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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
 
 
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