ID INSR_MOUSE Reviewed; 1372 AA. AC P15208; F8VPU4; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2012, sequence version 2. DT 27-MAR-2024, entry version 237. DE RecName: Full=Insulin receptor; DE Short=IR; DE EC=2.7.10.1; DE AltName: CD_antigen=CD220; DE Contains: DE RecName: Full=Insulin receptor subunit alpha; DE Contains: DE RecName: Full=Insulin receptor subunit beta; DE Flags: Precursor; GN Name=Insr; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2557333; DOI=10.1016/s0021-9258(20)88221-0; RA Flores-Riveros J.R., Sibley E., Kastelic T., Lane M.D.; RT "Substrate phosphorylation catalyzed by the insulin receptor tyrosine RT kinase. Kinetic correlation to autophosphorylation of specific sites in the RT beta subunit."; RL J. Biol. Chem. 264:21557-21572(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33. RX PubMed=2602374; DOI=10.1073/pnas.86.24.9732; RA Sibley E., Kastelic T., Kelly T.J., Lane M.D.; RT "Characterization of the mouse insulin receptor gene promoter."; RL Proc. Natl. Acad. Sci. U.S.A. 86:9732-9736(1989). RN [4] RP INTERACTION WITH IRS1 AND IRS2, AND MUTAGENESIS OF TYR-989. RX PubMed=8626379; DOI=10.1074/jbc.271.11.5980; RA Sawka-Verhelle D., Tartare-Deckert S., White M.F., Van Obberghen E.; RT "Insulin receptor substrate-2 binds to the insulin receptor through its RT phosphotyrosine-binding domain and through a newly identified domain RT comprising amino acids 591-786."; RL J. Biol. Chem. 271:5980-5983(1996). RN [5] RP INTERACTION WITH SORBS1. RX PubMed=9447983; DOI=10.1128/mcb.18.2.872; RA Ribon V., Printen J.A., Hoffman N.G., Kay B.K., Saltiel A.R.; RT "A novel, multifunctional c-Cbl binding protein in insulin receptor RT signaling in 3T3-L1 adipocytes."; RL Mol. Cell. Biol. 18:872-879(1998). RN [6] RP MUTAGENESIS OF TYR-989. RX PubMed=10207032; DOI=10.1074/jbc.274.17.12075; RA Chaika O.V., Chaika N., Volle D.J., Hayashi H., Ebina Y., Wang L.M., RA Pierce J.H., Lewis R.E.; RT "Mutation of tyrosine 960 within the insulin receptor juxtamembrane domain RT impairs glucose transport but does not inhibit ligand-mediated RT phosphorylation of insulin receptor substrate-2 in 3T3-L1 adipocytes."; RL J. Biol. Chem. 274:12075-12080(1999). RN [7] RP INTERACTION WITH SOCS3. RX PubMed=10821852; DOI=10.1074/jbc.275.21.15985; RA Emanuelli B., Peraldi P., Filloux C., Sawka-Verhelle D., Hilton D., RA Van Obberghen E.; RT "SOCS-3 is an insulin-induced negative regulator of insulin signaling."; RL J. Biol. Chem. 275:15985-15991(2000). RN [8] RP PHOSPHORYLATION, AND DEPHOSPHORYLATION BY PTPN2. RX PubMed=12612081; DOI=10.1128/mcb.23.6.2096-2108.2003; RA Galic S., Klingler-Hoffmann M., Fodero-Tavoletti M.T., Puryer M.A., RA Meng T.C., Tonks N.K., Tiganis T.; RT "Regulation of insulin receptor signaling by the protein tyrosine RT phosphatase TCPTP."; RL Mol. Cell. Biol. 23:2096-2108(2003). RN [9] RP INTERACTION WITH SOCS1 AND SOCS3. RX PubMed=15169905; DOI=10.1128/mcb.24.12.5434-5446.2004; RA Ueki K., Kondo T., Kahn C.R.; RT "Suppressor of cytokine signaling 1 (SOCS-1) and SOCS-3 cause insulin RT resistance through inhibition of tyrosine phosphorylation of insulin RT receptor substrate proteins by discrete mechanisms."; RL Mol. Cell. Biol. 24:5434-5446(2004). RN [10] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-445. RC TISSUE=Myoblast; RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200; RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.; RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome: RT identification, glycosite occupancy, and membrane orientation."; RL Mol. Cell. Proteomics 8:2555-2569(2009). RN [11] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-445. RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N-linked RT cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [12] RP INTERACTION WITH ARRB2. RX PubMed=19122674; DOI=10.1038/nature07617; RA Luan B., Zhao J., Wu H., Duan B., Shu G., Wang X., Li D., Jia W., Kang J., RA Pei G.; RT "Deficiency of a beta-arrestin-2 signal complex contributes to insulin RT resistance."; RL Nature 457:1146-1149(2009). RN [13] RP PHOSPHORYLATION AT TYR-1179 AND TYR-1180. RX PubMed=20655470; DOI=10.1016/j.cell.2010.06.003; RA Ferron M., Wei J., Yoshizawa T., Del Fattore A., DePinho R.A., Teti A., RA Ducy P., Karsenty G.; RT "Insulin signaling in osteoblasts integrates bone remodeling and energy RT metabolism."; RL Cell 142:296-308(2010). