NLP40_CAEEL
ID NLP40_CAEEL Reviewed; 123 AA.
AC Q9N4D8; V6CJ31;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Neuropeptide-like peptides nlp-40 {ECO:0000303|PubMed:16061202};
DE Contains:
DE RecName: Full=Peptide P1 {ECO:0000303|PubMed:23583549};
DE AltName: Full=P1 {ECO:0000303|PubMed:23583549};
DE Contains:
DE RecName: Full=Peptide P2 {ECO:0000303|PubMed:23583549};
DE AltName: Full=P2 {ECO:0000303|PubMed:23583549};
DE Contains:
DE RecName: Full=Peptide P3 {ECO:0000303|PubMed:23583549};
DE AltName: Full=P3 {ECO:0000303|PubMed:23583549};
DE Contains:
DE RecName: Full=Peptide P4 {ECO:0000303|PubMed:23583549};
DE AltName: Full=P4 {ECO:0000303|PubMed:23583549};
DE Flags: Precursor;
GN Name=nlp-40 {ECO:0000312|WormBase:Y74C9A.2a};
GN ORFNames=Y74C9A.2 {ECO:0000312|WormBase:Y74C9A.2a};
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|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 [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 18-29, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 52-65, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16945111; DOI=10.1111/j.1471-4159.2006.04014.x;
RA Husson S.J., Clynen E., Baggerman G., Janssen T., Schoofs L.;
RT "Defective processing of neuropeptide precursors in Caenorhabditis elegans
RT lacking proprotein convertase 2 (KPC-2/EGL-3): mutant analysis by mass
RT spectrometry.";
RL J. Neurochem. 98:1999-2012(2006).
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 18-29 AND 68-74, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=17564681; DOI=10.1111/j.1471-4159.2007.04474.x;
RA Husson S.J., Janssen T., Baggerman G., Bogert B., Kahn-Kirby A.H.,
RA Ashrafi K., Schoofs L.;
RT "Impaired processing of FLP and NLP peptides in carboxypeptidase E (EGL-
RT 21)-deficient Caenorhabditis elegans as analyzed by mass spectrometry.";
RL J. Neurochem. 102:246-260(2007).
RN [5] {ECO:0000305}
RP SYNTHESIS OF P1; P2; P3 AND P4, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23583549; DOI=10.1016/j.cub.2013.03.049;
RA Wang H., Girskis K., Janssen T., Chan J.P., Dasgupta K., Knowles J.A.,
RA Schoofs L., Sieburth D.;
RT "Neuropeptide secreted from a pacemaker activates neurons to control a
RT rhythmic behavior.";
RL Curr. Biol. 23:746-754(2013).
CC -!- FUNCTION: [Peptide P3]: Neuropeptide ligand for the G-protein coupled
CC receptor aex-2. Activates and regulates the rhythmic calcium influx in
CC DVB GABergic neurons during the defecation motor program, which is a
CC coordinated series of three muscle contractions that occurs every 45
CC seconds. {ECO:0000269|PubMed:23583549}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:23583549}.
CC Cytoplasmic vesicle {ECO:0000269|PubMed:23583549}. Note=Secreted by
CC intestinal cells and subsequently endocytosed by coelomocytes. Co-
CC localizes with snt-2 on the cell surface.
CC {ECO:0000269|PubMed:23583549}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:Y74C9A.2a};
CC IsoId=Q9N4D8-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:Y74C9A.2b};
CC IsoId=Q9N4D8-2; Sequence=VSP_058639;
CC -!- TISSUE SPECIFICITY: Expressed in intestinal cells.
CC {ECO:0000269|PubMed:23583549}.
CC -!- DISRUPTION PHENOTYPE: Defecation defects including a distended
CC intestinal lumen, a strong defect in intestinal content expulsion and
CC reduced anterior body wall contraction. {ECO:0000269|PubMed:23583549}.
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DR EMBL; BX284601; CCD68262.1; -; Genomic_DNA.
DR EMBL; BX284601; CDK13438.1; -; Genomic_DNA.
