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Insulin receptor (IR) (EC 2.7.10.1) (CD antigen CD220) [Cleaved into: Insulin receptor subunit alpha; Insulin receptor subunit beta]

 INSR_RAT                Reviewed;        1383 AA.
P15127; P97681;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
25-OCT-2017, entry version 177.
RecName: Full=Insulin receptor;
Short=IR;
EC=2.7.10.1;
AltName: CD_antigen=CD220;
Contains:
RecName: Full=Insulin receptor subunit alpha;
Contains:
RecName: Full=Insulin receptor subunit beta;
Flags: Precursor;
Name=Insr;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND ALTERNATIVE SPLICING
(ISOFORM SHORT).
PubMed=2330003; DOI=10.1210/mend-4-2-235;
Goldstein B.J., Dudley A.L.;
"The rat insulin receptor: primary structure and conservation of
tissue-specific alternative messenger RNA splicing.";
Mol. Endocrinol. 4:235-244(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 731-756; 758-819; 969-994 AND
1119-1177.
STRAIN=Sprague-Dawley;
Liu Y., Tam J.W.O.;
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
[3]
INTERACTION WITH GRB7.
PubMed=10803466; DOI=10.1038/sj.onc.1203469;
Kasus-Jacobi A., Bereziat V., Perdereau D., Girard J., Burnol A.F.;
"Evidence for an interaction between the insulin receptor and Grb7. A
role for two of its binding domains, PIR and SH2.";
Oncogene 19:2052-2059(2000).
[4]
FUNCTION, AND FORMATION OF A HYBRID RECEPTOR WITH IGF1R.
PubMed=16803852; DOI=10.1152/ajpendo.00565.2005;
Johansson G.S., Arnqvist H.J.;
"Insulin and IGF-I action on insulin receptors, IGF-I receptors, and
hybrid insulin/IGF-I receptors in vascular smooth muscle cells.";
Am. J. Physiol. 291:E1124-E1130(2006).
[5]
INTERACTION WITH CAV2.
PubMed=19778377; DOI=10.1111/j.1582-4934.2009.00391.x;
Kwon H., Jeong K., Pak Y.;
"Identification of pY19-caveolin-2 as a positive regulator of insulin-
stimulated actin cytoskeleton-dependent mitogenesis.";
J. Cell. Mol. Med. 13:1549-1564(2009).
[6]
INTERACTION WITH ATIC.
PubMed=25687571; DOI=10.1074/mcp.M114.047159;
Boutchueng-Djidjou M., Collard-Simard G., Fortier S., Hebert S.S.,
Kelly I., Landry C.R., Faure R.L.;
"The last enzyme of the de novo purine synthesis pathway 5-
aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP
cyclohydrolase (ATIC) plays a central role in insulin signaling and
the Golgi/endosomes protein network.";
Mol. Cell. Proteomics 14:1079-1092(2015).
-!- FUNCTION: Receptor tyrosine kinase which mediates the pleiotropic
actions of insulin. Binding of insulin leads to phosphorylation of
several intracellular substrates, including, insulin receptor
substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling
intermediates. Each of these phosphorylated proteins serve as
docking proteins for other signaling proteins that contain Src-
homology-2 domains (SH2 domain) that specifically recognize
different phosphotyrosine residues, including the p85 regulatory
subunit of PI3K and SHP2. Phosphorylation of IRSs proteins lead to
the activation of two main signaling pathways: the PI3K-AKT/PKB
pathway, which is responsible for most of the metabolic actions of
insulin, and the Ras-MAPK pathway, which regulates expression of
some genes and cooperates with the PI3K pathway to control cell
growth and differentiation. Binding of the SH2 domains of PI3K to
phosphotyrosines on IRS1 leads to the activation of PI3K and the
generation of phosphatidylinositol-(3, 4, 5)-triphosphate (PIP3),
a lipid second messenger, which activates several PIP3-dependent
serine/threonine kinases, such as PDPK1 and subsequently AKT/PKB.
The net effect of this pathway is to produce a translocation of
the glucose transporter SLC2A4/GLUT4 from cytoplasmic vesicles to
the cell membrane to facilitate glucose transport. Moreover, upon
insulin stimulation, activated AKT/PKB is responsible for: anti-
apoptotic effect of insulin by inducing phosphorylation of BAD;
regulates the expression of gluconeogenic and lipogenic enzymes by
controlling the activity of the winged helix or forkhead (FOX)
class of transcription factors. Another pathway regulated by PI3K-
AKT/PKB activation is mTORC1 signaling pathway which regulates
cell growth and metabolism and integrates signals from insulin.
