NLP31_CAEEL
ID NLP31_CAEEL Reviewed; 75 AA.
AC O44662;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Neuropeptide-like protein 31;
DE Contains:
DE RecName: Full=QWGYGGY-amide;
DE Contains:
DE RecName: Full=GYGGYGGY-amide;
DE Contains:
DE RecName: Full=GYGGY-amide;
DE Contains:
DE RecName: Full=GMYGGY-amide;
DE Contains:
DE RecName: Full=PYGGYGW-amide;
DE Flags: Precursor;
GN Name=nlp-31; ORFNames=B0213.6;
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 SYNTHESIS, 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).
CC -!- FUNCTION: Antimicrobial peptides that have antifungal activity against
CC D.coniospora. Has weak antibacterial activity against Gram-positive
CC bacteria M.luteus and Gram-negative E.coli.
CC {ECO:0000269|PubMed:15048112}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in hypoderm.
CC {ECO:0000269|PubMed:11717458, ECO:0000269|PubMed:15048112}.
CC -!- DEVELOPMENTAL STAGE: Expressed in precomma stasge embryos.
CC -!- INDUCTION: Strongly up-regulated upon D.coniospora infection.
CC {ECO:0000269|PubMed:15048112}.
CC -!- SIMILARITY: Belongs to the YARP (YGGW-amide related peptide) family.
CC {ECO:0000305}.
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DR EMBL; FO080121; CCD61356.1; -; Genomic_DNA.
DR PIR; A89016; A89016.
DR RefSeq; NP_504107.1; NM_071706.5.
DR AlphaFoldDB; O44662; -.
DR BioGRID; 43858; 1.
DR STRING; 6239.B0213.6; -.
DR EPD; O44662; -.
DR PaxDb; O44662; -.
DR PeptideAtlas; O44662; -.
DR EnsemblMetazoa; B0213.6.1; B0213.6.1; WBGene00003769.
DR GeneID; 178804; -.
DR KEGG; cel:CELE_B0213.6; -.
DR UCSC; B0213.6; c. elegans.
DR CTD; 178804; -.
DR WormBase; B0213.6; CE16777; WBGene00003769; nlp-31.
DR eggNOG; ENOG502TJS1; Eukaryota.
DR HOGENOM; CLU_193227_0_0_1; -.
DR OMA; CHPSCHE; -.
DR PRO; PR:O44662; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003769; Expressed in larva and 4 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:WormBase.
DR GO; GO:0042742; P:defense response to bacterium; IDA:WormBase.
DR GO; GO:0050832; P:defense response to fungus; IDA:WormBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:WormBase.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:WormBase.
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_0000041505"
FT PEPTIDE 32..39
FT /note="GYGGYGGY-amide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041506"
FT PEPTIDE 42..49
FT /note="GYGGYGGY-amide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041507"
FT PEPTIDE 52..56
FT /note="GYGGY-amide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041508"
FT PEPTIDE 59..64
FT /note="GMYGGY-amide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041509"
FT PEPTIDE 67..73
FT /note="PYGGYGW-amide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041510"
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 49
FT /note="Tyrosine amide"
FT /evidence="ECO:0000255"
FT MOD_RES 56
FT /note="Tyrosine amide"
FT /evidence="ECO:0000255"
FT MOD_RES 64
FT /note="Tyrosine amide"
FT /evidence="ECO:0000255"
FT MOD_RES 73
FT /note="Tryptophan amide"
FT /evidence="ECO:0000255"
SQ SEQUENCE 75 AA; 7788 MW; 5446D0D772B9F5E6 CRC64;
MISTSSILVL VVLLACFMAA NAQWGYGGYG RGYGGYGGYG RGYGGYGGYG RGYGGYGRGM
YGGYGRPYGG YGWGK