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and RC Pancreas; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [15] RP INTERACTION WITH LMBRD1. RX PubMed=24078630; DOI=10.1074/jbc.m113.479527; RA Tseng L.T., Lin C.L., Tzen K.Y., Chang S.C., Chang M.F.; RT "LMBD1 protein serves as a specific adaptor for insulin receptor RT internalization."; RL J. Biol. Chem. 288:32424-32432(2013). RN [16] RP FUNCTION, INTERACTION WITH SORL1, AND SUBCELLULAR LOCATION. RX PubMed=27322061; DOI=10.1172/jci84708; RA Schmidt V., Schulz N., Yan X., Schuermann A., Kempa S., Kern M., RA Blueher M., Poy M.N., Olivecrona G., Willnow T.E.; RT "SORLA facilitates insulin receptor signaling in adipocytes and exacerbates RT obesity."; RL J. Clin. Invest. 126:2706-2720(2016). CC -!- FUNCTION: Receptor tyrosine kinase which mediates the pleiotropic CC actions of insulin. Binding of insulin leads to phosphorylation of CC several intracellular substrates, including, insulin receptor CC substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling CC intermediates. Each of these phosphorylated proteins serve as docking CC proteins for other signaling proteins that contain Src-homology-2 CC domains (SH2 domain) that specifically recognize different CC phosphotyrosine residues, including the p85 regulatory subunit of PI3K CC and SHP2. Phosphorylation of IRSs proteins lead to the activation of CC two main signaling pathways: the PI3K-AKT/PKB pathway, which is CC responsible for most of the metabolic actions of insulin, and the Ras- CC MAPK pathway, which regulates expression of some genes and cooperates CC with the PI3K pathway to control cell growth and differentiation. CC Binding of the SH2 domains of PI3K to phosphotyrosines on IRS1 leads to CC the activation of PI3K and the generation of phosphatidylinositol-(3, CC 4, 5)-triphosphate (PIP3), a lipid second messenger, which activates CC several PIP3-dependent serine/threonine kinases, such as PDPK1 and CC subsequently AKT/PKB. The net effect of this pathway is to produce a CC translocation of the glucose transporter SLC2A4/GLUT4 from cytoplasmic CC vesicles to the cell membrane to facilitate glucose transport. CC Moreover, upon insulin stimulation, activated AKT/PKB is responsible CC for: anti-apoptotic effect of insulin by inducing phosphorylation of CC BAD; regulates the expression of gluconeogenic and lipogenic enzymes by CC controlling the activity of the winged helix or forkhead (FOX) class of CC transcription factors. Another pathway regulated by PI3K-AKT/PKB CC activation is mTORC1 signaling pathway which regulates cell growth and CC metabolism and integrates signals from insulin. AKT mediates insulin- CC stimulated protein synthesis by phosphorylating TSC2 thereby activating CC mTORC1 pathway. The Ras/RAF/MAP2K/MAPK pathway is mainly involved in CC mediating cell growth, survival and cellular differentiation of CC insulin. Phosphorylated IRS1 recruits GRB2/SOS complex, which triggers CC the activation of the Ras/RAF/MAP2K/MAPK pathway. In addition to CC binding insulin, the insulin receptor can bind insulin-like growth CC factors (IGFI and IGFII). When present in a hybrid receptor with IGF1R, CC binds IGF1 (By similarity). In adipocytes, inhibits lipolysis CC (PubMed:27322061). {ECO:0000250, ECO:0000269|PubMed:27322061}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028}; CC -!- ACTIVITY REGULATION: Activated in response to insulin. CC Autophosphorylation activates the kinase activity. PTPN1, PTPRE and CC PTPRF dephosphorylate important tyrosine residues, thereby reducing CC INSR activity. Inhibited by ENPP1. GRB10 and GRB14 inhibit the CC catalytic activity of the INSR, they block access of substrates to the CC activated receptor. SOCS1 and SOCS3 act as negative regulators of INSR CC activity, they bind to the activated INRS and interfere with the CC phosphorylation of INSR substrates (By similarity). Interacts with CC PTPRF (By similarity). Interacts with ATIC; ATIC together with CC PRKAA2/AMPK2 and HACD3/PTPLAD1 is proposed to be part of a signaling CC netwok regulating INSR autophosphorylation and endocytosis (By CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P15127}. CC -!