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Insulin-like receptor (IR) (EC 2.7.10.1) (Abnormal dauer formation protein 2) [Cleaved into: Insulin-like receptor subunit alpha; Insulin-like receptor subunit beta]

 INSR_CAEEL              Reviewed;        1846 AA.
Q968Y9; B5QS63; O16131;
03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
03-NOV-2009, sequence version 2.
27-SEP-2017, entry version 141.
RecName: Full=Insulin-like receptor {ECO:0000250|UniProtKB:P06213};
Short=IR {ECO:0000250|UniProtKB:P06213};
EC=2.7.10.1;
AltName: Full=Abnormal dauer formation protein 2 {ECO:0000303|PubMed:9252323};
Contains:
RecName: Full=Insulin-like receptor subunit alpha {ECO:0000250|UniProtKB:P06213};
Contains:
RecName: Full=Insulin-like receptor subunit beta {ECO:0000250|UniProtKB:P06213};
Flags: Precursor;
Name=daf-2; ORFNames=Y55D5A.5;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1] {ECO:0000305, ECO:0000312|EMBL:AAC47715.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, DISRUPTION
PHENOTYPE, AND MUTAGENESIS OF CYS-401; CYS-469; PRO-470; SER-573;
ASP-648; ASP-1374; PRO-1434 AND PRO-1465.
STRAIN=Bristol N2 {ECO:0000312|EMBL:AAC47715.1};
PubMed=9252323; DOI=10.1126/science.277.5328.942;
Kimura K.D., Tissenbaum H.A., Liu Y., Ruvkun G.;
"daf-2, an insulin receptor-like gene that regulates longevity and
diapause in Caenorhabditis elegans.";
Science 277:942-946(1997).
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3] {ECO:0000305}
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PRO-1465.
PubMed=9790527; DOI=10.1016/S0092-8674(00)81751-1;
Apfeld J., Kenyon C.;
"Cell nonautonomy of C. elegans daf-2 function in the regulation of
diapause and life span.";
Cell 95:199-210(1998).
[4] {ECO:0000305}
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ALA-580 AND
PRO-1465.
PubMed=11274053; DOI=10.1101/gad.867301;
Pierce S.B., Costa M., Wisotzkey R., Devadhar S., Homburger S.A.,
Buchman A.R., Ferguson K.C., Heller J., Platt D.M., Pasquinelli A.A.,
Liu L.X., Doberstein S.K., Ruvkun G.;
"Regulation of DAF-2 receptor signaling by human insulin and ins-1, a
member of the unusually large and diverse C. elegans insulin gene
family.";
Genes Dev. 15:672-686(2001).
[5]
MUTAGENESIS OF GLY-383; ASP-1374 AND PRO-1465.
PubMed=16950159; DOI=10.1016/j.neuron.2006.07.024;
Tomioka M., Adachi T., Suzuki H., Kunitomo H., Schafer W.R., Iino Y.;
"The insulin/PI 3-kinase pathway regulates salt chemotaxis learning in
Caenorhabditis elegans.";
Neuron 51:613-625(2006).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-364; ASN-453; ASN-696;
ASN-1017 AND ASN-1078, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Bristol N2;
PubMed=17761667; DOI=10.1074/mcp.M600392-MCP200;
Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
Taoka M., Takahashi N., Isobe T.;
"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
elegans and suggests an atypical translocation mechanism for integral
membrane proteins.";
Mol. Cell. Proteomics 6:2100-2109(2007).
[7]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PRO-1465.
PubMed=18782349; DOI=10.1111/j.1474-9726.2008.00435.x;
Evans E.A., Chen W.C., Tan M.-W.;
"The DAF-2 insulin-like signaling pathway independently regulates
aging and immunity in C. elegans.";
Aging Cell 7:879-893(2008).
[8]
DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-383; GLY-547; CYS-1045;
PRO-1434 AND PRO-1465.
PubMed=18436204; DOI=10.1016/j.ydbio.2008.03.019;
Dixon S.J., Alexander M., Chan K.K., Roy P.J.;
"Insulin-like signaling negatively regulates muscle arm extension
through DAF-12 in Caenorhabditis elegans.";
Dev. Biol. 318:153-161(2008).
[9]
ENZYME REGULATION, AND INTERACTION WITH SHC-1.
PubMed=18832074; DOI=10.1101/gad.478408;
Neumann-Haefelin E., Qi W., Finkbeiner E., Walz G., Baumeister R.,
Hertweck M.;
"SHC-1/p52Shc targets the insulin/IGF-1 and JNK signaling pathways to
modulate life span and stress response in C. elegans.";
Genes Dev. 22:2721-2735(2008).
