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Protein

Insulin-like growth factor 1 receptor

Gene

igf1r

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation1 Publication

Cofactori

Mn2+By similarity

Enzyme regulationi

Autophosphorylation activates the kinase activity.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1029 – 10291ATPPROSITE-ProRule annotationBy similarity
Active sitei1131 – 11311Proton acceptorPROSITE-ProRule annotationBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1001 – 10099ATPPROSITE-ProRule annotationBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • insulin-like growth factor-activated receptor activity Source: UniProtKB
  • insulin-like growth factor binding Source: UniProtKB
  • insulin receptor substrate binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • phosphatidylinositol 3-kinase binding Source: UniProtKB
  • protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  • insulin-like growth factor receptor signaling pathway Source: UniProtKB
  • multicellular organism development Source: UniProtKB-KW
  • oocyte maturation Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • protein tetramerization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Manganese, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Insulin-like growth factor 1 receptor (EC:2.7.10.1)
Short name:
xIGF-1R
Short name:
xIGFR
Cleaved into the following 2 chains:
Gene namesi
Name:igf1r
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-865040. igf1r.

Subcellular locationi

  • Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication

  • Note: Expressed at the oocyte surface.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini735 – 934200ExtracellularSequence analysisAdd
BLAST
Transmembranei935 – 95521HelicalSequence analysisAdd
BLAST
Topological domaini956 – 1358403CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Chaini26 – 730705Insulin-like growth factor 1 receptor alpha chain1 PublicationPRO_0000045749Add
BLAST
Chaini735 – 1358624Insulin-like growth factor 1 receptor beta chain1 PublicationPRO_0000045750Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi74 – 741N-linked (GlcNAc...)Sequence analysis
Glycosylationi99 – 991N-linked (GlcNAc...)Sequence analysis
Glycosylationi132 – 1321N-linked (GlcNAc...)Sequence analysis
Disulfide bondi212 ↔ 221By similarity
Disulfide bondi216 ↔ 227By similarity
Disulfide bondi228 ↔ 236By similarity
Disulfide bondi232 ↔ 245By similarity
Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence analysis
Disulfide bondi248 ↔ 257By similarity
Disulfide bondi261 ↔ 273By similarity
Disulfide bondi279 ↔ 299By similarity
Disulfide bondi303 ↔ 317By similarity
Glycosylationi310 – 3101N-linked (GlcNAc...)Sequence analysis
Disulfide bondi320 ↔ 324By similarity
Glycosylationi411 – 4111N-linked (GlcNAc...)Sequence analysis
Glycosylationi432 – 4321N-linked (GlcNAc...)Sequence analysis
Glycosylationi488 – 4881N-linked (GlcNAc...)Sequence analysis
Glycosylationi528 – 5281N-linked (GlcNAc...)Sequence analysis
Glycosylationi616 – 6161N-linked (GlcNAc...)Sequence analysis
Glycosylationi634 – 6341N-linked (GlcNAc...)Sequence analysis
Glycosylationi669 – 6691N-linked (GlcNAc...)Sequence analysis
Glycosylationi741 – 7411N-linked (GlcNAc...)Sequence analysis
Glycosylationi750 – 7501N-linked (GlcNAc...)Sequence analysis
Glycosylationi758 – 7581N-linked (GlcNAc...)Sequence analysis
Glycosylationi895 – 8951N-linked (GlcNAc...)Sequence analysis
Glycosylationi908 – 9081N-linked (GlcNAc...)Sequence analysis
Modified residuei976 – 9761Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1157 – 11571Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1161 – 11611Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1162 – 11621Phosphotyrosine; by autocatalysisBy similarity

Post-translational modificationi

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 - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiO73798.

Expressioni

Developmental stagei

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.3 Publications

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
gipc2Q5HZ832EBI-8068109,EBI-8068143

GO - Molecular functioni

Protein-protein interaction databases

IntActiO73798. 1 interaction.
MINTiMINT-609362.