- SUBUNIT: Tetramer of 2 alpha and 2 beta chains linked by disulfide CC bonds. The alpha chains carry the insulin-binding regions, while the CC beta chains carry the kinase domain. Forms a hybrid receptor with CC IGF1R, the hybrid is a tetramer consisting of 1 alpha chain and 1 beta CC chain of INSR and 1 alpha chain and 1 beta chain of IGF1R. Interacts CC with SORBS1 but dissociates from it following insulin stimulation. CC Binds SH2B2 (By similarity). Activated form of INSR interacts (via Tyr- CC 989) with the PTB/PID domains of IRS1 and SHC1. The sequences CC surrounding the phosphorylated NPXY motif contribute differentially to CC either IRS1 or SHC1 recognition. Interacts (via tyrosines in the C- CC terminus) with IRS2 (via PTB domain and 591-786 AA); the 591-786 would CC be the primary anchor of IRS2 to INSR while the PTB domain would have a CC stabilizing action on the interaction with INSR. Interacts with the SH2 CC domains of the 85 kDa regulatory subunit of PI3K (PIK3R1) in vitro, CC when autophosphorylated on tyrosine residues. Interacts with SOCS7 (By CC similarity). Interacts (via the phosphorylated Tyr-989), with SOCS3. CC Interacts (via the phosphorylated Tyr-1175, Tyr-1179, Tyr-1180) with CC SOCS1. Interacts with CAV2 (tyrosine-phosphorylated form); the CC interaction is increased with 'Tyr-27'phosphorylation of CAV2 (By CC similarity). Interacts with ARRB2. Interacts with GRB10; this CC interaction blocks the association between IRS1/IRS2 and INSR, CC significantly reduces insulin-stimulated tyrosine phosphorylation of CC IRS1 and IRS2 and thus decreases insulin signaling (By similarity). CC Interacts with GRB7 (By similarity). Interacts with PDPK1 (By CC similarity). Interacts (via Tyr-1180) with GRB14 (via BPS domain); this CC interaction protects the tyrosines in the activation loop from CC dephosphorylation, but promotes dephosphorylation of Tyr-989, this CC results in decreased interaction with, and phosphorylation of, IRS1 (By CC similarity). Interacts (via subunit alpha) with ENPP1 (via 485-599 AA); CC this interaction blocks autophosphorylation (By similarity). Interacts CC with PTPRE; this interaction is dependent of Tyr-1175, Tyr-1179 and CC Tyr-1180 of the INSR (By similarity). Interacts with STAT5B (via SH2 CC domain) (By similarity). Interacts with PTPRF (By similarity). CC Interacts with the insulin receptor SORL1; this interaction strongly CC increases its surface exposure, hence strengthens insulin signal CC reception (PubMed:27322061). Interacts (tyrosine phosphorylated) with CC CCDC88A/GIV (via SH2-like region); binding requires autophosphorylation CC of the INSR C-terminal region (By similarity). Interacts with GNAI3; CC the interaction is probably mediated by CCDC88A/GIV (By similarity). CC Interacts with LMBRD1 (PubMed:24078630). Interacts (in response to CC insulin stimulation) with NCK1; this interaction may recruit PTPN1 to CC mediate INSR dephosphorylation (By similarity). {ECO:0000250, CC ECO:0000250|UniProtKB:P06213, ECO:0000269|PubMed:24078630, CC ECO:0000269|PubMed:27322061}. CC -!- INTERACTION: CC P15208; P49817: Cav1; NbExp=2; IntAct=EBI-6999015, EBI-1161338; CC P15208; Q60760: Grb10; NbExp=6; IntAct=EBI-6999015, EBI-861810; CC P15208; Q1XH17: Trim72; NbExp=2; IntAct=EBI-6999015, EBI-16034016; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27322061}; CC Single-pass type I membrane protein {ECO:0000305}. Recycling endosome CC membrane {ECO:0000269|PubMed:27322061}. Late endosome CC {ECO:0000269|PubMed:27322061}. Lysosome {ECO:0000305|PubMed:27322061}. CC Note=Binding of insulin to INSR induces internalization and lysosomal CC degradation of the receptor, a means for down-regulating this signaling CC pathway after stimulation. In the presence of SORL1, internalized INSR CC molecules are redirected back to the cell surface, thereby preventing CC their lysosomal catabolism and strengthening insulin signal reception. CC {ECO:0000269|PubMed:27322061}. CC -!- DOMAIN: The tetrameric insulin receptor binds insulin via non-identical CC regions from two alpha chains, primarily via the C-terminal region of CC the first INSR alpha chain. Residues from the leucine-rich N-terminus CC of the other INSR alpha chain also contribute to this insulin binding CC site. A secondary insulin-binding site is formed by residues at the CC junction of fibronectin type-III domain 1 and 2 (By similarity). CC {ECO:0000250}. CC -!