[10]
DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-146 AND PRO-1465.
PubMed=18245374; DOI=10.1534/genetics.107.070813;
Patel D.S., Garza-Garcia A., Nanji M., McElwee J.J., Ackerman D.,
Driscoll P.C., Gems D.;
"Clustering of genetically defined allele classes in the
Caenorhabditis elegans DAF-2 insulin/IGF-1 receptor.";
Genetics 178:931-946(2008).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22560223; DOI=10.1016/j.cmet.2012.04.007;
Robida-Stubbs S., Glover-Cutter K., Lamming D.W., Mizunuma M.,
Narasimhan S.D., Neumann-Haefelin E., Sabatini D.M., Blackwell T.K.;
"TOR signaling and rapamycin influence longevity by regulating SKN-
1/Nrf and DAF-16/FoxO.";
Cell Metab. 15:713-724(2012).
[12]
FUNCTION, AND MUTAGENESIS OF PRO-1465.
PubMed=22278922; DOI=10.1242/dev.074047;
Korta D.Z., Tuck S., Hubbard E.J.;
"S6K links cell fate, cell cycle and nutrient response in C. elegans
germline stem/progenitor cells.";
Development 139:859-870(2012).
[13]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PRO-1434 AND
PRO-1465.
PubMed=24332851; DOI=10.1016/j.celrep.2013.11.018;
Chen D., Li P.W., Goldstein B.A., Cai W., Thomas E.L., Chen F.,
Hubbard A.E., Melov S., Kapahi P.;
"Germline signaling mediates the synergistically prolonged longevity
produced by double mutations in daf-2 and rsks-1 in C. elegans.";
Cell Rep. 5:1600-1610(2013).
[14]
FUNCTION, INTERACTION WITH DAF-18, AND MUTAGENESIS OF PRO-1465.
PubMed=23995781; DOI=10.1038/onc.2013.347;
Liu J., Visser-Grieve S., Boudreau J., Yeung B., Lo S.,
Chamberlain G., Yu F., Sun T., Papanicolaou T., Lam A., Yang X.,
Chin-Sang I.;
"Insulin activates the insulin receptor to downregulate the PTEN
tumour suppressor.";
Oncogene 33:3878-3885(2014).
[15]
MUTAGENESIS OF PRO-1465.
PubMed=26552888; DOI=10.1242/dev.130252;
Narbonne P., Maddox P.S., Labbe J.C.;
"DAF-18/PTEN locally antagonizes insulin signalling to couple germline
stem cell proliferation to oocyte needs in C. elegans.";
Development 142:4230-4241(2015).
-!- FUNCTION: Insulin receptor-like tyrosine kinase which regulates
metabolism, controls longevity and prevents developmental arrest
at the dauer stage (PubMed:9252323, PubMed:9790527,
PubMed:24332851). Binding of INS family members may either
stimulate, or antagonize, association of the receptor with
downstream mediators such as pdk-1 and age-1 (PubMed:11274053).
Required for germline progenitor proliferation during larval
development (PubMed:22278922). Required for the response to
environmental stimuli such as food, pheromone, and temperature.
Negatively regulates resistance to UV and oxidative stress
(PubMed:24332851). Role in immune function and pathogen resistance
(PubMed:18782349). Negatively regulates autophagy
(PubMed:22560223). Regulates daf-18/PTEN protein levels
(PubMed:23995781). {ECO:0000269|PubMed:11274053,
ECO:0000269|PubMed:18782349, ECO:0000269|PubMed:22278922,
ECO:0000269|PubMed:22560223, ECO:0000269|PubMed:23995781,
ECO:0000269|PubMed:24332851, ECO:0000269|PubMed:9252323,
ECO:0000269|PubMed:9790527}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000250|UniProtKB:P06213,
ECO:0000255|PROSITE-ProRule:PRU10028}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
-!- ENZYME REGULATION: Autophosphorylation activates the kinase
activity (By similarity). Interaction with shc-1 may inhibit its
activity (PubMed:18832074). {ECO:0000250|UniProtKB:P06213,
ECO:0000269|PubMed:18832074}.
