ID   ILB1_CAEEL              Reviewed;         106 AA.
AC   Q09626;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Probable insulin-like peptide beta-type 1;
DE   Flags: Precursor;
GN   Name=ins-4; ORFNames=ZK75.1;
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   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 50-ARG-ARG-51.
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, 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).
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).
CC       {ECO:0000269|PubMed:23665919, ECO:0000269|PubMed:24671950}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by ASI and ASJ sensory neurons and weakly
CC       by ventral cord motor neurons. {ECO:0000269|PubMed:24671950}.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; FO080104; CCD61234.1; -; Genomic_DNA.
DR   PIR; T27989; T27989.
DR   RefSeq; NP_495196.1; NM_062795.1.
DR   AlphaFoldDB; Q09626; -.
DR   SMR; Q09626; -.
DR   STRING; 6239.ZK75.1; -.
DR   PaxDb; Q09626; -.
DR   EnsemblMetazoa; ZK75.1.1; ZK75.1.1; WBGene00002087.
DR   GeneID; 191685; -.
DR   KEGG; cel:CELE_ZK75.1; -.
DR   UCSC; ZK75.1; c. elegans.
DR   CTD; 191685; -.
DR   WormBase; ZK75.1; CE02100; WBGene00002087; ins-4.
DR   eggNOG; ENOG502TIU4; Eukaryota.
DR   GeneTree; ENSGT00970000196018; -.
DR   HOGENOM; CLU_154797_1_0_1; -.
DR   InParanoid; Q09626; -.
DR   OMA; IATHCCA; -.
DR   PhylomeDB; Q09626; -.
DR   SignaLink; Q09626; -.
DR   PRO; PR:Q09626; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00002087; Expressed in adult organism and 2 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0040024; P:dauer larval development; IGI:UniProtKB.
DR   GO; GO:1905910; P:negative regulation of dauer entry; IGI:UniProtKB.
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   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..51
FT                   /note="Removed; by convertase egl-3"
FT                   /evidence="ECO:0000269|PubMed:23665919"
FT                   /id="PRO_0000016216"
FT   CHAIN           52..106
FT                   /note="Probable insulin-like peptide beta-type 1"
FT                   /id="PRO_0000016217"
FT   DISULFID        60..89
FT                   /evidence="ECO:0000255"
FT   DISULFID        72..102
FT                   /evidence="ECO:0000255"
FT   DISULFID        76..103
FT                   /evidence="ECO:0000255"
FT   DISULFID        88..93
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         50..51
FT                   /note="RR->AA: Loss of processing by convertase egl-3."
FT                   /evidence="ECO:0000269|PubMed:23665919"
SQ   SEQUENCE   106 AA;  11997 MW;  61D7459390674717 CRC64;
     MFSFFTYFLL SALLLSASCR QPSMDTSKAD RILREIEMET ELENQLSRAR RVPAGEVRAC
     GRRLLLFVWS TCGEPCTPQE DMDIATVCCT TQCTPSYIKQ ACCPEK