- PTM: Autophosphorylated on tyrosine residues in response to insulin (By CC similarity). Phosphorylation of Tyr-989 is required for IRS1-, SHC1-, CC and STAT5B-binding (By similarity). Dephosphorylated by PTPRE on Tyr- CC 989, Tyr-1175, Tyr-1179 and Tyr-1180 residues (By similarity). CC Dephosphorylated by PTPRF and PTPN1 (By similarity). Dephosphorylated CC by PTPN2 and Ptprv; down-regulates insulin-induced signaling CC (PubMed:12612081, PubMed:20655470). {ECO:0000250, CC ECO:0000269|PubMed:12612081, ECO:0000269|PubMed:20655470}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE- CC ProRule:PRU00159}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J05149; AAA39318.1; -; mRNA. DR EMBL; AC168068; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M28869; AAA39319.1; -; Genomic_DNA. DR CCDS; CCDS22059.1; -. DR PIR; A34157; A34157. DR RefSeq; NP_034698.2; NM_010568.3. DR PDB; 1LK2; X-ray; 1.35 A; P=423-430. DR PDB; 7SL1; EM; 3.40 A; A/B=1-1372. DR PDB; 7SL2; EM; 3.60 A; A/B=1-1372. DR PDB; 7SL3; EM; 3.40 A; A/B=1-1372. DR PDB; 7SL4; EM; 5.00 A; A/B=1-1372. DR PDB; 7SL6; EM; 3.70 A; A/B=1-1372. DR PDB; 7SL7; EM; 3.10 A; A/B=1-1372. DR PDB; 7STH; EM; 3.50 A; A/B=1-1372. DR PDB; 7STI; EM; 4.90 A; A/B=1-1372. DR PDB; 7STJ; EM; 4.40 A; A/B=1-1372. DR PDB; 7STK; EM; 4.00 A; A/B=1-1372. DR PDB; 8DTL; EM; 5.40 A; A/B=28-1372. DR PDB; 8DTM; EM; 3.50 A; A/B=28-1372. DR PDB; 8EYX; EM; 4.50 A; A/B=28-1372. DR PDB; 8EYY; EM; 4.90 A; A/B=28-1372. DR PDB; 8EZ0; EM; 3.70 A; A/B=28-1372. DR PDBsum; 1LK2; -. DR PDBsum; 7SL1; -. DR PDBsum; 7SL2; -. DR PDBsum; 7SL3; -. DR PDBsum; 7SL4; -. DR PDBsum; 7SL6; -. DR PDBsum; 7SL7; -. DR PDBsum; 7STH; -. DR PDBsum; 7STI; -. DR PDBsum; 7STJ; -. DR PDBsum; 7STK; -. DR PDBsum; 8DTL; -. DR PDBsum; 8DTM; -. DR PDBsum; 8EYX; -. DR PDBsum; 8EYY; -. DR PDBsum; 8EZ0; -. DR AlphaFoldDB; P15208; -. DR BMRB; P15208; -. DR EMDB; EMD-25188; -. DR EMDB; EMD-25189; -. DR EMDB; EMD-25190; -. DR EMDB; EMD-25191; -. DR EMDB; EMD-25192; -. DR EMDB; EMD-25193; -. DR EMDB; EMD-25428; -. DR EMDB; EMD-25429; -. DR EMDB; EMD-25430; -. DR EMDB; EMD-25431; -. DR EMDB; EMD-27704; -. DR EMDB; EMD-27705; -. DR EMDB; EMD-28723; -. DR EMDB; EMD-28724; -. DR EMDB; EMD-28725; -. DR SMR; P15208; -. DR BioGRID; 200774; 29. DR CORUM; P15208; -. DR DIP; DIP-41452N; -. DR IntAct; P15208; 21. DR MINT; P15208; -. DR STRING; 10090.ENSMUSP00000088837; -. DR BindingDB; P15208; -. DR ChEMBL; CHEMBL3187; -. DR CarbonylDB; P15208; -. DR GlyConnect; 2393; 7 N-Linked glycans (4 sites). DR GlyCosmos; P15208; 18 sites, 7 glycans. DR GlyGen; P15208; 19 sites, 7 N-linked glycans (4 sites), 1 O-linked glycan (1 site). DR iPTMnet; P15208; -. DR PhosphoSitePlus; P15208; -. DR jPOST; P15208; -. DR MaxQB; P15208; -. DR PaxDb; 10090-ENSMUSP00000088837; -. DR PeptideAtlas; P15208; -. DR ProteomicsDB; 267252; -. DR Pumba; P15208; -. DR Antibodypedia; 3403; 2541 antibodies from 53 providers. DR DNASU; 16337; -. DR Ensembl; ENSMUST00000091291.5; ENSMUSP00000088837.5; ENSMUSG00000005534.11. DR GeneID; 16337; -. DR KEGG; mmu:16337; -. DR UCSC; uc009krc.2; mouse. DR AGR; MGI:96575; -. DR CTD; 3643; -. DR MGI; MGI:96575; Insr. DR VEuPathDB; HostDB:ENSMUSG00000005534; -. DR eggNOG; KOG4258; Eukaryota. DR GeneTree; ENSGT00940000155404; -. DR HOGENOM; CLU_000288_166_0_1; -. DR InParanoid; P15208; -. DR OMA; VCITRRD; -. DR OrthoDB; 1614410at2759; -. DR PhylomeDB; P15208; -. DR TreeFam; TF351636; -. DR BRENDA; 2.7.10.1; 3474. DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling. DR Reactome; R-MMU-74713; IRS activation. DR Reactome; R-MMU-74749; Signal attenuation. DR Reactome; R-MMU-74751; Insulin receptor signalling cascade. DR Reactome; R-MMU-74752; Signaling by Insulin receptor. DR Reactome; R-MMU-77387; Insulin receptor recycling. DR BioGRID-ORCS; 16337; 3 hits in 79 CRISPR screens. DR ChiTaRS; Insr; mouse. DR EvolutionaryTrace; P15208; -. DR PRO; PR:P15208; -. DR Proteomes; UP000000589; Chromosome 8. DR RNAct; P15208; Protein. DR Bgee; ENSMUSG00000005534; Expressed in pigmented layer of retina and 217 other cell types or tissues. DR ExpressionAtlas; P15208; baseline and differential. DR GO; GO:0030424; C:axon; IBA:GO_Central. DR GO; GO:0005901; C:caveola; IDA:MGI. DR GO; GO:0032590; C:dendrite membrane; ISO:MGI. DR GO; GO:0005768; C:endosome; ISO:MGI. DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI. DR GO; GO:0005899; C:insulin receptor complex; ISO:MGI. DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IDA:BHF-UCL. DR