LURY1_CAEEL
ID LURY1_CAEEL Reviewed; 89 AA.
AC Q9XW71;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Luqin-like RYamide peptides lury-1 {ECO:0000303|PubMed:28847365};
DE Contains:
DE RecName: Full=LURY-1-1 {ECO:0000303|PubMed:28847365};
DE Contains:
DE RecName: Full=LURY-1-2 {ECO:0000303|PubMed:28847365};
DE Flags: Precursor;
GN Name=lury-1 {ECO:0000303|PubMed:28847365};
GN ORFNames=Y75B8A.11 {ECO:0000312|WormBase:Y75B8A.11a};
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 29-35 AND 38-43, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, MASS SPECTROMETRY, DISRUPTION PHENOTYPE,
RP AND AMIDATION AT TYR-35 AND TYR-43.
RX PubMed=28847365; DOI=10.7554/elife.28877;
RA Ohno H., Yoshida M., Sato T., Kato J., Miyazato M., Kojima M., Ida T.,
RA Iino Y.;
RT "Luqin-like RYamide peptides regulate food-evoked responses in C.
RT elegans.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: [LURY-1-1]: Acts as a ligand for the npr-22 receptor and
CC controls food-related processes including feeding, lifespan, egg-laying
CC and roaming behavior. Secreted in the presence of food, leading to
CC reduced feeding and roaming behavior and increased egg laying and
CC lifespan. Activity may be latent under normal conditions but induced
CC under conditions that cause hyperactivation of the pharynx such as
CC abrupt refeeding after starvation. {ECO:0000269|PubMed:28847365}.
CC -!- FUNCTION: [LURY-1-2]: Acts as a ligand for the npr-22 receptor and
CC controls food-related processes including feeding, lifespan, egg-laying
CC and roaming behavior. Secreted in the presence of food, leading to
CC reduced feeding and roaming behavior and increased egg laying and
CC lifespan. Activity may be latent under normal conditions but induced
CC under conditions that cause hyperactivation of the pharynx such as
CC abrupt refeeding after starvation. {ECO:0000269|PubMed:28847365}.
CC -!- SUBCELLULAR LOCATION: [LURY-1-1]: Secreted
CC {ECO:0000269|PubMed:28847365}. Note=Secreted from the M1 and M2
CC pharyngeal neurons in a food-dependent manner with secretion positively
CC controlled by the presence of food. {ECO:0000269|PubMed:28847365}.
CC -!- SUBCELLULAR LOCATION: [LURY-1-2]: Secreted
CC {ECO:0000269|PubMed:28847365}. Note=Secreted from the M1 and M2
CC pharyngeal neurons in a food-dependent manner with secretion positively
CC controlled by the presence of food. {ECO:0000269|PubMed:28847365}.
CC -!- TISSUE SPECIFICITY: Expressed in the M1 and M2 pharyngeal neurons from
CC where the LURY-1-1 and LURY-1-2 peptides are secreted.
CC {ECO:0000269|PubMed:28847365}.
CC -!- DEVELOPMENTAL STAGE: In the M1 pharyngeal neuron, expressed in all
CC larval stages and in adults. In the M2 pharyngeal neuron, expression is
CC not detected in most L1-L3 larva but increases at the L4 larval stage.
CC {ECO:0000269|PubMed:28847365}.
CC -!- MASS SPECTROMETRY: [LURY-1-1]: Mass=818.34; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:28847365};
CC -!- MASS SPECTROMETRY: [LURY-1-2]: Mass=717.25; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:28847365};
CC -!- DISRUPTION PHENOTYPE: Eggs are retained in the body as normal during
CC starvation but the number of eggs laid during the initial refeeding
CC period is reduced and satiety-induced suppression of pharyngeal pumping
CC is slower than wild-type. {ECO:0000269|PubMed:28847365}.
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DR EMBL; BX284603; CAA22099.2; -; Genomic_DNA.
DR RefSeq; NP_001255160.1; NM_001268231.1.
DR AlphaFoldDB; Q9XW71; -.
DR STRING; 6239.Y75B8A.11a; -.
DR PaxDb; Q9XW71; -.
DR EnsemblMetazoa; Y75B8A.11a.1; Y75B8A.11a.1; WBGene00013548.
DR GeneID; 190703; -.
DR KEGG; cel:CELE_Y75B8A.11; -.
DR UCSC; Y75B8A.11; c. elegans.
DR CTD; 190703; -.
DR WormBase; Y75B8A.11a; CE47414; WBGene00013548; lury-1.
DR eggNOG; ENOG502TIFM; Eukaryota.
DR HOGENOM; CLU_2485315_0_0_1; -.
DR InParanoid; Q9XW71; -.
DR OMA; YICLPVD; -.
DR OrthoDB; 1624990at2759; -.
DR PRO; PR:Q9XW71; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00013548; Expressed in larva and 3 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0071855; F:neuropeptide receptor binding; IDA:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:2000252; P:negative regulation of feeding behavior; IMP:UniProtKB.
DR GO; GO:0040013; P:negative regulation of locomotion; IMP:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:1901046; P:positive regulation of oviposition; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Neuropeptide; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..26
FT /evidence="ECO:0000305"
FT /id="PRO_0000442510"
FT PEPTIDE 29..35
FT /note="LURY-1-1"
FT /evidence="ECO:0000269|PubMed:28847365"
FT /id="PRO_0000442511"
FT PEPTIDE 38..43
FT /note="LURY-1-2"
FT /evidence="ECO:0000269|PubMed:28847365"
FT /id="PRO_0000442512"
FT PROPEP 47..89
FT /evidence="ECO:0000305"
FT /id="PRO_0000442513"
FT MOD_RES 35
FT /note="Tyrosine amide"
FT /evidence="ECO:0000305|PubMed:28847365"
FT MOD_RES 43
FT /note="Tyrosine amide"
FT /evidence="ECO:0000305|PubMed:28847365"
SQ SEQUENCE 89 AA; 10038 MW; D609F9AA871E55CD CRC64;
MLTRVPVLIL AVIVMLALCQ EPEKPEKRPA LLSRYGRAVL PRYGKRSGNL MESSQNSLTE
ESSDVVCQLI DGKYICLPVD AVRFRPFFL