Structurei

3D structure databases

ProteinModelPortaliO73798.
SMRiO73798. Positions 26-483, 973-1285.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini483 – 603121Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini604 – 70299Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini727 – 81892Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini829 – 92496Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini995 – 1270276Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.PROSITE-ProRule annotation
Contains 4 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG006134.
KOiK05087.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
3.80.20.20. 2 hits.
InterProiIPR003961. FN3_dom.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000494. Rcpt_L-dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016246. Tyr_kinase_insulin-like_rcpt.
IPR002011. Tyr_kinase_rcpt_2_CS.
[Graphical view]
PfamiPF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFiPIRSF000620. Insulin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00060. FN3. 3 hits.
SM00261. FU. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 4 hits.
SSF52058. SSF52058. 2 hits.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiPS50853. FN3. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O73798-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAELVPVCT AWILGLLLCL GPAAAKVCGP NMDIRNDVSE LKQLRDCVVI
60 70 80 90 100
EGYLQILLIS NAKAEDFRNL RFPNLTVITD YLLLFRVSGL VSLSNLFPNL
110 120 130 140 150
TVIRGRVLFY NYALVIFEMT DLKEIGLYNL RNITRGAVRI EKNSELCYVS
160 170 180 190 200
TVDWSLVLDA VYNNYIVGNK PPKECVDLCP GAREKMQICE KSSINNEFAD
210 220 230 240 250
RCWSDEHCQK VCPSVCGKRA CSDNNECCHP ECLGSCTAPD NDTACVACHH
260 270 280 290 300
YFYEGRCVPT CPSNTYKFEG WRCITREVCA KMHIWIHSTI PFIIHKGECV
310 320 330 340 350
YECPSGYMLN KSQSMTCSPC EGPCPKICEE KMKTIDSVTS AQMLEGCTVL
360 370 380 390 400
KGNLQLNIRK GQNIAAELEN FLGLIETVTG YVKIRHSHAL VSLSFLKSLR
410 420 430 440 450
YILGEEQMPG NYSFYVFDNN NLQQLWDWSK HNLTIKEGKI RFAFNSKLCA
460 470 480 490 500
SEIYRMEEVT GTKGRQAEED ISLSTNGNMA SCESHVLNFT SRSKIKNRIK
510 520 530 540 550
LTWERYRPPD YRDLISFTVY YKEAPFRNVT EYDGQDACGS NSWNMVDVDL
560 570 580 590 600
PASKESDPGI LLQGLKPWTQ YAIYVKAITL TMLENRHIHG AKSKIIYMRT
610 620 630 640 650
DAAVPSIPQD MISASNSSSQ LVVKWNPPSL PNGNLSYYIV RWQQQPQDRH
660 670 680 690 700
LYQYNYCFKD KVPNRKYANG TIDTEGGTEP TKPEGSVGEK GHYCACPKTE
710 720 730 740 750
AEEKAEKDEA EYRKVFENFL HNSIFVPRPN RRRRDVLAVG NSTVTSYEKN
760 770 780 790 800
STTEDFSNFS DSERDDIEYP FYETKVDYKW ERTVISNLQP FTLYRIDIHS
810 820 830 840 850
CNHEAEKLGC SASNFVFART MPAAGADDIP GIVNTKEEDD GVIFLGWPEP
860 870 880 890 900
LRPNGLILMY EIEYKHQGEV HRECVSRQDY RKNGGIKLVR LPPGNYSAQV
910 920 930 940 950
QAISLYGNGS WTEMVSFCVK LKPDVRNNIL QMVVAIPLAL SFLLVGIISI
960 970 980 990 1000
VCFVFKKRNS NRLGNGVLYA SVNPEYFSAA EMYVPDKWEV PREKITMNRE
1010 1020 1030 1040 1050
LGQGSFGMVY EGIAKGVVKD EAETKVAIKT VNEAASMRER IEFLNEASVM
1060 1070 1080 1090 1100
KEFNCHHVVR LLGVVSQGQP TLVIMELMTR GDLKSYLRSL RPDTESNSGQ
1110 1120 1130 1140 1150
PTPSLKKMIQ MAGEIADGMS YLNANKFVHR DLAARNCMVT EDFTVKIGDF
1160 1170 1180 1190 1200
GMTRDIYETD YYRKGGKGLL PVRWMSPESL KDGVFTTNSD VWSFGVVLWE
1210 1220 1230 1240 1250
IATLAEQPYQ GMSNEQVLRF VMEGGLLEKP DNCPDMLFEL MRMCWQFNPK
1260 1270 1280 1290 1300
MRPSFLEIIS SIKDELDPGF KEVSFFYSEE NKPPDTEELD LEAENMESIP
1310 1320 1330 1340 1350
LDPSCALQNS EHHAGHKSEN GPGVVVLRAS FDERQPYAHM NGGRKNERAL

PLPQSSAC
Length:1,358
Mass (Da):153,864
Last modified:August 1, 1998 - v1
Checksum:i2E4E1F8EA6696776
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF055980 mRNA. Translation: AAC12942.1.
RefSeqiNP_001081734.1. NM_001088265.1.
UniGeneiXl.269.

Genome annotation databases

GeneIDi398022.
KEGGixla:398022.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF055980 mRNA. Translation: AAC12942.1.
RefSeqiNP_001081734.1. NM_001088265.1.
UniGeneiXl.269.

3D structure databases

ProteinModelPortaliO73798.
SMRiO73798. Positions 26-483, 973-1285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO73798. 1 interaction.
MINTiMINT-609362.

Proteomic databases

PRIDEiO73798.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi398022.
KEGGixla:398022.

Organism-specific databases

CTDi3480.
XenbaseiXB-GENE-865040. igf1r.

Phylogenomic databases

HOVERGENiHBG006134.
KOiK05087.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
3.80.20.20. 2 hits.
InterProiIPR003961. FN3_dom.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000494. Rcpt_L-dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016246. Tyr_kinase_insulin-like_rcpt.
IPR002011. Tyr_kinase_rcpt_2_CS.
[Graphical view]
PfamiPF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFiPIRSF000620. Insulin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00060. FN3. 3 hits.
SM00261. FU. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 4 hits.
SSF52058. SSF52058. 2 hits.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiPS50853. FN3. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and characterization of Xenopus insulin-like growth factor-1 receptor: its role in mediating insulin-induced Xenopus oocyte maturation and expression during embryogenesis."
    Zhu L., Ohan N., Agazie Y., Cummings C., Farah S., Liu X.J.
    Endocrinology 139:949-954(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, AUTOPHOSPHORYLATION.
    Tissue: Oocyte1 Publication.
  2. "Insulin and insulin-like-growth-factor-I (IGF-I) receptors in Xenopus laevis oocytes. Comparison with insulin receptors from liver and muscle."
    Hainaut P., Kowalski A., Giorgetti S., Baron V., Van Obberghen E.
    Biochem. J. 273:673-678(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION.
  3. "Neural and head induction by insulin-like growth factor signals."
    Pera E.M., Wessely O., Li S.-Y., De Robertis E.M.
    Dev. Cell 1:655-665(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  4. "The IGF pathway regulates head formation by inhibiting Wnt signaling in Xenopus."
    Richard-Parpaillon L., Heligon C., Chesnel F., Boujard D., Philpott A.
    Dev. Biol. 244:407-417(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiIGF1R_XENLA
AccessioniPrimary (citable) accession number: O73798
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: August 1, 1998
Last modified: July 6, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.