GO; GO:0043025; C:neuronal cell body; ISO:MGI. DR GO; GO:0032809; C:neuronal cell body membrane; ISO:MGI. DR GO; GO:0005635; C:nuclear envelope; IEA:Ensembl. DR GO; GO:0031981; C:nuclear lumen; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0043235; C:receptor complex; ISO:MGI. DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0060417; C:yolk; ISO:MGI. DR GO; GO:0043423; F:3-phosphoinositide-dependent protein kinase binding; ISO:MGI. DR GO; GO:0001540; F:amyloid-beta binding; ISO:MGI. DR GO; GO:0005524; F:ATP binding; ISO:MGI. DR GO; GO:0038024; F:cargo receptor activity; ISO:MGI. DR GO; GO:0005525; F:GTP binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0043559; F:insulin binding; ISS:UniProtKB. DR GO; GO:0005009; F:insulin receptor activity; IDA:MGI. DR GO; GO:0043560; F:insulin receptor substrate binding; ISS:UniProtKB. DR GO; GO:0031994; F:insulin-like growth factor I binding; ISO:MGI. DR GO; GO:0031995; F:insulin-like growth factor II binding; ISO:MGI. DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISO:MGI. DR GO; GO:0031405; F:lipoic acid binding; ISO:MGI. DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISS:UniProtKB. DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI. DR GO; GO:0004672; F:protein kinase activity; ISO:MGI. DR GO; GO:0019901; F:protein kinase binding; ISO:MGI. DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI. DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0051425; F:PTB domain binding; ISS:UniProtKB. DR GO; GO:0005198; F:structural molecule activity; ISO:MGI. DR GO; GO:0030325; P:adrenal gland development; IGI:CACAO. DR GO; GO:0097242; P:amyloid-beta clearance; ISO:MGI. DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI. DR GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:MGI. DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI. DR GO; GO:0097062; P:dendritic spine maintenance; ISO:MGI. DR GO; GO:0008544; P:epidermis development; IMP:MGI. DR GO; GO:0031017; P:exocrine pancreas development; IMP:MGI. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI. DR GO; GO:0042593; P:glucose homeostasis; ISO:MGI. DR GO; GO:0003007; P:heart morphogenesis; ISO:MGI. DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:MGI. DR GO; GO:0008584; P:male gonad development; IGI:CACAO. DR GO; GO:0030238; P:male sex determination; IMP:MGI. DR GO; GO:2000252; P:negative regulation of feeding behavior; ISO:MGI. DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI. DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI. DR GO; GO:1990535; P:neuron projection maintenance; ISO:MGI. DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI. DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI. DR GO; GO:0048639; P:positive regulation of developmental growth; ISO:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IGI:CACAO. DR GO; GO:0046326; P:positive regulation of glucose import; ISO:MGI. DR GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IMP:BHF-UCL. DR GO; GO:0045821; P:positive regulation of glycolytic process; ISO:MGI. DR GO; GO:0010560; P:positive regulation of glycoprotein biosynthetic process; ISO:MGI. DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI. DR GO; GO:0051446; P:positive regulation of meiotic cell cycle; IGI:CACAO. DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IMP:MGI. DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IMP:BHF-UCL. DR GO; GO:0042327; P:positive regulation of phosphorylation; ISO:MGI. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI. DR GO; GO:0043243; P:positive regulation of protein-containing complex disassembly; ISO:MGI. DR GO; GO:0002092; P:positive regulation of receptor internalization; ISO:MGI. DR GO; GO:0060267; P:positive regulation of respiratory burst; ISO:MGI. DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB. DR GO; GO:0031623; P:receptor internalization; IDA:MGI. DR GO; GO:0006898; P:receptor-mediated endocytosis; ISO:MGI. DR GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:0045995; P:regulation of embryonic development; ISO:MGI. DR GO; GO:2000194; P:regulation of female gonad development; IGI:CACAO. DR GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; ISO:MGI. DR GO; GO:0031667; P:response to nutrient levels; ISO:MGI. DR GO; GO:0034612; P:response to tumor necrosis factor; ISO:MGI. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central. DR GO; GO:0046718; P:viral entry into host cell; ISO:MGI. DR CDD; cd00063; FN3; 2. DR CDD; cd00064; FU; 1. DR CDD; cd05061; PTKc_InsR; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 3. DR Gene3D; 3.80.20.20; Receptor L-domain; 2. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR006211; Furin-like_Cys-rich_dom. DR InterPro; IPR006212; Furin_repeat. DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR040969; Insulin_TMD. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR000494; Rcpt_L-dom. DR InterPro; IPR036941; Rcpt_L-dom_sf. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR008266; Tyr_kinase_AS. DR InterPro; IPR020635; Tyr_kinase_cat_dom. DR InterPro; IPR016246; Tyr_kinase_insulin-like_rcpt. DR InterPro; IPR002011; Tyr_kinase_rcpt_2_CS. DR PANTHER; PTHR24416:SF535; INSULIN RECEPTOR; 1. DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1. DR Pfam; PF00041; fn3; 1. DR Pfam; PF00757; Furin-like; 1. DR Pfam; PF17870; Insulin_TMD; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR Pfam; PF01030; Recep_L_domain; 2. DR PIRSF; PIRSF000620; Insulin_receptor; 1. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00060; FN3; 3. DR SMART; SM00261; FU; 1. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF49265; Fibronectin type III; 3. DR SUPFAM; SSF57184; Growth factor receptor domain; 1. DR SUPFAM; SSF52058; L domain-like; 2. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50853; FN3; 3. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1. DR Genevisible; P15208; MM. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell membrane; KW Cleavage on pair of basic residues; Disulfide bond; Endosome; Glycoprotein; KW Kinase; Lysosome; Membrane; Nucleotide-binding; Phosphoprotein; Receptor; KW Reference proteome; Repeat; Signal; Transferase; Transmembrane; KW Transmembrane helix; Tyrosine-protein kinase. FT SIGNAL 1..27 FT CHAIN 28..748 FT /note="Insulin receptor subunit alpha" FT /id="PRO_0000016693" FT CHAIN 753..1372 FT /note="Insulin receptor subunit beta" FT /id="PRO_0000016695" FT TOPO_DOM 28..748 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TOPO_DOM 753..946 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 947..967 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 968..1372 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT DOMAIN 626..728 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 744..838 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 843..937 FT /note="Fibronectin type-III 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1013..1288 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 688..709 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 735..743 FT /note="Insulin-binding" FT /evidence="ECO:0000250" FT REGION 986..989 FT /note="Important for interaction with IRS1, SHC1 and FT STAT5B" FT /evidence="ECO:0000250" FT REGION 1349..1372 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1351..1354 FT /note="PIK3R1 binding" FT /evidence="ECO:0000250" FT ACT_SITE 1149 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250" FT BINDING 1023 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 1047 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 1094..1100 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 1153..1154 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 1167 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT SITE 66 FT /note="Insulin-binding" FT /evidence="ECO:0000250" FT MOD_RES 400 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P06213" FT MOD_RES 401 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P06213" FT MOD_RES 407 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P06213" FT MOD_RES 989 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P06213" FT MOD_RES 1175 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P06213" FT MOD_RES 1179 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:20655470" FT MOD_RES 1180 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:20655470" FT MOD_RES 1345 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P06213" FT MOD_RES 1351 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P06213" FT CARBOHYD 43 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 52 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 105 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 138 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 