-!- SUBUNIT: Tetramer of 2 alpha and 2 beta chains linked by disulfide
bonds. The alpha chains contribute to the formation of the ligand-
binding domain, while the beta chains carry the kinase domain (By
similarity). Interacts (via cytoplasmic domain) with shc-1 (PID
domain) (PubMed:18832074). Interacts (via kinase domain) with daf-
18 (via C-terminus) (PubMed:23995781).
{ECO:0000250|UniProtKB:P06213, ECO:0000269|PubMed:18832074,
ECO:0000269|PubMed:23995781}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P06213};
Single-pass type I membrane protein
{ECO:0000250|UniProtKB:P06213}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=a {ECO:0000269|PubMed:9252323, ECO:0000269|PubMed:9851916};
IsoId=Q968Y9-1; Sequence=Displayed;
Name=b {ECO:0000269|PubMed:9851916};
IsoId=Q968Y9-2; Sequence=VSP_053157, VSP_053158;
Note=No experimental confirmation available. {ECO:0000305};
-!- DISRUPTION PHENOTYPE: Accumulation of fat, pigmented intestine,
increased lifespan, increased dauer formation and increased
resistance to pathogens. Severe loss of function mutants display
recessive early embryonic lethality (PubMed:9252323,
PubMed:9790527, PubMed:11274053, PubMed:18782349,
PubMed:18245374). RNAi-mediated knockdown in germline, hypodermis,
intestine or in muscles causes increased lifespan
(PubMed:24332851). RNAi-mediated knockdown in adults causes an
increase in lgg-1 positive autophagic vesicles (PubMed:22560223).
RNAi-mediated knockdown results in an increase in the number of
muscle arm extensions (PubMed:18436204).
{ECO:0000269|PubMed:11274053, ECO:0000269|PubMed:18245374,
ECO:0000269|PubMed:18436204, ECO:0000269|PubMed:18782349,
ECO:0000269|PubMed:22560223, ECO:0000269|PubMed:24332851,
ECO:0000269|PubMed:9252323, ECO:0000269|PubMed:9790527}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; AF012437; AAC47715.1; -; mRNA.
EMBL; FO081525; CCD72201.2; -; Genomic_DNA.
EMBL; FO081525; CCD72203.2; -; Genomic_DNA.
PIR; T42047; T42047.
RefSeq; NP_497650.4; NM_065249.4. [Q968Y9-1]
UniGene; Cel.8775; -.
ProteinModelPortal; Q968Y9; -.
BioGrid; 40655; 164.
STRING; 6239.Y55D5A.5a; -.
EPD; Q968Y9; -.
PaxDb; Q968Y9; -.
PeptideAtlas; Q968Y9; -.
EnsemblMetazoa; Y55D5A.5a; Y55D5A.5a; WBGene00000898. [Q968Y9-1]
GeneID; 175410; -.
KEGG; cel:CELE_Y55D5A.5; -.
CTD; 175410; -.
WormBase; Y55D5A.5a; CE46852; WBGene00000898; daf-2. [Q968Y9-1]
eggNOG; KOG4258; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118818; -.
HOGENOM; HOG000151241; -.
InParanoid; Q968Y9; -.
KO; K04527; -.
OrthoDB; EOG091G014Y; -.
PhylomeDB; Q968Y9; -.
Reactome; R-CEL-77387; Insulin receptor recycling.
SignaLink; Q968Y9; -.
PRO; PR:Q968Y9; -.
Proteomes; UP000001940; Chromosome III.
Bgee; WBGene00000898; -.
ExpressionAtlas; Q968Y9; baseline.
GO; GO:0030424; C:axon; IDA:WormBase.
GO; GO:0005737; C:cytoplasm; IDA:WormBase.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:WormBase.
GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
GO; GO:0097730; C:non-motile cilium; IDA:WormBase.
GO; GO:0044214; C:spanning component of plasma membrane; IDA:WormBase.
GO; GO:0005524; F:ATP binding; ISS:WormBase.
GO; GO:0005009; F:insulin-activated receptor activity; ISS:WormBase.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0017046; F:peptide hormone binding; ISS:WormBase.
GO; GO:0019901; F:protein kinase binding; IPI:WormBase.
GO; GO:0051425; F:PTB domain binding; IPI:WormBase.
GO; GO:0042169; F:SH2 domain binding; IPI:WormBase.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
GO; GO:1902075; P:cellular response to salt; IMP:UniProtKB.
GO; GO:0043053; P:dauer entry; IGI:UniProtKB.
GO; GO:0043054; P:dauer exit; IMP:WormBase.
GO; GO:0040024; P:dauer larval development; IMP:UniProtKB.
GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
GO; GO:0010286; P:heat acclimation; IMP:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0008286; P:insulin receptor signaling pathway; ISS:WormBase.
GO; GO:0030536; P:larval feeding behavior; IMP:UniProtKB.
GO; GO:1905910; P:negative regulation of dauer entry; IMP:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:0010888; P:negative regulation of lipid storage; IMP:UniProtKB.
GO; GO:1900181; P:negative regulation of protein localization to nucleus; IMP:UniProtKB.
GO; GO:0042992; P:negative regulation of transcription factor import into nucleus; IMP:WormBase.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:WormBase.
GO; GO:1900075; P:positive regulation of neuromuscular synaptic transmission; IGI:UniProtKB.
GO; GO:0045887; P:positive regulation of synaptic growth at neuromuscular junction; IGI:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISS:WormBase.
GO; GO:2000785; P:regulation of autophagosome assembly; IMP:BHF-UCL.
GO; GO:1905909; P:regulation of dauer entry; IGI:UniProtKB.
GO; GO:0061065; P:regulation of dauer larval development; IMP:UniProtKB.
GO; GO:0040034; P:regulation of development, heterochronic; IGI:WormBase.
GO; GO:1903998; P:regulation of eating behavior; IMP:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IGI:UniProtKB.
GO; GO:0010883; P:regulation of lipid storage; IGI:UniProtKB.
GO; GO:1901031; P:regulation of response to reactive oxygen species; IMP:WormBase.
GO; GO:0000003; P:reproduction; IMP:WormBase.
GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
GO; GO:0009411; P:response to UV; IMP:UniProtKB.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.40.10; -; 3.
Gene3D; 3.80.20.20; -; 2.
InterPro; IPR003961; FN3_dom.
InterPro; IPR006211; Furin-like_Cys-rich_dom.
InterPro; IPR009030; Growth_fac_rcpt_.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR032675; L_dom-like.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR000494; Rcpt_L-dom.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF00757; Furin-like; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF01030; Recep_L_domain; 2.
PRINTS; PR00109; TYRKINASE.
SMART; SM00060; FN3; 2.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF49265; SSF49265; 3.
SUPFAM; SSF52058; SSF52058; 3.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS50853; FN3; 3.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Carbohydrate metabolism;
Cleavage on pair of basic residues; Complete proteome;
Developmental protein; Disulfide bond; Glycoprotein; Immunity;
Innate immunity; Kinase; Manganese; Membrane; Metal-binding;
Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
Repeat; Signal; Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase.
SIGNAL 1 ? {ECO:0000255}.
CHAIN ? 966 Insulin-like receptor subunit alpha.
{ECO:0000255}.
/FTId=PRO_0000386619.
CHAIN 970 1846 Insulin-like receptor subunit beta.
{ECO:0000255}.
/FTId=PRO_0000386620.
TOPO_DOM 970 1183 Extracellular. {ECO:0000255}.
TRANSMEM 1184 1204 Helical. {ECO:0000255}.
TOPO_DOM 1205 1846 Cytoplasmic. {ECO:0000255}.
DOMAIN 775 869 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 969 1067 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1077 1179 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1246 1528 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 1252 1260 ATP. {ECO:0000250|UniProtKB:P28523,
ECO:0000255|PROSITE-ProRule:PRU00159}.
ACT_SITE 1388 1388 Proton acceptor.
{ECO:0000250|UniProtKB:P28523,
ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10028}.
BINDING 1282 1282 ATP. {ECO:0000250|UniProtKB:P28523,
ECO:0000255|PROSITE-ProRule:PRU00159}.
CARBOHYD 113 113 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 180 180 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 364 364 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17761667}.
CARBOHYD 453 453 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17761667}.
CARBOHYD 518 518 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 652 652 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 671 671 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 696 696 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17761667}.
CARBOHYD 1017 1017 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17761667}.
CARBOHYD 1047 1047 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1078 1078 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17761667}.
CARBOHYD 1087 1087 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1093 1093 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 371 386 {ECO:0000250|UniProtKB:P06213}.
DISULFID 393 401 {ECO:0000250|UniProtKB:P06213}.
DISULFID 397 410 {ECO:0000250|UniProtKB:P06213}.
DISULFID 413 422 {ECO:0000250|UniProtKB:P06213}.
DISULFID 426 438 {ECO:0000250|UniProtKB:P06213}.
DISULFID 469 483 {ECO:0000250|UniProtKB:P06213}.
