ILB4_CAEEL
ID ILB4_CAEEL Reviewed; 105 AA.
AC Q23430;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Insulin-like peptide 7 {ECO:0000305};
DE AltName: Full=Insulin-like peptide beta-type 4 {ECO:0000305};
DE Flags: Precursor;
GN Name=ins-7 {ECO:0000312|WormBase:ZK1251.2a};
GN ORFNames=ZK1251.2 {ECO:0000312|WormBase:ZK1251.2a};
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, AND DISRUPTION PHENOTYPE.
RX PubMed=32366357; DOI=10.7554/elife.53757;
RA Borbolis F., Rallis J., Kanatouris G., Kokla N., Karamalegkos A.,
RA Vasileiou C., Vakaloglou K.M., Diallinas G., Stravopodis D.J., Zervas C.G.,
RA Syntichaki P.;
RT "mRNA decapping is an evolutionarily conserved modulator of neuroendocrine
RT signaling that controls development and ageing.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Insulin-like peptide which plays a role in ageing as a
CC consequence of daf-16 activity. {ECO:0000269|PubMed:32366357}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:32366357}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown extends lifespan.
CC {ECO:0000269|PubMed:32366357}.
CC -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR EMBL; BX284604; CAA92498.1; -; Genomic_DNA.
DR PIR; T27719; T27719.
DR RefSeq; NP_001255418.1; NM_001268489.1.
DR AlphaFoldDB; Q23430; -.
DR SMR; Q23430; -.
DR STRING; 6239.ZK1251.2b; -.
DR PaxDb; Q23430; -.
DR EnsemblMetazoa; ZK1251.2a.1; ZK1251.2a.1; WBGene00002090.
DR GeneID; 191688; -.
DR UCSC; ZK1251.2; c. elegans.
DR CTD; 191688; -.
DR WormBase; ZK1251.2a; CE03849; WBGene00002090; ins-7.
DR eggNOG; ENOG502TK5N; Eukaryota.
DR GeneTree; ENSGT00970000196994; -.
DR HOGENOM; CLU_154797_0_0_1; -.
DR PhylomeDB; Q23430; -.
DR PRO; PR:Q23430; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00002090; Expressed in adult organism and 1 other tissue.
DR ExpressionAtlas; Q23430; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR GO; GO:0008355; P:olfactory learning; IGI:WormBase.
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 3: Inferred from homology;
KW Cleavage on pair of basic residues; Disulfide bond; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..57
FT /evidence="ECO:0000255"
FT /id="PRO_0000016222"
FT CHAIN 58..105
FT /note="Insulin-like peptide 7"
FT /id="PRO_0000016223"
FT DISULFID 61..90
FT /evidence="ECO:0000255"
FT DISULFID 73..103
FT /evidence="ECO:0000255"
FT DISULFID 77..104
FT /evidence="ECO:0000255"
FT DISULFID 89..94
FT /evidence="ECO:0000255"
SQ SEQUENCE 105 AA; 12198 MW; EB4000DDB7732969 CRC64;
MPPIILVFFL VLIPASQQYP FSLESLNDQI INEEVIEYML ENSIRSSRTR RVPDEKKIYR
CGRRIHSYVF AVCGKACESN TEVNIASKCC REECTDDFIR KQCCP