242 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 282 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 322 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 364 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 424 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 445 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973, FT ECO:0000269|PubMed:19656770" FT CARBOHYD 541 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 635 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 653 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 700 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 759 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 772 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 910 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 923 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 35..53 FT /evidence="ECO:0000250" FT DISULFID 153..182 FT /evidence="ECO:0000250" FT DISULFID 186..209 FT /evidence="ECO:0000250" FT DISULFID 196..215 FT /evidence="ECO:0000250" FT DISULFID 219..228 FT /evidence="ECO:0000250" FT DISULFID 223..234 FT /evidence="ECO:0000250" FT DISULFID 235..243 FT /evidence="ECO:0000250" FT DISULFID 239..252 FT /evidence="ECO:0000250" FT DISULFID 255..264 FT /evidence="ECO:0000250" FT DISULFID 268..280 FT /evidence="ECO:0000250" FT DISULFID 286..311 FT /evidence="ECO:0000250" FT DISULFID 293..301 FT /evidence="ECO:0000250" FT DISULFID 315..328 FT /evidence="ECO:0000250" FT DISULFID 331..335 FT /evidence="ECO:0000250" FT DISULFID 339..360 FT /evidence="ECO:0000250" FT DISULFID 462..495 FT /evidence="ECO:0000250" FT DISULFID 551 FT /note="Interchain" FT /evidence="ECO:0000250" FT DISULFID 676..889 FT /evidence="ECO:0000250" FT DISULFID 815..824 FT /evidence="ECO:0000250" FT MUTAGEN 989 FT /note="Y->F: Abolishes interaction with IRS1 but not with FT IRS2." FT /evidence="ECO:0000269|PubMed:10207032, FT ECO:0000269|PubMed:8626379" FT CONFLICT 1089 FT /note="T -> M (in Ref. 1; AAA39318)" FT /evidence="ECO:0000305" FT STRAND 38..44 FT /evidence="ECO:0007829|PDB:7SL7" FT HELIX 45..50 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 53..58 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 60..65 FT /evidence="ECO:0007829|PDB:7SL7" FT HELIX 70..72 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 83..86 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 88..93 FT /evidence="ECO:0007829|PDB:7SL7" FT TURN 100..102 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 115..117 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 119..124 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 144..149 FT /evidence="ECO:0007829|PDB:7SL7" FT HELIX 160..163 FT /evidence="ECO:0007829|PDB:7SL7" FT HELIX 167..169 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 171..175 FT /evidence="ECO:0007829|PDB:7SL7" FT HELIX 176..179 FT /evidence="ECO:0007829|PDB:7SL7" FT TURN 187..192 FT /evidence="ECO:0007829|PDB:7SL1" FT STRAND 198..207 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 209..213 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 223..226 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 230..232 FT /evidence="ECO:0007829|PDB:7SL1" FT STRAND 239..247 FT /evidence="ECO:0007829|PDB:7SL7" FT HELIX 249..251 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 252..260 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 263..267 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 272..275 FT /evidence="ECO:0007829|PDB:7SL7" FT TURN 276..278 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 279..282 FT /evidence="ECO:0007829|PDB:7SL7" FT HELIX 283..294 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 305..307 FT /evidence="ECO:0007829|PDB:7SL1" FT STRAND 308..314 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 319..321 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 323..325 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 327..330 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 332..334 FT /evidence="ECO:0007829|PDB:7SL1" FT HELIX 342..344 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 346..348 FT /evidence="ECO:0007829|PDB:7SL7" FT HELIX 351..355 FT /evidence="ECO:0007829|PDB:7SL7" FT TURN 356..359 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 361..365 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 367..369 FT /evidence="ECO:0007829|PDB:7SL7" FT