DISULFID 486 490 {ECO:0000250|UniProtKB:P06213}.
DISULFID 615 646 {ECO:0000250|UniProtKB:P06213}.
DISULFID 706 706 Interchain.
{ECO:0000250|UniProtKB:P06213}.
VAR_SEQ 925 1020 DTMRVRRSIEDANRVSEELEKAENLGKAPKTLGGKKPLIHI
SKKKPSSSSTTSTPAPTIASMYALTRKPTTVPGTRIRLYEI
YEPLPGSWAINVSA -> CDIKNDPVGCAMLLLPPEIDDSD
VGDDDEEPGGGSEQQQRILRNSEILKRQKRQILGRSLGGIH
GIRSIGRKEYEQFADMILYGNLHDLMMSVMHD (in
isoform b). {ECO:0000303|PubMed:9851916}.
/FTId=VSP_053157.
VAR_SEQ 1021 1846 Missing (in isoform b).
{ECO:0000303|PubMed:9851916}.
/FTId=VSP_053158.
MUTAGEN 146 146 C->Y: Embronically lethal.
{ECO:0000269|PubMed:18245374}.
MUTAGEN 383 383 G->E: In m41; slight decrease in NaCl
avoidance behavior after exposure to NaCl
under starvation conditions. Normal
number of muscle membrane extensions.
{ECO:0000269|PubMed:16950159,
ECO:0000269|PubMed:18436204}.
MUTAGEN 401 401 C->Y: Dauer formation; when associated
with L-470. {ECO:0000269|PubMed:9252323}.
MUTAGEN 469 469 C->S: Dauer formation above 20 degrees
Celsius. {ECO:0000269|PubMed:9252323}.
MUTAGEN 470 470 P->L: Dauer formation; when associated
with Y-401. {ECO:0000269|PubMed:9252323}.
MUTAGEN 547 547 G->S: In m596; increases the number of
muscle membrane extensions during larval
development.
{ECO:0000269|PubMed:18436204}.
MUTAGEN 573 573 S->L: Dauer formation above 25 degrees
Celsius. {ECO:0000269|PubMed:9252323}.
MUTAGEN 580 580 A->T: Dauer formation above 26 degrees
Celsius. {ECO:0000269|PubMed:11274053}.
MUTAGEN 648 648 D->N: Dauer formation above 25 degrees
Celsius. {ECO:0000269|PubMed:9252323}.
MUTAGEN 1045 1045 C->Y: In m577; normal number of muscle
membrane extensions.
{ECO:0000269|PubMed:18436204}.
MUTAGEN 1374 1374 D->N: In sa219; dauer formation above 20
degrees Celsius. Normal NaCl avoidance
behavior after exposure to NaCl under
starvation conditions.
{ECO:0000269|PubMed:16950159,
ECO:0000269|PubMed:9252323}.
MUTAGEN 1434 1434 P->L: In e1391; dauer formation above 20
degrees Celsius and increased lifespan.
Increases the number of muscle membrane
extensions during larval development.
{ECO:0000269|PubMed:18436204,
ECO:0000269|PubMed:24332851,
ECO:0000269|PubMed:9252323}.
MUTAGEN 1465 1465 P->S: In e1370; extended lifespan.
Accumulates fat and undergoes dauer
formation above 25 degrees Celsius.
Pigmented intestine and increased
resistance to bacterial pathogens, UV,
high temperature and paraquat treatment.
Reduced number of germline progenitors
during larval development and
proliferation of germline stem cells.
Fails to avoid NaCl after exposure to
NaCl under starvation conditions.
Increases the number of muscle membrane
extensions during larval development.
Overextension of PML neuron axons.
{ECO:0000269|PubMed:11274053,
ECO:0000269|PubMed:16950159,
ECO:0000269|PubMed:18245374,
ECO:0000269|PubMed:18436204,
ECO:0000269|PubMed:18782349,
ECO:0000269|PubMed:22278922,
ECO:0000269|PubMed:23995781,
ECO:0000269|PubMed:24332851,
ECO:0000269|PubMed:26552888,
ECO:0000269|PubMed:9252323,
ECO:0000269|PubMed:9790527}.
CONFLICT 838 838 H -> R (in Ref. 1; AAC47715).
{ECO:0000305}.
CONFLICT 1313 1313 K -> Q (in Ref. 1; AAC47715).
{ECO:0000305}.