AKT mediates insulin-stimulated protein synthesis by
phosphorylating TSC2 thereby activating mTORC1 pathway. The
Ras/RAF/MAP2K/MAPK pathway is mainly involved in mediating cell
growth, survival and cellular differentiation of insulin.
Phosphorylated IRS1 recruits GRB2/SOS complex, which triggers the
activation of the Ras/RAF/MAP2K/MAPK pathway. In addition to
binding insulin, the insulin receptor can bind insulin-like growth
factors (IGFI and IGFII). When present in a hybrid receptor with
IGF1R, binds IGF1 (By similarity). {ECO:0000250,
ECO:0000269|PubMed:16803852}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME REGULATION: Activated in response to insulin.
Autophosphorylation activates the kinase activity. PTPN1, PTPRE
and PTPRF dephosphorylate important tyrosine residues, thereby
reducing INSR activity. Inhibited by ENPP1. GRB10 and GRB14
inhibit the catalytic activity of the INSR, they block access of
substrates to the activated receptor. SOCS1 and SOCS3 act as
negative regulators of INSR activity, they bind to the activated
INRS and interfere with the phosphorylation of INSR substrates (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Tetramer of 2 alpha and 2 beta chains linked by disulfide
bonds. The alpha chains carry the insulin-binding regions, while
the beta chains carry the kinase domain. Forms a hybrid receptor
with IGF1R, the hybrid is a tetramer consisting of 1 alpha chain
and 1 beta chain of INSR and 1 alpha chain and 1 beta chain of
IGF1R. Interacts with SORBS1 but dissociates from it following
insulin stimulation. Binds SH2B2. Activated form of INSR interacts
(via Tyr-1000) with the PTB/PID domains of IRS1 and SHC1. The
sequences surrounding the phosphorylated NPXY motif contribute
differentially to either IRS1 or SHC1 recognition. Interacts (via
tyrosines in the C-terminus) with IRS2 (via PTB domain and 591-786
AA); the 591-786 would be the primary anchor of IRS2 to INSR while
the PTB domain would have a stabilizing action on the interaction
with INSR. Interacts with the SH2 domains of the 85 kDa regulatory
subunit of PI3K (PIK3R1) in vitro, when autophosphorylated on
tyrosine residues. Interacts with SOCS7. Interacts (via the
phosphorylated Tyr-1000), with SOCS3. Interacts (via the
phosphorylated Tyr-1186, Tyr-1190, Tyr-1191) with SOCS1. Interacts
with ARRB2 (By similarity). Interacts with GRB10; this interaction
blocks the association between IRS1/IRS2 and INSR, significantly
reduces insulin-stimulated tyrosine phosphorylation of IRS1 and
IRS2 and thus decreases insulin signaling. Interacts with PDPK1.
Interacts (via Tyr-1191) with GRB14 (via BPS domain); this
interaction protects the tyrosines in the activation loop from
dephosphorylation, but promotes dephosphorylation of Tyr-1000,
this results in decreased interaction with, and phosphorylation
of, IRS1. Interacts (via subunit alpha) with ENPP1 (via 485-599
AA); this interaction blocks autophosphorylation. Interacts with
PTPRE; this interaction is dependent of Tyr-1186, Tyr-1190 and
Tyr-1191 of the INSR. Interacts with STAT5B (via SH2 domain).
Interacts with PTPRF (By similarity). Interacts with GRB7.
Interacts with CAV2 (tyrosine-phosphorylated form); the
interaction is increased with 'Tyr-27'phosphorylation of CAV2.
Interacts with ATIC; ATIC together with PRKAA2/AMPK2 and
HACD3/PTPLAD1 is proposed to be part of a signaling netwok
regulating INSR autophosphorylation and endocytosis
(PubMed:25687571). {ECO:0000250, ECO:0000269|PubMed:10803466,
ECO:0000269|PubMed:19778377, ECO:0000269|PubMed:25687571}.
