ILB5_CAEEL
ID ILB5_CAEEL Reviewed; 112 AA.
AC P56174; Q23631;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Probable insulin-like peptide beta-type 5;
DE Flags: Precursor;
GN Name=ins-6; ORFNames=ZK84.6;
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 SEQUENCE REVISION, AND SIMILARITY TO INSULIN.
RX PubMed=9548970; DOI=10.1101/gr.8.4.348;
RA Duret L., Guex N., Peitsch M.C., Bairoch A.;
RT "New insulin-like proteins with atypical disulfide bond pattern
RT characterized in Caenorhabditis elegans by comparative sequence analysis
RT and homology modeling.";
RL Genome Res. 8:348-353(1998).
RN [3]
RP FUNCTION, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF 57-ARG-ARG-58.
RX PubMed=23665919; DOI=10.1038/emboj.2013.91;
RA Hung W.L., Hwang C., Gao S., Liao E.H., Chitturi J., Wang Y., Li H.,
RA Stigloher C., Bessereau J.L., Zhen M.;
RT "Attenuation of insulin signalling contributes to FSN-1-mediated regulation
RT of synapse development.";
RL EMBO J. 32:1745-1760(2013).
RN [4]
RP FUNCTION, PROTEOLYTIC CLEAVAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 57-ARG-ARG-58.
RX PubMed=24013594; DOI=10.1038/nn.3511;
RA Leinwand S.G., Chalasani S.H.;
RT "Neuropeptide signaling remodels chemosensory circuit composition in
RT Caenorhabditis elegans.";
RL Nat. Neurosci. 16:1461-1467(2013).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=24671950; DOI=10.1242/dev.103846;
RA Hung W.L., Wang Y., Chitturi J., Zhen M.;
RT "A Caenorhabditis elegans developmental decision requires insulin
RT signaling-mediated neuron-intestine communication.";
RL Development 141:1767-1779(2014).
RN [6]
RP STRUCTURE BY NMR OF 63-112, AND DISULFIDE BONDS.
RX PubMed=12670864; DOI=10.1101/gad.1090203;
RA Nelson D.W., Padgett R.W.;
RT "Insulin worms its way into the spotlight.";
RL Genes Dev. 17:813-818(2003).
CC -!- FUNCTION: Probable insulin-like peptide which negatively regulates
CC synapse development at the neuromuscular junctions (PubMed:23665919).
CC Probably acts as a daf-2/InsR agonist ligand to prevent dauer formation
CC under optimal environmental conditions (PubMed:24671950). Acts on AWC
CC sensory neurons to regulate high salt chemotaxis responses
CC (PubMed:24013594). {ECO:0000269|PubMed:23665919,
CC ECO:0000269|PubMed:24013594, ECO:0000269|PubMed:24671950}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed by ASI and ASJ sensory neurons.
CC {ECO:0000269|PubMed:24671950}.
CC -!- PTM: May be processed by serine endoprotease bli-4.
CC {ECO:0000305|PubMed:24013594}.
CC -!- DISRUPTION PHENOTYPE: Severe reduction in Ca(2+) signal in AWC neuron
CC and in chemotaxis in response to high salt concentrations.
CC {ECO:0000269|PubMed:24013594}.
CC -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR EMBL; FO081688; CCD73329.1; -; Genomic_DNA.
DR PIR; T29014; T29014.
DR RefSeq; NP_495198.1; NM_062797.1.
DR PDB; 2KJI; NMR; -; A=63-112.
DR PDBsum; 2KJI; -.
DR AlphaFoldDB; P56174; -.
DR SMR; P56174; -.
DR BioGRID; 56186; 1.
DR DIP; DIP-25033N; -.
DR STRING; 6239.ZK84.6; -.
DR PaxDb; P56174; -.
DR EnsemblMetazoa; ZK84.6.1; ZK84.6.1; WBGene00002089.
DR GeneID; 191687; -.
DR KEGG; cel:CELE_ZK84.6; -.
DR UCSC; ZK84.6; c. elegans.
DR CTD; 191687; -.
DR WormBase; ZK84.6; CE15253; WBGene00002089; ins-6.
DR eggNOG; ENOG502TIU4; Eukaryota.
DR GeneTree; ENSGT00970000196018; -.
DR HOGENOM; CLU_154797_1_0_1; -.
DR InParanoid; P56174; -.
DR OMA; NLASECC; -.
DR OrthoDB; 1855388at2759; -.
DR PhylomeDB; P56174; -.
DR SignaLink; P56174; -.
DR EvolutionaryTrace; P56174; -.
DR PRO; PR:P56174; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00002089; Expressed in larva and 3 other tissues.
DR GO; GO:0005615; C:extracellular space; ISS:WormBase.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0005158; F:insulin receptor binding; IDA:WormBase.
DR GO; GO:1902075; P:cellular response to salt; IMP:UniProtKB.
DR GO; GO:0007635; P:chemosensory behavior; IMP:UniProtKB.
DR GO; GO:0040024; P:dauer larval development; IGI:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:WormBase.
DR GO; GO:1905910; P:negative regulation of dauer entry; IGI:UniProtKB.
DR GO; GO:0008355; P:olfactory learning; IMP:WormBase.
DR GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; IGI:UniProtKB.
DR InterPro; IPR036438; Insulin-like_sf.
DR InterPro; IPR022353; Insulin_CS.
DR InterPro; IPR003235; Nem_insulin-like_b-type.
DR Pfam; PF03488; Ins_beta; 1.
DR SUPFAM; SSF56994; SSF56994; 1.
DR PROSITE; PS00262; INSULIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cleavage on pair of basic residues; Disulfide bond; Hormone;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..58
FT /note="Removed; by convertase egl-3"
FT /evidence="ECO:0000269|PubMed:23665919"
FT /id="PRO_0000016224"
FT CHAIN 59..112
FT /note="Probable insulin-like peptide beta-type 5"
FT /id="PRO_0000016225"
FT DISULFID 68..97
FT /evidence="ECO:0000269|PubMed:12670864"
FT DISULFID 80..110
FT /evidence="ECO:0000269|PubMed:12670864"
FT DISULFID 84..111
FT /evidence="ECO:0000269|PubMed:12670864"
FT DISULFID 96..101
FT /evidence="ECO:0000269|PubMed:12670864"
FT MUTAGEN 57..58
FT /note="RR->AA: Loss of processing by convertase egl-3."
FT /evidence="ECO:0000269|PubMed:23665919"
FT MUTAGEN 57..58
FT /note="RR->SS: Probable loss of processing by protease bli-
FT 4. Severe reduction in Ca(2+) signal in AWC neuron and in
FT chemotaxis in response to high salt concentrations."
FT /evidence="ECO:0000269|PubMed:24013594"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:2KJI"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:2KJI"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:2KJI"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:2KJI"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:2KJI"
SQ SEQUENCE 112 AA; 12273 MW; 67EAAC5052308742 CRC64;
MNSVFTIIFV LCALQVAASF RQSFGPSMSE ESASMQLLRE LQHNMMESAH RPMPRARRVP
APGETRACGR KLISLVMAVC GDLCNPQEGK DIATECCGNQ CSDDYIRSAC CP
