O73798 · IGF1R_XENLA
- ProteinInsulin-like growth factor 1 receptor
- Geneigf1r
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1358 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
This receptor binds insulin-like growth factor 1 (IGF1) with a high affinity and IGF2 with a lower affinity. It has a tyrosine-protein kinase activity, which is necessary for the activation of the IGF1-stimulated downstream signaling cascade. Plays a role in oocyte maturation. Promotes head development by inhibiting Wnt signaling during embryogenesis.
Catalytic activity
- ATP + L-tyrosyl-[protein] = ADP + H+ + O-phospho-L-tyrosyl-[protein]
Cofactor
Activity regulation
Autophosphorylation activates the kinase activity.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | insulin receptor substrate binding | |
Molecular Function | insulin-like growth factor binding | |
Molecular Function | insulin-like growth factor receptor activity | |
Molecular Function | metal ion binding | |
Molecular Function | phosphatidylinositol 3-kinase binding | |
Molecular Function | protein tyrosine kinase activity | |
Molecular Function | structural molecule activity | |
Biological Process | insulin-like growth factor receptor signaling pathway | |
Biological Process | oocyte maturation | |
Biological Process | protein autophosphorylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameInsulin-like growth factor 1 receptor
- EC number
- Short namesxIGF-1R; xIGFR
- Cleaved into 2 chains
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus
Accessions
- Primary accessionO73798
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Note: Expressed at the oocyte surface.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 735-934 | Extracellular | ||||
Sequence: DVLAVGNSTVTSYEKNSTTEDFSNFSDSERDDIEYPFYETKVDYKWERTVISNLQPFTLYRIDIHSCNHEAEKLGCSASNFVFARTMPAAGADDIPGIVNTKEEDDGVIFLGWPEPLRPNGLILMYEIEYKHQGEVHRECVSRQDYRKNGGIKLVRLPPGNYSAQVQAISLYGNGSWTEMVSFCVKLKPDVRNNILQMVV | ||||||
Transmembrane | 935-955 | Helical | ||||
Sequence: AIPLALSFLLVGIISIVCFVF | ||||||
Topological domain | 956-1358 | Cytoplasmic | ||||
Sequence: KKRNSNRLGNGVLYASVNPEYFSAAEMYVPDKWEVPREKITMNRELGQGSFGMVYEGIAKGVVKDEAETKVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMTRGDLKSYLRSLRPDTESNSGQPTPSLKKMIQMAGEIADGMSYLNANKFVHRDLAARNCMVTEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTNSDVWSFGVVLWEIATLAEQPYQGMSNEQVLRFVMEGGLLEKPDNCPDMLFELMRMCWQFNPKMRPSFLEIISSIKDELDPGFKEVSFFYSEENKPPDTEELDLEAENMESIPLDPSCALQNSEHHAGHKSENGPGVVVLRASFDERQPYAHMNGGRKNERALPLPQSSAC |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-25 | |||||
Sequence: MKAELVPVCTAWILGLLLCLGPAAA | ||||||
Chain | PRO_0000045749 | 26-730 | Insulin-like growth factor 1 receptor alpha chain | |||
Sequence: KVCGPNMDIRNDVSELKQLRDCVVIEGYLQILLISNAKAEDFRNLRFPNLTVITDYLLLFRVSGLVSLSNLFPNLTVIRGRVLFYNYALVIFEMTDLKEIGLYNLRNITRGAVRIEKNSELCYVSTVDWSLVLDAVYNNYIVGNKPPKECVDLCPGAREKMQICEKSSINNEFADRCWSDEHCQKVCPSVCGKRACSDNNECCHPECLGSCTAPDNDTACVACHHYFYEGRCVPTCPSNTYKFEGWRCITREVCAKMHIWIHSTIPFIIHKGECVYECPSGYMLNKSQSMTCSPCEGPCPKICEEKMKTIDSVTSAQMLEGCTVLKGNLQLNIRKGQNIAAELENFLGLIETVTGYVKIRHSHALVSLSFLKSLRYILGEEQMPGNYSFYVFDNNNLQQLWDWSKHNLTIKEGKIRFAFNSKLCASEIYRMEEVTGTKGRQAEEDISLSTNGNMASCESHVLNFTSRSKIKNRIKLTWERYRPPDYRDLISFTVYYKEAPFRNVTEYDGQDACGSNSWNMVDVDLPASKESDPGILLQGLKPWTQYAIYVKAITLTMLENRHIHGAKSKIIYMRTDAAVPSIPQDMISASNSSSQLVVKWNPPSLPNGNLSYYIVRWQQQPQDRHLYQYNYCFKDKVPNRKYANGTIDTEGGTEPTKPEGSVGEKGHYCACPKTEAEEKAEKDEAEYRKVFENFLHNSIFVPRPN | ||||||
Glycosylation | 74 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 99 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 132 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 212↔221 | |||||
Sequence: CPSVCGKRAC | ||||||
Disulfide bond | 216↔227 | |||||
Sequence: CGKRACSDNNEC | ||||||
Disulfide bond | 228↔236 | |||||
Sequence: CHPECLGSC | ||||||
Disulfide bond | 232↔245 | |||||
Sequence: CLGSCTAPDNDTAC | ||||||
Glycosylation | 241 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 248↔257 | |||||
Sequence: CHHYFYEGRC | ||||||
Disulfide bond | 261↔273 | |||||
Sequence: CPSNTYKFEGWRC | ||||||
Disulfide bond | 279↔299 | |||||
Sequence: CAKMHIWIHSTIPFIIHKGEC | ||||||
Disulfide bond | 303↔317 | |||||
Sequence: CPSGYMLNKSQSMTC | ||||||
Glycosylation | 310 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 320↔324 | |||||
Sequence: CEGPC | ||||||