-!- INTERACTION:
O35567:Atic; NbExp=3; IntAct=EBI-10768746, EBI-10768817;
Q62689:Jak2; NbExp=2; IntAct=EBI-7472166, EBI-8656708;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long; Synonyms=RIR-B;
IsoId=P15127-1; Sequence=Displayed;
Name=Short; Synonyms=RIR-A;
IsoId=P15127-2; Sequence=VSP_036680;
-!- DOMAIN: The tetrameric insulin receptor binds insulin via non-
identical regions from two alpha chains, primarily via the C-
terminal region of the first INSR alpha chain. Residues from the
leucine-rich N-terminus of the other INSR alpha chain also
contribute to this insulin binding site. A secondary insulin-
binding site is formed by residues at the junction of fibronectin
type-III domain 1 and 2 (By similarity). {ECO:0000250}.
-!- PTM: Autophosphorylated on tyrosine residues in response to
insulin. Phosphorylation of Tyr-1000 is required for binding to
IRS1, SHC1, and STAT5B. Dephosphorylated by PTPRE on Tyr-1000,
Tyr-1186, Tyr-1190 and Tyr-1191 residues. Dephosphorylated by
PTPRF and PTPN1. Dephosphorylated by PTPN2; down-regulates
insulin-induced signaling. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; M29014; AAA41441.1; -; mRNA.
EMBL; AF005776; AAB61414.1; -; Genomic_DNA.
EMBL; AF005777; AAB61415.1; -; Genomic_DNA.
EMBL; AH004882; AAB38967.1; -; Genomic_DNA.
EMBL; AH004883; AAB38968.1; -; Genomic_DNA.
EMBL; U80633; AAB38746.1; -; Genomic_DNA.
PIR; A36080; A36080.
UniGene; Rn.9876; -.
PDB; 4XST; X-ray; 3.00 A; F=726-748.
PDB; 5TQ1; X-ray; 1.49 A; B=1008-1018.
PDBsum; 4XST; -.
PDBsum; 5TQ1; -.
ProteinModelPortal; P15127; -.
SMR; P15127; -.
DIP; DIP-42209N; -.
IntAct; P15127; 11.
MINT; MINT-1348005; -.
STRING; 10116.ENSRNOP00000060141; -.
BindingDB; P15127; -.
ChEMBL; CHEMBL5486; -.
iPTMnet; P15127; -.
PhosphoSitePlus; P15127; -.
UniCarbKB; P15127; -.
PaxDb; P15127; -.
PeptideAtlas; P15127; -.
PRIDE; P15127; -.
UCSC; RGD:2917; rat. [P15127-1]
RGD; 2917; Insr.
eggNOG; KOG4258; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000038045; -.
HOVERGEN; HBG006134; -.
InParanoid; P15127; -.
PhylomeDB; P15127; -.
BRENDA; 2.7.10.1; 5301.
PRO; PR:P15127; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0032590; C:dendrite membrane; IDA:ARUK-UCL.
GO; GO:0005768; C:endosome; IDA:RGD.
GO; GO:0009897; C:external side of plasma membrane; IDA:ARUK-UCL.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IDA:ARUK-UCL.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0032809; C:neuronal cell body membrane; IDA:ARUK-UCL.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0045202; C:synapse; IDA:RGD.
GO; GO:0043423; F:3-phosphoinositide-dependent protein kinase binding; IDA:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0043559; F:insulin binding; IDA:RGD.
GO; GO:0043560; F:insulin receptor substrate binding; IMP:RGD.
GO; GO:0005009; F:insulin-activated receptor activity; IDA:RGD.
GO; GO:0031405; F:lipoic acid binding; IPI:RGD.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:InterPro.
GO; GO:0032403; F:protein complex binding; IDA:RGD.
GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
GO; GO:0004672; F:protein kinase activity; IDA:RGD.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0019903; F:protein phosphatase binding; IMP:RGD.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:RGD.
GO; GO:0097242; P:amyloid-beta clearance; IMP:ARUK-UCL.
GO; GO:0021549; P:cerebellum development; IEP:RGD.
GO; GO:0097062; P:dendritic spine maintenance; IGI:ARUK-UCL.
GO; GO:0045444; P:fat cell differentiation; IEP:RGD.
GO; GO:0042593; P:glucose homeostasis; IDA:RGD.
GO; GO:0021766; P:hippocampus development; IEP:RGD.
GO; GO:0008286; P:insulin receptor signaling pathway; IDA:RGD.
