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Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) [Cleaved into: Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain] (Fragment)

 IGF1R_BOVIN             Reviewed;         640 AA.
Q05688;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 149.
RecName: Full=Insulin-like growth factor 1 receptor;
EC=2.7.10.1;
AltName: Full=Insulin-like growth factor I receptor;
Short=IGF-I receptor;
AltName: CD_antigen=CD221;
Contains:
RecName: Full=Insulin-like growth factor 1 receptor alpha chain;
Contains:
RecName: Full=Insulin-like growth factor 1 receptor beta chain;
Flags: Precursor; Fragment;
Name=IGF1R;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
PubMed=1662995; DOI=10.3109/10425179109020797;
Sneyers M., Kettmann R., Massart S., Renaville R., Burny A.,
Portetelle D.;
"Cloning and characterization of a cDNA encoding the beta-subunit of
the bovine insulin-like growth factor-1 receptor.";
DNA Seq. 1:405-406(1991).
-!- FUNCTION: Receptor tyrosine kinase which mediates actions of
insulin-like growth factor 1 (IGF1). Binds IGF1 with high affinity
and IGF2 and insulin (INS) with a lower affinity. The activated
IGF1R is involved in cell growth and survival control. IGF1R is
crucial for tumor transformation and survival of malignant cell.
Ligand binding activates the receptor kinase, leading to receptor
autophosphorylation, and tyrosines phosphorylation of multiple
substrates, that function as signaling adapter proteins including,
the insulin-receptor substrates (IRS1/2), Shc and 14-3-3 proteins.
Phosphorylation of IRSs proteins lead to the activation of two
main signaling pathways: the PI3K-AKT/PKB pathway and the Ras-MAPK
pathway. The result of activating the MAPK pathway is increased
cellular proliferation, whereas activating the PI3K pathway
inhibits apoptosis and stimulates protein synthesis.
Phosphorylated IRS1 can activate the 85 kDa regulatory subunit of
PI3K (PIK3R1), leading to activation of several downstream
substrates, including protein AKT/PKB. AKT phosphorylation, in
turn, enhances protein synthesis through mTOR activation and
triggers the antiapoptotic effects of IGFIR through
phosphorylation and inactivation of BAD. In parallel to PI3K-
driven signaling, recruitment of Grb2/SOS by phosphorylated IRS1
or Shc leads to recruitment of Ras and activation of the ras-MAPK
pathway. In addition to these two main signaling pathways IGF1R
signals also through the Janus kinase/signal transducer and
activator of transcription pathway (JAK/STAT). Phosphorylation of
JAK proteins can lead to phosphorylation/activation of signal
transducers and activators of transcription (STAT) proteins. In
particular activation of STAT3, may be essential for the
transforming activity of IGF1R. The JAK/STAT pathway activates
gene transcription and may be responsible for the transforming
activity. JNK kinases can also be activated by the IGF1R. IGF1
exerts inhibiting activities on JNK activation via phosphorylation
and inhibition of MAP3K5/ASK1, which is able to directly associate
with the IGF1R (By similarity). When present in a hybrid receptor
with INSR, binds IGF1 (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ACTIVITY REGULATION: Activated by autophosphorylation at Tyr-434,
Tyr-438 and Tyr-439 on the kinase activation loop; phosphorylation
at all three tyrosine residues is required for optimal kinase
activity. Inhibited by MSC1609119A-1, BMS-754807, PQIP,
benzimidazole pyridinone, isoquinolinedione, bis-azaindole, 3-
cyanoquinoline, 2,4-bis-arylamino-1,3-pyrimidine,
pyrrolopyrimidine, pyrrole-5-carboxaldehyde, picropodophyllin
(PPP), tyrphostin derivatives. While most inhibitors bind to the
ATP binding pocket, MSC1609119A-1 functions as allosteric
inhibitor and binds close to the DFG motif and the activation loop
(By similarity). {ECO:0000250}.
-!- 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.
Interacts with PIK3R1 and with the PTB/PID domains of IRS1 and
SHC1 in vitro when autophosphorylated on tyrosine residues. Forms
a hybrid receptor with INSR, 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 ARRB1 and ARRB2. Interacts
with GRB10. Interacts with RACK1 (By similarity). Interacts with
SOCS1, SOCS2 and SOCS3 (By similarity). Interacts with 14-3-3
proteins (By similarity). Interacts with NMD2 (By similarity).
Interacts with MAP3K5 (By similarity). Interacts with STAT3 (By
similarity). Interacts (nascent precursor form) with ZFAND2B (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:P08069}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}.
-!- PTM: Autophosphorylated on tyrosine residues in response to ligand
binding. Autophosphorylation occurs in trans, i.e. one subunit of
the dimeric receptor phosphorylates tyrosine residues on the other
subunit. Autophosphorylation occurs in a sequential manner; Tyr-
438 is predominantly phosphorylated first, followed by
phosphorylation of Tyr-434 and Tyr-439. While every single
phosphorylation increases kinase activity, all three tyrosine
residues in the kinase activation loop (Tyr-438, Tyr-434 and Tyr-
439) have to be phosphorylated for optimal activity. Can be
autophosphorylated at additional tyrosine residues (in vitro).
Autophosphorylated is followed by phosphorylation of juxtamembrane
tyrosines and C-terminal serines. Phosphorylation of Tyr-253 is
required for IRS1- and SHC1-binding (By similarity).