SEQUENCE 1846 AA; 207124 MW; 230B28322FF0F126 CRC64;
MTRMNIVRCR RRHKILENLE EENLGPSCSS TTSTTAATEA LGTTTEDMRL KQQRSSSRAT
EHDIVDGNHH DDEHITMRRL RLVKNSRTRR RTTPDSSMDC YEENPPSQKT SINYSWISKK
SSMTSLMLLL LFAFVQPCAS IVEKRCGPID IRNRPWDIKP QWSKLGDPNE KDLAGQRMVN
CTVVEGSLTI SFVLKHKTKA QEEMHRSLQP RYSQDEFITF PHLREITGTL LVFETEGLVD
LRKIFPNLRV IGGRSLIQHY ALIIYRNPDL EIGLDKLSVI RNGGVRIIDN RKLCYTKTID
WKHLITSSIN DVVVDNAAEY AVTETGLMCP RGACEEDKGE SKCHYLEEKN QEQGVERVQS
CWSNTTCQKS CAYDRLLPTK EIGPGCDANG DRCHDQCVGG CERVNDATAC HACKNVYHKG
KCIEKCDAHL YLLLQRRCVT REQCLQLNPV LSNKTVPIKA TAGLCSDKCP DGYQINPDDH
RECRKCVGKC EIVCEINHVI DTFPKAQAIR LCNIIDGNLT IEIRGKQDSG MASELKDIFA
NIHTITGYLL VRQSSPFISL NMFRNLRRIE AKSLFRNLYA ITVFENPNLK KLFDSTTDLT
LDRGTVSIAN NKMLCFKYIK QLMSKLNIPL DPIDQSEGTN GEKAICEDMA INVSITAVNA
DSVFFSWPSF NITDIDQRKF LGYELFFKEV PRIDENMTIE EDRSACVDSW QSVFKQYYET
SNGEPTPDIF MDIGPRERIR PNTLYAYYVA TQMVLHAGAK NGVSKIGFVR TSYYTPDPPT
LALAQVDSDA IHITWEAPLQ PNGDLTHYTI MWRENEVSPY EEAEKFCTDA STPANRQHTK
DPKETIVADK PVDIPSSRTV APTLLTMMGH EDQQKTCAAT PGCCSCSAIE ESSEQNKKKR
PDPMSAIESS AFENKLLDEV LMPRDTMRVR RSIEDANRVS EELEKAENLG KAPKTLGGKK
PLIHISKKKP SSSSTTSTPA PTIASMYALT RKPTTVPGTR IRLYEIYEPL PGSWAINVSA
LALDNSYVIR NLKHYTLYAI SLSACQNMTV PGASCSISHR AGALKRTKHI TDIDKVLNET
IEWRFMNNSQ QVNVTWDPPT EVNGGIFGYV VKLKSKVDGS IVMTRCVGAK RGYSTRNQGV
LFQNLADGRY FVSVTATSVH GAGPEAESSD PIVVMTPGFF TVEIILGMLL VFLILMSIAG
CIIYYYIQVR YGKKVKALSD FMQLNPEYCV DNKYNADDWE LRQDDVVLGQ QCGEGSFGKV
YLGTGNNVVS LMGDRFGPCA IKINVDDPAS TENLNYLMEA NIMKNFKTNF IVKLYGVIST
VQPAMVVMEM MDLGNLRDYL RSKREDEVFN ETDCNFFDII PRDKFHEWAA QICDGMAYLE
SLKFCHRDLA ARNCMINRDE TVKIGDFGMA RDLFYHDYYK PSGKRMMPVR WMSPESLKDG
KFDSKSDVWS FGVVLYEMVT LGAQPYIGLS NDEVLNYIGM ARKVIKKPEC CENYWYKVMK
MCWRYSPRDR PTFLQLVHLL AAEASPEFRD LSFVLTDNQM ILDDSEALDL DDIDDTDMND
QVVEVAPDVE NVEVQSDSER RNTDSIPLKQ FKTIPPINAT TSHSTISIDE TPMKAKQREG
SLDEEYALMN HSGGPSDAEV RTYAGDGDYV ERDVRENDVP TRRNTGASTS SYTGGGPYCL
TNRGGSNERG AGFGEAVRLT DGVGSGHLND DDYVEKEISS MDTRRSTGAS SSSYGVPQTN
WSGNRGATYY TSKAQQAATA AAAAAAALQQ QQNGGRGDRL TQLPGTGHLQ STRGGQDGDY
IETEPKNYRN NGSPSRNGNS RDIFNGRSAF GENEHLIEDN EHHPLV


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