GO; GO:0010629; P:negative regulation of gene expression; IMP:RGD.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:RGD.
GO; GO:0032410; P:negative regulation of transporter activity; IMP:RGD.
GO; GO:1990535; P:neuron projection maintenance; IGI:ARUK-UCL.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IMP:RGD.
GO; GO:0010560; P:positive regulation of glycoprotein biosynthetic process; IMP:RGD.
GO; GO:0042327; P:positive regulation of phosphorylation; IDA:BHF-UCL.
GO; GO:0043243; P:positive regulation of protein complex disassembly; IGI:ARUK-UCL.
GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
GO; GO:0051290; P:protein heterotetramerization; IDA:RGD.
GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; IDA:RGD.
GO; GO:0014823; P:response to activity; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
GO; GO:0009749; P:response to glucose; IEP:BHF-UCL.
GO; GO:0009725; P:response to hormone; IEP:RGD.
GO; GO:0032868; P:response to insulin; IEP:BHF-UCL.
GO; GO:0010042; P:response to manganese ion; IEP:RGD.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
GO; GO:0033574; P:response to testosterone; IEP:RGD.
GO; GO:0034612; P:response to tumor necrosis factor; IMP:RGD.
GO; GO:0033280; P:response to vitamin D; IEP:RGD.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.40.10; -; 3.
Gene3D; 3.80.20.20; -; 3.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR006211; Furin-like_Cys-rich_dom.
InterPro; IPR006212; Furin_repeat.
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; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR000494; Rcpt_L-dom.
InterPro; IPR036941; Rcpt_L-dom_sf.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016246; Tyr_kinase_insulin-like_rcpt.
InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
Pfam; PF00041; fn3; 1.
Pfam; PF00757; Furin-like; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF01030; Recep_L_domain; 2.
PIRSF; PIRSF000620; Insulin_receptor; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00060; FN3; 3.
SMART; SM00261; FU; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF49265; SSF49265; 4.
SUPFAM; SSF52058; SSF52058; 2.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS50853; FN3; 3.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell membrane;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
Glycoprotein; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
Receptor; Reference proteome; Repeat; Signal; Transferase;
Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
SIGNAL 1 26
CHAIN 27 759 Insulin receptor subunit alpha.
/FTId=PRO_0000016696.
CHAIN 764 1383 Insulin receptor subunit beta.
/FTId=PRO_0000016698.
TOPO_DOM 27 759 Extracellular. {ECO:0000305}.
TOPO_DOM 764 957 Extracellular. {ECO:0000305}.
TRANSMEM 958 978 Helical. {ECO:0000255}.
TOPO_DOM 979 1383 Cytoplasmic. {ECO:0000305}.
DOMAIN 625 727 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 754 848 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 854 948 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1024 1299 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 1105 1111 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 1164 1165 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 734 742 Insulin-binding. {ECO:0000250}.
REGION 997 1000 Important for interaction with IRS1, SHC1
and STAT5B.
REGION 1362 1365 PIK3R1 binding. {ECO:0000250}.
COMPBIAS 27 173 Leu-rich.
ACT_SITE 1160 1160 Proton donor/acceptor. {ECO:0000250}.
BINDING 1034 1034 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 1058 1058 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 1178 1178 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 65 65 Insulin-binding. {ECO:0000250}.
MOD_RES 399 399 Phosphoserine.
{ECO:0000250|UniProtKB:P06213}.
MOD_RES 400 400 Phosphotyrosine.
{ECO:0000250|UniProtKB:P06213}.
MOD_RES 406 406 Phosphoserine.
{ECO:0000250|UniProtKB:P06213}.
MOD_RES 1000 1000 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 1186 1186 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P06213}.
MOD_RES 1190 1190 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P06213}.
MOD_RES 1191 1191 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P06213}.
MOD_RES 1356 1356 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 1362 1362 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
CARBOHYD 42 42 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 51 51 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 137 137 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 241 241 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 281 281 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 321 321 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 363 363 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 423 423 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 444 444 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 540 540 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 634 634 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 652 652 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 699 699 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 770 770 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 783 783 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 921 921 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 934 934 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 34 52 {ECO:0000250}.
DISULFID 152 181 {ECO:0000250}.
DISULFID 185 208 {ECO:0000250}.
DISULFID 195 214 {ECO:0000250}.
DISULFID 218 227 {ECO:0000250}.