Phosphorylation of Ser-551 by GSK-3beta restrains kinase activity
and promotes cell surface expression, it requires a priming
phosphorylation at Ser-555. Dephosphorylated by PTPN1 (By
similarity). {ECO:0000250}.
-!- PTM: Polyubiquitinated at Lys-441 and Lys-444 through both 'Lys-
48' and 'Lys-29' linkages, promoting receptor endocytosis and
subsequent degradation by the proteasome. Ubiquitination is
facilitated by pre-existing phosphorylation (By similarity).
{ECO:0000250}.
-!- PTM: Sumoylated with SUMO1. {ECO:0000250}.
-!- PTM: Controlled by regulated intramembrane proteolysis (RIP).
Undergoes metalloprotease-dependent constitutive ectodomain
shedding to produce a membrane-anchored 52 kDa C-Terminal fragment
which is further processed by presenilin gamma-secretase to yield
an intracellular 50 kDa fragment (By similarity). {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; X54980; CAA38724.1; -; mRNA.
PIR; S23008; S23008.
RefSeq; NP_001231541.1; NM_001244612.1.
UniGene; Bt.105919; -.
UniGene; Bt.12759; -.
ProteinModelPortal; Q05688; -.
SMR; Q05688; -.
STRING; 9913.ENSBTAP00000028690; -.
PaxDb; Q05688; -.
PRIDE; Q05688; -.
GeneID; 281848; -.
KEGG; bta:281848; -.
CTD; 3480; -.
eggNOG; KOG4258; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000038045; -.
HOVERGEN; HBG006134; -.
InParanoid; Q05688; -.
KO; K05087; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:AgBase.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:AgBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0043560; F:insulin receptor substrate binding; ISS:UniProtKB.
GO; GO:0005520; F:insulin-like growth factor binding; IMP:AgBase.
GO; GO:0005010; F:insulin-like growth factor-activated receptor activity; ISS:UniProtKB.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISS:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0051389; P:inactivation of MAPKK activity; ISS:UniProtKB.
GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0051262; P:protein tetramerization; ISS:UniProtKB.
GO; GO:0046328; P:regulation of JNK cascade; ISS:UniProtKB.
CDD; cd00063; FN3; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
Pfam; PF00041; fn3; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00060; FN3; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF49265; SSF49265; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50853; FN3; 2.
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.
2: Evidence at transcript level;
ATP-binding; Cell membrane; Cleavage on pair of basic residues;
Complete proteome; Disulfide bond; Glycoprotein; Isopeptide bond;
Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
Reference proteome; Repeat; Transferase; Transmembrane;
Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
CHAIN <1 9 Insulin-like growth factor 1 receptor
alpha chain.
/FTId=PRO_0000016679.
CHAIN 14 640 Insulin-like growth factor 1 receptor
beta chain.
/FTId=PRO_0000016680.
TOPO_DOM 14 208 Extracellular. {ECO:0000255}.
TRANSMEM 209 232 Helical. {ECO:0000255}.
TOPO_DOM 233 640 Cytoplasmic. {ECO:0000255}.
DOMAIN 5 101 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 107 200 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 272 547 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 278 286 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 250 253 IRS1- and SHC1-binding. {ECO:0000250}.
ACT_SITE 408 408 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 306 306 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 253 253 Phosphotyrosine.
{ECO:0000250|UniProtKB:P08069}.
MOD_RES 434 434 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P08069}.
MOD_RES 438 438 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P08069}.
MOD_RES 439 439 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P08069}.
MOD_RES 551 551 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:Q60751}.
MOD_RES 555 555 Phosphoserine.
{ECO:0000250|UniProtKB:Q60751}.
CARBOHYD 20 20 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 29 29 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 37 37 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 173 173 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 186 186 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CROSSLNK 441 441 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P08069}.
CROSSLNK 444 444 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P08069}.
NON_TER 1 1
SEQUENCE 640 AA; 72511 MW; 1E645258BDC6FF29 CRC64;
NAIFVPRPER KRREVMQIAN TTMSSRSRNT TVLDTYNITD PEELETEYPF FESRVDNKER
TVISNLRPFT LYRIDIHSCN HEAEKLGCSA SNFVFARTMP AEGADDIPGP VTWEPRPENS
IFLKWPEPEN PNGLILMYEI KYGSQVEDQR ECVSRQEYRK YGGAKLNRLN PGNYTARIQA
TSLSGNGSWT DPVFFYVQAK TTYENFIHLM IALPIAVLLI VGGLVIMLYV FHRKRNSSRL
GNGVLYASVN PEYFSAADVY VPDEWEVARE KITMSRELGQ GSFGMVYEGV AKGVVKDEPE
TRVAIKTVNE AASMRERIEF LNEASVMKEF NCHHVVRLLG VVSQGQPTLV IMELMTRGDL
KSYLRSLRPE MENNPVLAPP SLSKMIQMAG EIADGMAYLN ANKFVHRDLA ARNCMVAEDF
TVKIGDFGMT RDIYETDYYR KGGKGLLPVR WMSPESLKDG VFTTHSDVWS FGVVLWEIAT
LAEQPYQGLS NEQVLRFVME GGLLDKPDNC PDMLFELMRM CWQYNPKMRP SFLEIISSVK
DEMEAGFREV SFYYSEENKP PEPEELDLEP ENMESVPLDP SASSASLPLP DRHSGHKAEN
GPGPGVLVLR ASFDERQPYA HMNGGRKNER ALPLPQSSTC


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