HELIX 378..384 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 385..387 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 390..393 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 395..399 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 404..406 FT /evidence="ECO:0007829|PDB:7SL7" FT TURN 422..424 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 425..430 FT /evidence="ECO:0007829|PDB:7SL7" FT TURN 441..443 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 452..457 FT /evidence="ECO:0007829|PDB:7SL7" FT HELIX 463..473 FT /evidence="ECO:0007829|PDB:7SL7" FT HELIX 476..478 FT /evidence="ECO:0007829|PDB:7SL7" FT TURN 481..483 FT /evidence="ECO:0007829|PDB:7SL1" FT STRAND 486..490 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 498..500 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 502..507 FT /evidence="ECO:0007829|PDB:7SL1" FT STRAND 512..514 FT /evidence="ECO:0007829|PDB:7SL7" FT HELIX 524..526 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 527..536 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 538..540 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 557..561 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 579..582 FT /evidence="ECO:0007829|PDB:7SL1" FT STRAND 590..599 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 603..605 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 610..612 FT /evidence="ECO:0007829|PDB:7SL1" FT STRAND 615..618 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 628..633 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 636..638 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 640..645 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 656..663 FT /evidence="ECO:0007829|PDB:7SL7" FT HELIX 668..672 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 677..679 FT /evidence="ECO:0007829|PDB:7SL1" FT HELIX 718..742 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 788..793 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 795..799 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 807..816 FT /evidence="ECO:0007829|PDB:7SL7" FT TURN 819..821 FT /evidence="ECO:0007829|PDB:7SL1" FT STRAND 828..833 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 838..842 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 848..851 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 853..855 FT /evidence="ECO:0007829|PDB:7SL1" FT STRAND 857..860 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 871..880 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 886..891 FT /evidence="ECO:0007829|PDB:7SL7" FT HELIX 892..898 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 900..903 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 908..921 FT /evidence="ECO:0007829|PDB:7SL7" FT STRAND 930..933 FT /evidence="ECO:0007829|PDB:7SL1" SQ SEQUENCE 1372 AA; 155610 MW; B0FA7DBD2AD4646A CRC64; MGFGRGCETT AVPLLVAVAA LLVGTAGHLY PGEVCPGMDI RNNLTRLHEL ENCSVIEGHL QILLMFKTRP EDFRDLSFPK LIMITDYLLL FRVYGLESLK DLFPNLTVIR GSRLFFNYAL VIFEMVHLKE LGLYNLMNIT RGSVRIEKNN ELCYLATIDW SRILDSVEDN YIVLNKDDNE ECGDVCPGTA KGKTNCPATV INGQFVERCW THSHCQKVCP TICKSHGCTA EGLCCHKECL GNCSEPDDPT KCVACRNFYL DGQCVETCPP PYYHFQDWRC VNFSFCQDLH FKCRNSRKPG CHQYVIHNNK CIPECPSGYT MNSSNLMCTP CLGPCPKVCQ ILEGEKTIDS VTSAQELRGC TVINGSLIIN IRGGNNLAAE LEANLGLIEE ISGFLKIRRS YALVSLSFFR KLHLIRGETL EIGNYSFYAL DNQNLRQLWD WSKHNLTITQ GKLFFHYNPK LCLSEIHKME EVSGTKGRQE RNDIALKTNG DQASCENELL KFSFIRTSFD KILLRWEPYW PPDFRDLLGF MLFYKEAPYQ NVTEFDGQDA CGSNSWTVVD IDPPQRSNDP KSQTPSHPGW LMRGLKPWTQ YAIFVKTLVT FSDERRTYGA KSDIIYVQTD ATNPSVPLDP ISVSNSSSQI ILKWKPPSDP NGNITHYLVY WERQAEDSEL FELDYCLKGL KLPSRTWSPP FESDDSQKHN QSEYDDSASE CCSCPKTDSQ ILKELEESSF RKTFEDYLHN VVFVPRPSRK RRSLEEVGNV TATTLTLPDF PNVSSTIVPT SQEEHRPFEK VVNKESLVIS GLRHFTGYRI ELQACNQDSP DERCSVAAYV SARTMPEAKA DDIVGPVTHE IFENNVVHLM WQEPKEPNGL IVLYEVSYRR YGDEELHLCV SRKHFALERG CRLRGLSPGN YSVRVRATSL AGNGSWTEPT YFYVTDYLDV PSNIAKIIIG PLIFVFLFSV VIGSIYLFLR KRQPDGPMGP LYASSNPEYL SASDVFPSSV YVPDEWEVPR EKITLLRELG QGSFGMVYEG NAKDIIKGEA ETRVAVKTVN ESASLRERIE FLNEASVMKG FTCHHVVRLL GVVSKGQPTL VVMELMAHGD LKSHLRSLRP DAENNPGRPP PTLQEMIQMT AEIADGMAYL NAKKFVHRDL AARNCMVAHD FTVKIGDFGM TRDIYETDYY RKGGKGLLPV RWMSPESLKD GVFTASSDMW SFGVVLWEIT SLAEQPYQGL SNEQVLKFVM DGGYLDPPDN CPERLTDLMR MCWQFNPKMR PTFLEIVNLL KDDLHPSFPE VSFFYSEENK APESEELEME FEDMENVPLD RSSHCQREEA GGREGGSSLS IKRTYDEHIP YTHMNGGKKN GRVLTLPRSN PS //