DISULFID 222 233 {ECO:0000250}.
DISULFID 234 242 {ECO:0000250}.
DISULFID 238 251 {ECO:0000250}.
DISULFID 254 263 {ECO:0000250}.
DISULFID 267 279 {ECO:0000250}.
DISULFID 285 310 {ECO:0000250}.
DISULFID 292 300 {ECO:0000250}.
DISULFID 314 327 {ECO:0000250}.
DISULFID 330 334 {ECO:0000250}.
DISULFID 338 359 {ECO:0000250}.
DISULFID 461 494 {ECO:0000250}.
DISULFID 550 550 Interchain. {ECO:0000250}.
DISULFID 675 900 {ECO:0000250}.
VAR_SEQ 746 757 Missing (in isoform Short).
{ECO:0000305}.
/FTId=VSP_036680.
HELIX 727 736 {ECO:0000244|PDB:4XST}.
SEQUENCE 1383 AA; 156757 MW; 4B919566902A944A CRC64;
MGSGRGCETT AVPLLMAVAV AGGTAGHLYP GEVCPGMDIR NNLTRLHELE NCSVIEGHLQ
ILLMFKTRPE DFRDLSFPKL IMITDYLLLF RVYGLESLKD LFPNLTVIRG SRLFFNYALV
IFEMVHLKEL GLYNLMNITR GSVRIEKNNE LCYLATIDWS RILDYVEDNY IVLNKDDNEE
CGDVCPGTAK GKTNCPATVI NGQFVERCWT HSHCQKVCPT ICKSHGCTAE GLCCHKECLG
NCSEPDDPTK CVACRNFYLD GQCVETCPPP YYHFQDWRCV NFSFCQDLHY KCRNSRKPGC
HQYVIHNNKC IPECPSGYTM NSSNLMCTPC LGPCPKVCQI LEGEKTIDSV TSAQELRGCT
VINGSLIINI RGGNNLAAEL EANLGLIEEI SGFLKIRRSY ALVSLSFFRK LHLIRGETLE
IGNYSFYALD NQNLRQLWDW NKHNLTITQG KLFFHYNPKL CLSEIHKMEE VSGTKGRQER
NDIALKTNGD QASCENELLK FSFIRTSFDK ILLRWEPYWP PDFRDLLGFM LFYKEAPYQN
VTEFDGQDAC GSNSWTVVDI DPPQRSNDPK SQTPSHPGWL MRGLKPWTQY AIFVKTLVTF
SDERRTYGAK SDIIYVQTDA TNPSVPLDPI SVSNSSSQII LKWKPPSDPN GNITHYLVYW
ERQAEDSELF ELDYCLKGLK LPSRTWSPPF ESDDSQKHNQ SEYDDSASEC CSCPKTDSQI
LKELEESSFR KTFEDYLHNV VFVPRKTSSG NGAEDTRPSR KRRSLEEVGN VTATTPTLPD
FPNISSTIAP TSHEEHRPFE KVVNKESLVI SGLRHFTGYR IELQACNQDS PEERSGVAAY
VSARTMPEAK ADDIVGPVTH EIFENNVVHL MWQEPKEPNG LIVLYEVSYR RYGDEELHLC
VSRKHFALER GCRLRGLSPG NYSVRVRATS LAGNGSWTEP TYFYVTDYLD VPSNIAKIII
GPLIFVFLFS VVIGSIYLFL RKRQPDGPMG PLYASSNPEY LSASDVFPSS VYVPDEWEVP
REKITLLREL GQGSFGMVYE GNAKDIIKGE VETRVAVKTV NESASLRERI EFLNEASVMK
GFTCHHVVRL LGVVSKGQPT LVVMELMAHG DLKSHLRSLR PDAENNPGRP PPTLQEMIQM
TAEIADGMAY LNAKKFVHRD LAARNCMVAH DFTVKIGDFG MTRDIYETDY YRKGGKGLLP
VRWMSPESLK DGVFTASSDM WSFGVVLWEI TSLAEQPYQG LSNEQVLKFV MDGGYLDPPD
NCPERLTDLM RMCWQFNPKM RPTFLEIVNL LKDDLHPSFP EVSFFYSEEN KAPESEELEM
EFEDMENVPL DRSSHCQREE AGCREGGSSL SIKRTYDEHI PYTHMNGGKK NGRVLTLPRS
NPS


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