Glycosylation | 411 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 432 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 488 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 528 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 616 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 634 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 669 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Chain | PRO_0000045750 | 735-1358 | Insulin-like growth factor 1 receptor beta chain | |||
Sequence: DVLAVGNSTVTSYEKNSTTEDFSNFSDSERDDIEYPFYETKVDYKWERTVISNLQPFTLYRIDIHSCNHEAEKLGCSASNFVFARTMPAAGADDIPGIVNTKEEDDGVIFLGWPEPLRPNGLILMYEIEYKHQGEVHRECVSRQDYRKNGGIKLVRLPPGNYSAQVQAISLYGNGSWTEMVSFCVKLKPDVRNNILQMVVAIPLALSFLLVGIISIVCFVFKKRNSNRLGNGVLYASVNPEYFSAAEMYVPDKWEVPREKITMNRELGQGSFGMVYEGIAKGVVKDEAETKVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMTRGDLKSYLRSLRPDTESNSGQPTPSLKKMIQMAGEIADGMSYLNANKFVHRDLAARNCMVTEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTNSDVWSFGVVLWEIATLAEQPYQGMSNEQVLRFVMEGGLLEKPDNCPDMLFELMRMCWQFNPKMRPSFLEIISSIKDELDPGFKEVSFFYSEENKPPDTEELDLEAENMESIPLDPSCALQNSEHHAGHKSENGPGVVVLRASFDERQPYAHMNGGRKNERALPLPQSSAC | ||||||
Glycosylation | 741 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 750 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 758 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 895 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 908 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 976 | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y | ||||||
Modified residue | 1157 | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y | ||||||
Modified residue | 1161 | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y | ||||||
Modified residue | 1162 | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y |
Post-translational modification
The cytoplasmic domain of the beta subunit is autophosphorylated on Tyr residues in response to low concentrations of insulin-like growth factor (IGF 1) and higher concentrations of insulin.
Keywords
- PTM
PTM databases
Expression
Developmental stage
Expressed both maternally and zygotically. Shows biphasic expression during early development. Expressed ubiquitously in fertilized eggs and throughout the midblastula transition. Expression then decreases at mid-gastrulation. Shortly after gastrulation, expression is seen throughout the dorsal side of the embryo with expression strongest in the anterior and absent ventrally. Expression increases along the dorsal midline at early neurulation and is seen in the head region as neurulation progresses, particularly in the area of the cement gland primordium. Also present in the anterior mesoderm but is absent from the neural tube and the most ventral part of the embryo. Remains expressed throughout early embryogenesis. By the tailbud stages, expression is anterior, in the head and the most rostral part of the neural tube.
Gene expression databases
Interaction
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 chain carries the kinase domain (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O73798 | gipc2.S Q5HZ83 | 2 | EBI-8068109, EBI-8068143 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 483-603 | Fibronectin type-III 1 | ||||
Sequence: ESHVLNFTSRSKIKNRIKLTWERYRPPDYRDLISFTVYYKEAPFRNVTEYDGQDACGSNSWNMVDVDLPASKESDPGILLQGLKPWTQYAIYVKAITLTMLENRHIHGAKSKIIYMRTDAA | ||||||
Domain | 604-702 | Fibronectin type-III 2 | ||||
Sequence: VPSIPQDMISASNSSSQLVVKWNPPSLPNGNLSYYIVRWQQQPQDRHLYQYNYCFKDKVPNRKYANGTIDTEGGTEPTKPEGSVGEKGHYCACPKTEAE | ||||||
Region | 670-691 | Disordered | ||||
Sequence: GTIDTEGGTEPTKPEGSVGEKG | ||||||
Domain | 727-818 | Fibronectin type-III 3 | ||||
Sequence: PRPNRRRRDVLAVGNSTVTSYEKNSTTEDFSNFSDSERDDIEYPFYETKVDYKWERTVISNLQPFTLYRIDIHSCNHEAEKLGCSASNFVFA | ||||||
Domain | 829-924 | Fibronectin type-III 4 | ||||
Sequence: IPGIVNTKEEDDGVIFLGWPEPLRPNGLILMYEIEYKHQGEVHRECVSRQDYRKNGGIKLVRLPPGNYSAQVQAISLYGNGSWTEMVSFCVKLKPD | ||||||
Domain | 995-1270 | Protein kinase | ||||
Sequence: ITMNRELGQGSFGMVYEGIAKGVVKDEAETKVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMTRGDLKSYLRSLRPDTESNSGQPTPSLKKMIQMAGEIADGMSYLNANKFVHRDLAARNCMVTEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTNSDVWSFGVVLWEIATLAEQPYQGMSNEQVLRFVMEGGLLEKPDNCPDMLFELMRMCWQFNPKMRPSFLEIISSIKDELDPGF | ||||||
Region | 1336-1358 | Disordered | ||||
Sequence: PYAHMNGGRKNERALPLPQSSAC |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,358
- Mass (Da)153,864
- Last updated1998-08-01 v1
- Checksum2E4E1F8EA6696776
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF055980 EMBL· GenBank· DDBJ | AAC12942.1 EMBL· GenBank· DDBJ | mRNA |