the transcription
CC regulator hlh-11, to promote expression of atgl-1, and thus atgl-1-
CC dependent fat oxidation in response to mitochondrial stress
CC (PubMed:33078707). {ECO:0000269|PubMed:16377032,
CC ECO:0000269|PubMed:28128367, ECO:0000269|PubMed:33078707}.
CC -!- FUNCTION: TPMQRSSMVRF-amide: Acts as a ligand for the npr-22 receptor
CC in vitro. {ECO:0000269|PubMed:16377032}.
CC -!- FUNCTION: SPMQRSSMVRF-amide: Acts as a ligand for the npr-22 receptor
CC in vitro. {ECO:0000269|PubMed:16377032}.
CC -!- FUNCTION: [SPMERSAMVRF-amide]: Acts as a ligand for the npr-22 receptor
CC in vitro. {ECO:0000269|PubMed:16377032}.
CC -!- FUNCTION: [SPMDRSKMVRF-amide]: Acts as a ligand for the npr-22 receptor
CC in vitro. {ECO:0000269|PubMed:16377032}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28128367}.
CC Note=Secreted from the ASI sensory neurons in response to serotonin or
CC octopamine. {ECO:0000269|PubMed:28128367}.
CC -!- TISSUE SPECIFICITY: Expressed in the ASI sensory neurons, the ALA
CC interneuron and the AVG interneuron from where secretion occurs.
CC Expression in the ASI neurons is necessary and sufficient to maintain
CC serotonin-induced fat loss. {ECO:0000269|PubMed:28128367}.
CC -!- DEVELOPMENTAL STAGE: Expressed in eggs, all larval stages and in adult
CC (PubMed:9685599). Expressed in the ALA neuron in L4 stage larvae
CC (PubMed:27546573). {ECO:0000269|PubMed:27546573,
CC ECO:0000269|PubMed:9685599}.
CC -!- DISRUPTION PHENOTYPE: Retention of a significantly greater proportion
CC of body fat compared to wild-type following treatment with serotonin,
CC almost complete suppression of the transcriptional induction of the
CC atgl-1 lipase, reduced egg-laying and suppression of octopamine-induced
CC fat loss. No effect on serotonin-induced food intake, reproduction or
CC the enhanced slowing response which is a satiety-like locomotor
CC response to food availability. {ECO:0000269|PubMed:28128367}.
CC -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.
CC {ECO:0000305}.
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DR EMBL; AF042393; AAC08944.1; -; mRNA.
DR EMBL; BX284606; CCD71566.1; -; Genomic_DNA.
DR PIR; T34292; T34292.
DR RefSeq; NP_508985.1; NM_076584.4.
DR AlphaFoldDB; G5EEC2; -.
DR IntAct; G5EEC2; 2.
DR STRING; 6239.F49E10.3; -.
DR PaxDb; G5EEC2; -.
DR EnsemblMetazoa; F49E10.3.1; F49E10.3.1; WBGene00001450.
DR GeneID; 180854; -.
DR KEGG; cel:CELE_F49E10.3; -.
DR CTD; 180854; -.
DR WormBase; F49E10.3; CE07264; WBGene00001450; flp-7.
DR eggNOG; ENOG502SVJ1; Eukaryota.
DR HOGENOM; CLU_1519225_0_0_1; -.
DR InParanoid; G5EEC2; -.
DR OMA; MERSAMV; -.
DR OrthoDB; 1744397at2759; -.
DR PhylomeDB; G5EEC2; -.
DR PRO; PR:G5EEC2; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001450; Expressed in larva and 3 other tissues.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0071855; F:neuropeptide receptor binding; IDA:WormBase.
DR GO; GO:0040013; P:negative regulation of locomotion; IDA:WormBase.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:WormBase.
DR GO; GO:0019932; P:second-messenger-mediated signaling; IDA:WormBase.
DR InterPro; IPR002544; FMRFamid-related_peptide-like.
DR Pfam; PF01581; FARP; 7.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Neuropeptide;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..49
FT /evidence="ECO:0000305"
FT /id="PRO_0000442500"
FT PEPTIDE 52..62
FT /note="TPMQRSSMVRF-amide 1"
FT /evidence="ECO:0000305|PubMed:16377032"
FT /id="PRO_0000442501"
FT PEPTIDE 65..75
FT /note="SPMQRSSMVRF-amide 1"
FT /evidence="ECO:0000305|PubMed:16377032"
FT /id="PRO_0000442502"
FT PEPTIDE 79..89
FT /note="SPMQRSSMVRF-amide 2"
FT /evidence="ECO:0000305|PubMed:16377032"
FT /id="PRO_0000442503"
FT PEPTIDE 93..103
FT /note="SPMQRSSMVRF-amide 3"
FT /evidence="ECO:0000305|PubMed:16377032"
FT /id="PRO_0000442504"
FT PEPTIDE 107..117
FT /note="SPMERSAMVRF-amide"
FT /evidence="ECO:0000305|PubMed:16377032"
FT /id="PRO_0000442505"
FT PEPTIDE 120..130
FT /note="SPMDRSKMVRF-amide"
FT /evidence="ECO:0000305|PubMed:16377032"
FT /id="PRO_0000442506"
FT PEPTIDE 133..143
FT /note="SSIDRASMVRL-amide"
FT /evidence="ECO:0000305|PubMed:16377032"
FT /id="PRO_0000442507"
FT PEPTIDE 147..157
FT /note="TPMQRSSMVRF-amide 2"
FT /evidence="ECO:0000305|PubMed:16377032"
FT /id="PRO_0000442508"
FT PROPEP 161..177
FT /evidence="ECO:0000305"
FT /id="PRO_0000442509"
FT REGION 25..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 62
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000305|PubMed:16377032"
FT MOD_RES 75
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000305|PubMed:16377032"
FT MOD_RES 89
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000305|PubMed:16377032"
FT MOD_RES 103
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000305|PubMed:16377032"
FT MOD_RES 117
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000305|PubMed:16377032"
FT MOD_RES 130
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000305|PubMed:16377032"
FT MOD_RES 143
FT /note="Leucine amide"
FT /evidence="ECO:0000305|PubMed:16377032"
FT MOD_RES 157
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000305|PubMed:16377032"
SQ SEQUENCE 177 AA; 20513 MW; 897445FB204B3AE1 CRC64;
MLGSRFLLLA LGLLVLVLAE ESAEQQVQEP TELEKSGEQL SEEDLIDEQK RTPMQRSSMV
RFGRSPMQRS SMVRFGKRSP MQRSSMVRFG KRSPMQRSSM VRFGKRSPME RSAMVRFGRS
PMDRSKMVRF GRSSIDRASM VRLGKRTPMQ RSSMVRFGKR SMEFEMQSNE KNIEDSE