DR RefSeq; NP_001293206.1; NM_001306277.1. [Q9N4D8-2]
DR RefSeq; NP_490661.1; NM_058259.4. [Q9N4D8-1]
DR AlphaFoldDB; Q9N4D8; -.
DR SMR; Q9N4D8; -.
DR STRING; 6239.Y74C9A.2.4; -.
DR EPD; Q9N4D8; -.
DR PaxDb; Q9N4D8; -.
DR PeptideAtlas; Q9N4D8; -.
DR EnsemblMetazoa; Y74C9A.2a.1; Y74C9A.2a.1; WBGene00022276. [Q9N4D8-1]
DR EnsemblMetazoa; Y74C9A.2a.2; Y74C9A.2a.2; WBGene00022276. [Q9N4D8-1]
DR EnsemblMetazoa; Y74C9A.2a.3; Y74C9A.2a.3; WBGene00022276. [Q9N4D8-1]
DR EnsemblMetazoa; Y74C9A.2b.1; Y74C9A.2b.1; WBGene00022276. [Q9N4D8-2]
DR GeneID; 171591; -.
DR KEGG; cel:CELE_Y74C9A.2; -.
DR UCSC; Y74C9A.2.2; c. elegans. [Q9N4D8-1]
DR CTD; 171591; -.
DR WormBase; Y74C9A.2a; CE24660; WBGene00022276; nlp-40. [Q9N4D8-1]
DR WormBase; Y74C9A.2b; CE49228; WBGene00022276; nlp-40. [Q9N4D8-2]
DR eggNOG; ENOG502T1KT; Eukaryota.
DR HOGENOM; CLU_2087024_0_0_1; -.
DR InParanoid; Q9N4D8; -.
DR OMA; LAWQPMK; -.
DR OrthoDB; 1536510at2759; -.
DR PRO; PR:Q9N4D8; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00022276; Expressed in larva and 4 other tissues.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IDA:WormBase.
DR GO; GO:0071855; F:neuropeptide receptor binding; IC:WormBase.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:WormBase.
DR GO; GO:2000294; P:positive regulation of defecation; IMP:WormBase.
PE 1: Evidence at protein level;
KW Alternative splicing; Cleavage on pair of basic residues;
KW Cytoplasmic vesicle; Direct protein sequencing; Neuropeptide;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:16061202,
FT ECO:0000269|PubMed:17564681"
FT PEPTIDE 18..29
FT /note="Peptide P1"
FT /evidence="ECO:0000269|PubMed:16061202,
FT ECO:0000269|PubMed:17564681"
FT /id="PRO_0000438284"
FT PROPEP 30..31
FT /evidence="ECO:0000269|PubMed:16061202"
FT /id="PRO_0000438285"
FT PEPTIDE 32..65
FT /note="Peptide P2"
FT /evidence="ECO:0000305|PubMed:16061202"
FT /id="PRO_0000438286"
FT PROPEP 66..67
FT /evidence="ECO:0000269|PubMed:16061202"
FT /id="PRO_0000438287"
FT PEPTIDE 68..74
FT /note="Peptide P3"
FT /evidence="ECO:0000269|PubMed:17564681"
FT /id="PRO_0000438288"
FT PROPEP 75..76
FT /evidence="ECO:0000269|PubMed:16061202,
FT ECO:0000269|PubMed:17564681"
FT /id="PRO_0000438289"
FT PEPTIDE 77..123
FT /note="Peptide P4"
FT /evidence="ECO:0000303|PubMed:23583549"
FT /id="PRO_0000438290"
FT VAR_SEQ 1..67
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058639"
SQ SEQUENCE 123 AA; 13682 MW; 9C546AE50511AD4F CRC64;
MKLVILLSFV ATVAVFAAPS APAGLEEKLR ALQEQLYSLE KENGVDVKQK EQPAAADTFL
GFVPQKRMVA WQPMKRSMIN EDSRAPLLHA IEARLAEVLR AGERLGVNPE EVLADLRARN
QFQ
