NLP29_CAEEL
ID NLP29_CAEEL Reviewed; 73 AA.
AC O44664;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Neuropeptide-like protein 29;
DE Contains:
DE RecName: Full=QWGYGGY-amide;
DE Contains:
DE RecName: Full=GYGGYGGY-amide;
DE Contains:
DE RecName: Full=GMYGGY-amide;
DE Contains:
DE RecName: Full=GMYGGW-amide;
DE Flags: Precursor;
GN Name=nlp-29; ORFNames=B0213.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=11717458; DOI=10.1073/pnas.241231298;
RA Nathoo A.N., Moeller R.A., Westlund B.A., Hart A.C.;
RT "Identification of neuropeptide-like protein gene families in
RT Caenorhabditis elegans and other species.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14000-14005(2001).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15048112; DOI=10.1038/ni1060;
RA Couillault C., Pujol N., Reboul J., Sabatier L., Guichou J.-F., Kohara Y.,
RA Ewbank J.J.;
RT "TLR-independent control of innate immunity in Caenorhabditis elegans by
RT the TIR domain adaptor protein TIR-1, an ortholog of human SARM.";
RL Nat. Immunol. 5:488-494(2004).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18394898; DOI=10.1016/j.cub.2008.02.079;
RA Pujol N., Cypowyj S., Ziegler K., Millet A., Astrain A., Goncharov A.,
RA Jin Y., Chisholm A.D., Ewbank J.J.;
RT "Distinct innate immune responses to infection and wounding in the C.
RT elegans epidermis.";
RL Curr. Biol. 18:481-489(2008).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY FUNGAL INFECTION; PHYSICAL
RP INJURY AND OSMOTIC STRESS.
RX PubMed=19380113; DOI=10.1016/j.chom.2009.03.006;
RA Ziegler K., Kurz C.L., Cypowyj S., Couillault C., Pophillat M., Pujol N.,
RA Ewbank J.J.;
RT "Antifungal innate immunity in C. elegans: PKCdelta links G protein
RT signaling and a conserved p38 MAPK cascade.";
RL Cell Host Microbe 5:341-352(2009).
CC -!- FUNCTION: Antimicrobial peptides that have antibacterial activity
CC against the Gram-negative bacteria S.marcescens. Has antifungal
CC activity against D.coniospora (PubMed:15048112, PubMed:19380113). May
CC play a role in response to physical injury and osmotic stress
CC (PubMed:18394898, PubMed:19380113). {ECO:0000269|PubMed:15048112,
CC ECO:0000269|PubMed:18394898, ECO:0000269|PubMed:19380113}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Weakly or not expressed in absence of infection.
CC Upon infection by D.coniospora, it is expressed in hypoderm. Also
CC expressed in perivulval cells when D.coniospora spores adhere to this
CC region (PubMed:11717458, PubMed:15048112, PubMed:18394898,
CC PubMed:19380113). Expressed in hypodermis upon physical injury
CC (PubMed:18394898). {ECO:0000269|PubMed:11717458,
CC ECO:0000269|PubMed:15048112, ECO:0000269|PubMed:18394898,
CC ECO:0000269|PubMed:19380113}.
CC -!- INDUCTION: Upon D.coniospora and S.marcescens infection
CC (PubMed:15048112, PubMed:19380113). Upon physical injury and osmotic
CC stress (PubMed:19380113). {ECO:0000269|PubMed:15048112,
CC ECO:0000269|PubMed:19380113}.
CC -!- SIMILARITY: Belongs to the YARP (YGGW-amide related peptide) family.
CC {ECO:0000305}.
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DR EMBL; FO080121; CCD61354.1; -; Genomic_DNA.
DR PIR; C89016; C89016.
DR RefSeq; NP_504109.1; NM_071708.4.
DR AlphaFoldDB; O44664; -.
DR BioGRID; 43859; 1.
DR STRING; 6239.B0213.4; -.
DR EPD; O44664; -.
DR PaxDb; O44664; -.
DR EnsemblMetazoa; B0213.4.1; B0213.4.1; WBGene00003767.
DR GeneID; 178805; -.
DR KEGG; cel:CELE_B0213.4; -.
DR UCSC; B0213.4; c. elegans.
DR CTD; 178805; -.
DR WormBase; B0213.4; CE16775; WBGene00003767; nlp-29.
DR eggNOG; ENOG502TJS1; Eukaryota.
DR HOGENOM; CLU_193227_0_0_1; -.
DR OMA; CCGWGYP; -.
DR PRO; PR:O44664; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003767; Expressed in larva and 4 other tissues.
DR GO; GO:0005615; C:extracellular space; ISM:WormBase.
DR GO; GO:0071855; F:neuropeptide receptor binding; ISM:WormBase.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
PE 2: Evidence at transcript level;
KW Amidation; Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW Fungicide; Neuropeptide; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PEPTIDE 23..29
FT /note="QWGYGGY-amide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041493"
FT PEPTIDE 32..39
FT /note="GYGGYGGY-amide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041494"
FT PEPTIDE 42..47
FT /note="GMYGGY-amide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041495"
FT PEPTIDE 50..55
FT /note="GMYGGY-amide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041496"
FT PEPTIDE 58..63
FT /note="GMYGGY-amide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041497"
FT PEPTIDE 66..71
FT /note="GMYGGW-amide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041498"
FT MOD_RES 29
FT /note="Tyrosine amide"
FT /evidence="ECO:0000255"
FT MOD_RES 39
FT /note="Tyrosine amide"
FT /evidence="ECO:0000255"
FT MOD_RES 47
FT /note="Tyrosine amide"
FT /evidence="ECO:0000255"
FT MOD_RES 55
FT /note="Tyrosine amide"
FT /evidence="ECO:0000255"
FT MOD_RES 63
FT /note="Tyrosine amide"
FT /evidence="ECO:0000255"
FT MOD_RES 71
FT /note="Tryptophan amide"
FT /evidence="ECO:0000255"
SQ SEQUENCE 73 AA; 7617 MW; E359319650D652CC CRC64;
MISTSSILVL VVLLACFMAA SAQWGYGGYG RGYGGYGGYG RGMYGGYGRG MYGGYGRGMY
GGYGRGMYGG WGK
