FLP16_CAEBR
ID FLP16_CAEBR Reviewed; 95 AA.
AC A8WTF8;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=FMRFamide-like neuropeptides 16 {ECO:0000250|UniProtKB:Q7YX32};
DE Contains:
DE RecName: Full=AQTFVRF-amide 1 {ECO:0000250|UniProtKB:Q7YX32};
DE Contains:
DE RecName: Full=AQTFVRF-amide 2 {ECO:0000250|UniProtKB:Q7YX32};
DE Contains:
DE RecName: Full=GQTFVRF-amide {ECO:0000250|UniProtKB:Q7YX32};
DE Flags: Precursor;
GN Name=flp-16; ORFNames=CBG02820;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: FMRFamides and FMRFamide-like peptides are neuropeptides.
CC AQTFVRF-amide inhibits the activity of dissected pharyngeal myogenic
CC muscle system (By similarity). {ECO:0000250|UniProtKB:Q7YX32}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q7YX32}.
CC -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.
CC {ECO:0000255}.
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DR EMBL; HE601438; CAP23770.3; -; Genomic_DNA.
DR RefSeq; XP_002631056.1; XM_002631010.1.
DR AlphaFoldDB; A8WTF8; -.
DR SMR; A8WTF8; -.
DR STRING; 6238.CBG02820; -.
DR EnsemblMetazoa; CBG02820a.1; CBG02820a.1; WBGene00025799.
DR GeneID; 8572570; -.
DR KEGG; cbr:CBG_02820; -.
DR CTD; 8572570; -.
DR WormBase; CBG02820a; CBP21170; WBGene00025799; Cbr-flp-16.
DR eggNOG; ENOG502TI12; Eukaryota.
DR HOGENOM; CLU_2456864_0_0_1; -.
DR InParanoid; A8WTF8; -.
DR OMA; VDYASQY; -.
DR OrthoDB; 1584688at2759; -.
DR Proteomes; UP000008549; Chromosome II.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0071244; P:cellular response to carbon dioxide; IEA:EnsemblMetazoa.
DR GO; GO:1903745; P:negative regulation of pharyngeal pumping; IEA:EnsemblMetazoa.
DR GO; GO:0045988; P:negative regulation of striated muscle contraction; ISS:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Amidation; Cleavage on pair of basic residues; Neuropeptide;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..58
FT /evidence="ECO:0000250|UniProtKB:Q7YX32"
FT /id="PRO_0000396646"
FT PEPTIDE 61..67
FT /note="AQTFVRF-amide 1"
FT /evidence="ECO:0000250|UniProtKB:Q7YX32"
FT /id="PRO_0000396647"
FT PEPTIDE 71..77
FT /note="AQTFVRF-amide 2"
FT /evidence="ECO:0000250|UniProtKB:Q7YX32"
FT /id="PRO_0000396648"
FT PEPTIDE 81..87
FT /note="GQTFVRF-amide"
FT /evidence="ECO:0000250|UniProtKB:Q7YX32"
FT /id="PRO_0000396649"
FT PROPEP 90..95
FT /evidence="ECO:0000250|UniProtKB:Q7YX32"
FT /id="PRO_0000396650"
FT MOD_RES 67
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:Q7YX32"
FT MOD_RES 77
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:Q7YX32"
FT MOD_RES 87
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:Q7YX32"
SQ SEQUENCE 95 AA; 10454 MW; 703353AC814DA23B CRC64;
MSLSGFEFSS IIAVLLLLIQ LSSAAVLPVD YASQYGVASA DEMTALPEEG SLFAERPAKR
AQTFVRFGKR AQTFVRFGKR GQTFVRFGRS APFEQ